Besides our previous experimental discovery （Zhao Y R, et al. 2015 Langmuir, 31, 12975） that acetonitrile （ACN） can tune the morphological features of nanostructures self-assembled by short peptides KIIIIK （KI4K...Besides our previous experimental discovery （Zhao Y R, et al. 2015 Langmuir, 31, 12975） that acetonitrile （ACN） can tune the morphological features of nanostructures self-assembled by short peptides KIIIIK （KI4K） in aqueous solution, further experiments reported in this work demonstrate that ACN can also tune the mass of the self-assembled nanostructures. To understand the microscopic mechanism how ACN molecules interfere peptide self-assembly process, we conducted a series of molecular dynamics simulations on a monomer, a cross-β sheet structure, and a proto-fibril of KI4K in pure water, pure ACN, and ACN-water mixtures, respectively. The simulation results indicate that ACN enhances the intra-sheet interaction dominated by the hydrogen bonding （H-bonding） interactions between peptide backbones, but weakens the inter-sheet interaction dominated by the interactions between hydrophobic side chains. Through analyzing the correlations between different groups of solvent and peptides and the solvent behaviors around the proto-fibril, we have found that both the polar and nonpolar groups of ACN play significant roles in causing the opposite effects on intermolecular interactions among peptides. The weaker correlation of the polar group of ACN than water molecule with the peptide backbone enhances H-bonding interactions between peptides in the proto-fibril. The stronger correlation of the nonpolar group of ACN than water molecule with the peptide side chain leads to the accumulation of ACN molecules around the proto-fibril with their hydrophilic groups exposed to water, which in turn allows more water molecules close to the proto-fibril surface and weakens the inter-sheet interactions. The two opposite effects caused by ACN form a microscopic mechanism clearly explaining our experimental observations.展开更多
Under appropriate physicochemical conditions, short peptide fragments and their synthetic mimics have been shown to form elongated cross-fl nanostructures through self-assembly. The self-assembly process and the resul...Under appropriate physicochemical conditions, short peptide fragments and their synthetic mimics have been shown to form elongated cross-fl nanostructures through self-assembly. The self-assembly process and the resultant peptide nanos- tructures are not only related to neurodegenerative diseases but also provide inspiration for the development of novel bionanomaterials. Both experimental and theoretical studies on peptide self-assembly have shown that the self-assembly process spans multiple time and length scales and is hierarchical, β-sheet self-assembly consists of three sub-processes from the microscopic to the mesoscopic level： β-sheet locking, lateral stacking, and morphological transformation. De- tailed atomistic simulation studies have provided insight into the early stages of peptide nanostructure formation and the interplay between different non-covalent interactions at the microscopic level. This review gives a brief introduction of the hierarchical peptide self-assembly process and focuses on the roles of various non-covalent interactions in the sub-processes based on recent simulation, experimental, and theoretical studies.展开更多
In order to study the biocompatibility of self-assembled FGL peptide nanofibers scaffold with neural stem cells （NSCs）, FGL pepitide-amphiphile （FGL-PA） was synthesized by solid-phase peptide synthesis technique. ...In order to study the biocompatibility of self-assembled FGL peptide nanofibers scaffold with neural stem cells （NSCs）, FGL pepitide-amphiphile （FGL-PA） was synthesized by solid-phase peptide synthesis technique. The diluted hydrochloric acid was added into FGL-PA solution to reduce the PH value and accordingly induce self-assembly. The morphological features of the assembled material were studied by transmission electron microscope. NSCs were cultured and added with self-assembled FGL-PA. CCK-8 kit was used to test its effect on the proliferation of NSCs. The differentiation of NSCs was also tested after FGL-PA assembled material added. The experimental results showed that FGL-PA could be self-assembled to form a hydrogel. TEM analysis showed the self-assembled hydrogel was nanofibers with diameter of 10-20 nm and length of hundreds nanometers. FGL-PA with concentrations of 50,100, or 200 mg/L could promote the proliferation of NSCs, and absorbance of them was increased （P〈0.05）. The rate of neurons differentiated from NSCs was improved greatly by FGL-PA assembled material compared with control （P〈0.05）. The findings suggested that FGL-PA could self-assemble to nanofiber hydrogel, which had good biocompatibility with NSCs.展开更多
Peptide GAV-9 is derived from 3 different disease related proteins. The self-assembly of GAV-9 in a water nanofilm attracted much attention recently. We studied how the temperature factor influenced the peptide selfas...Peptide GAV-9 is derived from 3 different disease related proteins. The self-assembly of GAV-9 in a water nanofilm attracted much attention recently. We studied how the temperature factor influenced the peptide selfassembly in a water nanofilm and found interesting phenomena: 1) the higher the temperature, the faster the nanofilaments grow; 2) the GAV-9 peptide formed double monolayers in a water nanofilm at 60℃, which further supports the hypothesis that the water nanofilm could change the hydrophobicity of mica. We believe these results can help not only the microcontact printing of amyloid peptides, but also a better understanding on how temperature controls the properties of water nanofilm.展开更多
Peptide-based assemblies have gained increasing attention in different areas of nanotechnology,drug delivery and molecular biology.Among these,non-natural β-peptide scaffolds are particularly promising,as their progr...Peptide-based assemblies have gained increasing attention in different areas of nanotechnology,drug delivery and molecular biology.Among these,non-natural β-peptide scaffolds are particularly promising,as their programmable and diverse secondary structures,high metabolic stability and strong self-association propensity can be easily exploited to create variable constructs.We have recently demonstrated that heterochiral,acyclic β^(3)-peptides assembled into striped lamellar nanostructures that induced antibacterial activity.The process of this assembly formation could be exploited in diverse areas,however identifying oligomerisation stages,and more importantly,controlling the spontaneous process at different levels is still lacking.In this study,a set of analogues heterochiral hexameric β^(3)-peptide sequences was investigated to understand how systematic,small variations of the sequences,such as single point mutation or N-terminal chemical modification,can influence the resulting assemblies and allow the control of formed morphologies.TEM and cryo-EM combined with molecular dynamics simulation enabled the identification and differentiation of morphological stages throughout the entire multi-step process.Depending on the position of the sequence modifications,the self-assembled structures formed small oligomers,individual protofibrils,extended,flat lamellae,bundles and macroscopic clusters.These results outline how the self-assembly process of short heterochiral β-peptides can be qualitatively fine-tuned by sequence modifications,which contribute to understanding the general peptide assembly processes for their fibrillar morphologies.展开更多
The simultaneous detection of carcinoembryonic antigen(CEA)and microRNA-21(miR-21)is of significant clinical importance for cancer diagnosis,prognosis evaluation,and therapy monitoring.In this study,we developed a nov...The simultaneous detection of carcinoembryonic antigen(CEA)and microRNA-21(miR-21)is of significant clinical importance for cancer diagnosis,prognosis evaluation,and therapy monitoring.In this study,we developed a novel electrochemical biosensor utilizing a peptide-self-assembly-engineered signal amplification(PSA-e-SA)nanoarchitectonic strategy to achieve ultrasensitive and simultaneous quantification of these two critical biomarkers.By designing amphiphilic peptides(C_(16)-MB-AptamerCEA and C_(16)-Fc-ssDNA2)as multifunctional probes,the system exploits their dual roles in target recognition and signal amplification.These peptides self-assemble into nanostructures under mild conditions,facilitating enhanced loading of electroactive molecules such as methylene blue(MB)and ferrocene(Fc),thereby significantly amplifying the electrochemical signal.The biosensor achieved detection limits of 0.788 pM for CEA and 0.0357 nM for miR-21,demonstrating remarkable sensitivity enhancements of 18-fold and 3.8-fold compared to unamplified approaches.As a proof-of-concept study,further experiments underscored the excellent reproducibility and stability of the strategy while also demonstrating its applicability when tested with simulated serum samples.Thus,this work not only presents a valuable assay tool for early cancer diagnosis and biomarker analysis but also indicates that this signal amplification strategy based on peptide self-assembly engineering can be extended to detect other disease-related biomarkers,propelling the development of clinical applications for multifunctional biosensors.展开更多
Developing novel building blocks with predictable side-chain orientations and minimal intramolecular interactions is essential for peptide-based self-assembling materials.Traditional structures likeα-helices andβ-sh...Developing novel building blocks with predictable side-chain orientations and minimal intramolecular interactions is essential for peptide-based self-assembling materials.Traditional structures likeα-helices andβ-sheets rely on such interactions for stability,limiting control over exposed interacting moieties.Here,we reported a novel,frame-like peptide scaffold that maintains exceptional stability without intramolecular interactions.This structure exposes its backbone and orients side chains for hierarchical self-assembly into micron-scale cubes.By introducing mutations at specific sites,we controlled packing orientations,offering new options for tunable self-assembly.Our scaffold provides a versatile platform for designing advanced peptide materials,with applications in nanotechnology and biomaterials.展开更多
Biopolymer-driven supramolecular chirality in aqueous media has gained significant advancements in hierarchical chiral nanostructures.However,researches on the aqueous circularly polarized luminescence(CPL)induced by ...Biopolymer-driven supramolecular chirality in aqueous media has gained significant advancements in hierarchical chiral nanostructures.However,researches on the aqueous circularly polarized luminescence(CPL)induced by supramolecular selfassembly and its mechanism have been rarely reported.Herein,we explore the hierarchical chirality transfer in self-assembled fluorescent homopolypeptide systems showing aqueous CPL,and unveil anα-helix-dominated CPL regulation mechanism.A relationship is established between molecular structure(degree of polymerization,DP),supramolecular assembly(self-assembly temperature,T_(SA)),and resulting CPL properties.The stabilization for the homopolypeptideα-helix by increasing DP and decreasing T_(SA) enables efficient chirality transfer from the polypeptide backbone to its terminal chromophore,thereby improving CPL properties.Our work elucidates the critical role ofα-helix control in aqueous CPL systems,providing insights for designing biocompatible and tunable CPL-active nanomaterials.展开更多
CONSPECTUS:Controlling self-assembled peptide nanostructures has emerged as a significant area of research,offering versatile tools for developing functional materials for various applications.This Account emphasizes ...CONSPECTUS:Controlling self-assembled peptide nanostructures has emerged as a significant area of research,offering versatile tools for developing functional materials for various applications.This Account emphasizes the essential role of noncovalent interactions,particularly in peptide-based materials.Key forces,such as aromatic stacking and hydrogen bonding,are crucial for promoting molecular aggregation and stabilizing supramolecular structures.Numerous studies demonstrate how these interactions influence the phase transitions and the morphology of self-assembled structures.Recent advances in computational methodologies,including molecular dynamics simulations and machine learning,have significantly enhanced our understanding of self-assembly processes.These tools enable researchers to predict how molecular properties,such as hydrophobicity,charge distribution,and aromaticity,affect assembly behavior.Simulations uncover the energetic landscapes governing peptide aggregation,providing insights into the kinetic pathways and thermodynamic stabilities.Meanwhile,machine learning facilitates the rapid screening of peptide libraries,identifying sequences with optimal self-assembly characteristics,and accelerating material design with tailored functionalities.Beyond their structural and physicochemical properties,self-assembled peptide nanostructures hold immense potential in biological applications due to their versatility and biocompatibility.By manipulating molecular interactions,researchers have engineered responsive systems that interact with cellular environments to elicit specific biological responses.These peptide nanostructures can mimic extracellular matrices,facilitating cell adhesion,proliferation,and differentiation.They also show promise in modulating immune responses,recruiting immune cells,and regulating signaling pathways,making them valuable tools in immunotherapy and regenerative medicine.Moreover,their ability to disrupt bacterial membranes positions them as innovative alternatives to conventional antibiotics,addressing the urgent need for solutions to antimicrobial resistance.Despite its promise,peptide self-assembly faces several challenges.The assembly process is highly sensitive to environmental conditions,such as pH,temperature,and ionic strength,leading to variability in the morphology and properties.Furthermore,peptide aggregation can result in heterogeneous and poorly defined assemblies,complicating the reproducibility and scalability.Designing peptides with predictable self-assembly behavior remains a significant hurdle.Looking ahead,integrating computational predictions with experimental validations will be crucial in discovering novel peptide sequences with tailored self-assembly properties.Machine learning,combined with high-throughput screening techniques,will enable the rapid identification of optimal peptide sequences.In situ characterization tools,such as cryoelectron microscopy and advanced spectroscopy,will provide deeper insights into assembly mechanisms,aiding the rational design of peptide materials.As research progresses,the dynamic and reversible nature of noncovalent interactions can be leveraged to create adaptive responsive to environmental stimuli.Self-assembled peptide nanostructures are poised for impactful applications in biomedicine including targeted drug delivery,tissue repair,and advanced therapeutic strategies.Ultimately,these nanostructures represent a powerful platform for addressing complex challenges in biomedicine and beyond,paving the way for transformative breakthroughs in science and technology.展开更多
Nanostructures self-assembled by cross-β peptides with ordered structures and advantageous mechanical properties have many potential applications in biomaterials and nanotechnologies. Quantifying the intra-and inter-...Nanostructures self-assembled by cross-β peptides with ordered structures and advantageous mechanical properties have many potential applications in biomaterials and nanotechnologies. Quantifying the intra-and inter-molecular driving forces for peptide self-assembly at the atomistic level is essential for understanding the formation mechanism and nanomechanics of various morphologies of self-assembled peptides. We investigate the thermodynamics of the intra-and inter-sheet structure formations in the self-assembly process of cross-β peptide KⅢIK by means of steered molecular dynamics simulation combined with umbrella sampling. It is found that the mechanical properties of the intra-and inter-sheet structures are highly anisotropic with their intermolecular bond stiffness at the temperature of 300 K being 5.58 N/m and 0.32 N/m, respectively. This mechanical anisotropy comes from the fact that the intra-sheet structure is stabilized by enthalpy but the inter-sheet structure is stabilized by entropy. Moreover, the formation process of KⅢIK intra-sheet structure is cooperatively driven by the van der Waals （VDW） interaction between the hydrophobic side chains and the electrostatic interaction between the hydrophilic backbones, but that of the inter-sheet structure is primarily driven by the VDW interaction between the hydrophobic side chains. Although only peptide KⅢIK is studied, the qualitative conclusions on the formation mechanism should also apply to other cross-β peptides.展开更多
Effective countermeasures against multidrug-resistant nosocomial pathogens,such as carbapenem-resistant Klebsiella pneumoniae and methicillin-resistant Staphylococcus aureus(MRSA),require the development of innovative...Effective countermeasures against multidrug-resistant nosocomial pathogens,such as carbapenem-resistant Klebsiella pneumoniae and methicillin-resistant Staphylococcus aureus(MRSA),require the development of innovative antimicrobial strategies.This study presents a structure-function approach to antimicrobial peptide(AMP)design through the strategic integration of a cationic backbone with a hydrophobic core.This dual-domain architecture enables robust hydrophobic and electrostatic interactions,promoting spontaneous self-assembly and efficient membrane engagement.The lead peptide,Tryptolycin(TRPY),formed stable,monodisperse nanoparticles and demonstrated broad-spectrum bactericidal activity,with minimum inhibitory concentrations≤1μmol/L against multiple strains of MRSA and K.pneumoniae,while exerting minimal cytotoxicity toward mammalian cells.TRPY achieved rapid bacterial elimination,eradicating 99.9%of both planktonic and persister populations within minutes.Mechanistic investigations revealed that TRPY induced membrane permeabilization,promoted reactive oxygen species(ROS)production,and inhibited biofilm formation.In murine infection models,TRPY effectively eradicated established infections,reducing bacterial burden across target organs by 3-to 5-fold without significant cytotoxicity at therapeutic concentrations.Collectively,these findings establish TRPY as a promising therapeutic agent for clinical translation in the treatment of refractory bacterial infections.展开更多
Peptides play important roles in chemistry,medicinal chemistry and life science,due to their high efficiency and specificity,unusual biological and therapeutic properties.As naturally occurring peptides often face wit...Peptides play important roles in chemistry,medicinal chemistry and life science,due to their high efficiency and specificity,unusual biological and therapeutic properties.As naturally occurring peptides often face with their intrinsic limitations including metabolic instability and low membrane permeability,the strategies for synthesizing unnatural amino acids and peptides are explored.Among the methods for modifying amino acids and peptides,chemo-and site-selective approaches are preferred because of the ability to fine-tuning structural features.Recently,transition metal-catalyzed C–H activation has been employed for the functionalization of amino acids and peptides.Through domino C–H activation/annulation,a series of structurally complex and diverse amino acids and peptides is constructed.This review highlights recent advances in the synthesis of unnatural amino acids and peptides via transition metal-catalyzed C–H activation/annulation.展开更多
The escalating global crisis of antibiotic resistance necessitates urgent development of novel antimicrobial agents.In this context,antimicrobial peptides(AMPs)derived from fish emerge as a highly promising strategic ...The escalating global crisis of antibiotic resistance necessitates urgent development of novel antimicrobial agents.In this context,antimicrobial peptides(AMPs)derived from fish emerge as a highly promising strategic resource,owing to their unique structural diversity and the exceptional adaptability and tolerance conferred by evolutionary pressures in aquatic environments.This review systematically synthesizes key advances in fish-derived AMP research.It details their diverse sourcing avenues,encompassing tissues from live fish(e.g.,skin,mucus,gills,intestines)and processing byproducts(e.g.,scales,skins,viscera).The discussion covers efficient isolation,purification,and synthesis strategies,and critically examines their defining feature:unique multi-target synergistic antimicrobial mechanisms(including microbial membrane disruption,intracellular targeting,and immunomodulation),which contribute to a reduced propensity for resistance development.To address inherent limitations of natural AMPs(such as susceptibility to proteolysis and potential toxicity),the review highlights innovative optimization approaches,including computational-aided rational design,amino acid modification,cyclization,and hybrid peptide construction.Furthermore,the review elaborates on their significant application potential across crucial domains:food preservation(inhibiting spoilage organisms,extending shelf-life),sustainable aquaculture(as antibiotic alternatives,enhancing disease resistance,improving water quality),and the development of novel anti-infective therapeutics(particularly against drug-resistant infections).Therefore,this work aims to provide a comprehensive theoretical foundation and innovative strategic insights to foster in-depth research and the sustainable exploitation of this vital strategic biological resource.展开更多
Sustainability and scalability remain critical hurdles for the commercialization of organic solar cells(OSCs).However,addressing both poses challenge.Herein,we introduce a simple yet effective strategy utilizing 3,5-d...Sustainability and scalability remain critical hurdles for the commercialization of organic solar cells(OSCs).However,addressing both poses challenge.Herein,we introduce a simple yet effective strategy utilizing 3,5-dichloropyridine(PDCC)as a solid additive to fine-tune the self-assembly behavior of Y-series non-fullerene acceptors(NFAs)to tackle the upscaling limitations in green-solvent-processed OSCs.PDCC predominantly interacts with Y-series NFAs,facilitating molecular crystallization and thereby driving the self-assembly of Y-series NFAs during film-forming dynamics,leading to more uniform active layers with improved molecular packing and reduced charge recombination.As a result,PDCC-driven self-assembly strategy enables high-performance OSCs with a power conversion efficiency(PCE)of 20.47%.When translated to sustainable fabrication,this strategy significantly boosts the PCE of large-area green-solvent-processed OSC modules(19.3 cm^(2))from 13.87%to 15.79%,ranking it among the best-performing green-solvent-processed large-area OSC modules(>18 cm^(2)).Beyond its impact on PCE enhancement,PDCC serves as a multifunctional additive to improve long-term stability and exhibits strong universality across multiple material systems.This work establishes a promising approach for advancing sustainable and scalable OSCs,paving the way for their commercialization.展开更多
The rapid advancement of flexible electronics technology has placed higher demands on the structural design and performance regulation of elastic materials.Cellulosic elastomers,with their biodegradability,renewabilit...The rapid advancement of flexible electronics technology has placed higher demands on the structural design and performance regulation of elastic materials.Cellulosic elastomers,with their biodegradability,renewability,and tunability,emerge as ideal candidate materials.Entropy-driven self-as sembly promotes the spontaneous formation of ordered structures,serving as a crucial pathway for optimizing cellulose elastomer properties.However,the structure-property relationship between the self-assembled ordered structures of cellulose elastomers and their mechanical and electrical properties remains insufficiently explored.It hinders the expansion of their applications in electronic devices.This paper systematically reviews the structure-property regulation mechanisms of self-assembled cellulosic elastomers from an entropy-driven perspective.It elucidates the application principles and performance optimization strategies for mechanical energy harvesting and self-powered sensing,while also exploring the challenges and prospects for performance enhancement.This work provides a reference for the development of self-assembled cellulosic elastomers in the field of energy devices.展开更多
The antioxidant activity of selenium-containing soybean peptides(SePPs)has been previously demonstrated,despite their limited absorption in the small intestine.This study investigates the antioxidant mechanism of a se...The antioxidant activity of selenium-containing soybean peptides(SePPs)has been previously demonstrated,despite their limited absorption in the small intestine.This study investigates the antioxidant mechanism of a selenium-containing tetrapeptide,Ser-Phe-Gln-SeM(SFQSeM),identified from SePPs,with particular emphasis on its interaction with the intestinal microbiota and its role in modulating host antioxidant defenses.The effects of SFQSeM were evaluated in a D-galactose-induced oxidative stress model and an antibiotictreated mouse model.SFQSeM supplementation significantly reduced the oxidative stress in D-galactosetreated mice.It also promoted the growth of beneficial bacteria and increased the levels of acetate,butyrate and lactate in the intestine(P<0.05).In the antibiotic-treated mouse model,depletion of the intestinal microbiota significantly reduced hepatic glutathione peroxidase(GSH-Px)activity(26.6%)and glutathione peroxidase 1(GPx-1)expression(48.77%)compared to normal mice supplemented with SFQSeM(P<0.05).In contrast to Na_(2)SeO_(3)and selenomethionine,SFQSeM effectively restored the diversity of the intestinal microbiota disrupted by antibiotics.Lactobacillus,Lachnospiraceae_NK4A136_group,and Muribaculaceae were identified as predominant bacteria in the SFQSeM group,and were strongly associated with increased hepatic GSH-Px activity and GPx-1 mRNA expression(P<0.05).In conclusion,intestinal microbiota enhances the antioxidant efficacy of SFQSeM by modulating microbial composition,producing active metabolites,and converting SFQSeM into a bioactive form of selenium.展开更多
Peroxymonosulfate(PMS)-assisted visible-light photocatalytic degradation of organic pollutants using graphitic carbon nitride(g-C_(3)N_(4))presents a promising and environmentally friendly approach.However,pristine g-...Peroxymonosulfate(PMS)-assisted visible-light photocatalytic degradation of organic pollutants using graphitic carbon nitride(g-C_(3)N_(4))presents a promising and environmentally friendly approach.However,pristine g-C_(3)N_(4) suffers from limited visible-light absorption and low charge-carrier mobility.In this study,a phosphorus-doped tubular carbon nitride(5P-TCN)was synthesized via a precursor self-assembly method using phosphoric acid and melamine as raw materials,eliminating the need for organic solvents or templates.The 5P-TCN catalyst demonstrated enhanced visible-light absorption,improved charge transfer capability,and a 5.25-fold increase in specific surface area(31.092 m^(2)/g),which provided abundant active sites to efficiently drive the PMS-assisted photocatalytic reaction.The 5P-TCN/vis/PMS system exhibited exceptional degradation performance for organic pollutants across a broad pH range(3–9),achieving over 92%degradation of Rhodamine B(RhB)within 15 min.Notably,the system retained>98%RhB degradation efficiency after three consecutive operational cycles,demonstrating robust operational stability and reusability.Moreover,key parameters influencing,active radi-cals,degradation pathways,and potential mechanisms for RhB degradation were systematically investigated.This work proposes a green and cost-effective strategy for developing high-efficiency photocatalysts,while demon-strating the exceptional capability of a PMS-assisted photocatalytic system for rapid degradation of RhB.展开更多
Peptide-and drug-protected gold nanoclusters(Au NCs)with atomic precision have attracted research attention in the last few years owing to their ultrasmall size(<2 nm),well-defined structures,tunable photoluminesce...Peptide-and drug-protected gold nanoclusters(Au NCs)with atomic precision have attracted research attention in the last few years owing to their ultrasmall size(<2 nm),well-defined structures,tunable photoluminescence from the visible to near-infrared range,water solubility,and good biocompatibility.These features,combined with low toxicity and efficient renal clearance,make such Au NCs promising candidates for biomedical use,including diagnosis,therapy,and theranostic.The incorporation of peptides or drugs into Au NCs enhances the stability,targeting specificity,cellular uptake,and prolonged circulation,enabling precise modulation of biological responses.Despite notable advances in achieving atomic precision employing complex ligands such as peptides or drugs,the synthetic methods of this new class of NCs remain a challenge.Careful control of molar ratio(Au:peptide/drug),reducing agent,temperature,and reaction time is required,because these factors directly influence the cluster size,optical properties,and in vivo performance.In this review,we highlight different synthetic approaches of atomically precise peptide-and drug-protected Au NCs,emphasizing the role of rational ligand design and reaction conditions,as well as the challenges associated with structural determination.We further discuss the optical and photoluminescence properties of peptide-protected Au NCs-the mostly explored features for biomedical applications.Finally,we conclude by outlining the current challenges,opportunities for scale-up synthesis,and future design perspectives for these emerging nanomaterials.展开更多
Fluorescent probes,with their superior optical properties and labeling versatility,have greatly advanced the visualization of intracellular molecules and subcellular structures.However,poor cytoplasmic delivery,caused...Fluorescent probes,with their superior optical properties and labeling versatility,have greatly advanced the visualization of intracellular molecules and subcellular structures.However,poor cytoplasmic delivery,caused by charge,size,or targeting groups,limits the effective use of many fluorescent probes in live cells.Recently,cell-penetrating peptides(CPPs)have emerged as efficient carriers,offering great potential for the cytoplasmic delivery of fluorescent probes in live cells.This review provides a comprehensive overview of CPPs as vehicles for probe delivery,outlining advances in their development,conjugation chemistries,and intracellular delivery mechanisms.Recent applications in live-cell imaging are highlighted and organized according to major CPP modification strategies,including sequence engineering,cyclization,hybrid design and enhancement by chemical reagents.Finally,the challenges that remain and the future outlook of this rapidly evolvingfield are discussed.展开更多
The blood-brain barrier(BBB)is a major challenge in drug delivery for the treatment of central nervous system diseases.Walnut derived peptide TWLPLPR(TW-7)has been proved to promote neuronal mitochondrial autophagy an...The blood-brain barrier(BBB)is a major challenge in drug delivery for the treatment of central nervous system diseases.Walnut derived peptide TWLPLPR(TW-7)has been proved to promote neuronal mitochondrial autophagy and enhance hippocampal neuronal synaptic plasticity,thereby improving learning and memory abilities in mice.We investigated the internalization mechanism and intracellular transport pathway for the walnut-derived peptide,TW-7,using b End.3 cells in an in vitro BBB model system.TW-7 was taken up by the b End.3 cells in a concentration-,temperature-,and energy-dependent manner;this involved increases in caveolin-1 and caveolin-2 protein expression and phosphorylation and inhibition of P-glycoprotein-mediated efflux.Subcellular localization of TW-7 in b End.3 cells was observed,indicating that the plasma membrane,endoplasmic reticulum,Golgi apparatus,lysosomes,and mitochondria participated in intracellular trafficking and that the peptide escaped from lysosomes over time.Caveolae may be critical for TW-7 uptake by brain microvascular endothelial cells,assisting TW-7 to cross the BBB.The results of this study provide a theoretical basis for the mechanism of active peptide penetrating the BBB,and provide a reference for developing neuroprotective active peptide products.展开更多
基金Project supported by the National Basic Research Program of China(Grant No.2013CB932804)the National Natural Science Foundation of China(Grant Nos.91227115,11421063,11504431,and 21503275)+1 种基金the Fundamental Research Funds for Central Universities of China(Grant No.15CX02025A)the Application Research Foundation for Post-doctoral Scientists of Qingdao City,China(Grant No.T1404096)
文摘Besides our previous experimental discovery （Zhao Y R, et al. 2015 Langmuir, 31, 12975） that acetonitrile （ACN） can tune the morphological features of nanostructures self-assembled by short peptides KIIIIK （KI4K） in aqueous solution, further experiments reported in this work demonstrate that ACN can also tune the mass of the self-assembled nanostructures. To understand the microscopic mechanism how ACN molecules interfere peptide self-assembly process, we conducted a series of molecular dynamics simulations on a monomer, a cross-β sheet structure, and a proto-fibril of KI4K in pure water, pure ACN, and ACN-water mixtures, respectively. The simulation results indicate that ACN enhances the intra-sheet interaction dominated by the hydrogen bonding （H-bonding） interactions between peptide backbones, but weakens the inter-sheet interaction dominated by the interactions between hydrophobic side chains. Through analyzing the correlations between different groups of solvent and peptides and the solvent behaviors around the proto-fibril, we have found that both the polar and nonpolar groups of ACN play significant roles in causing the opposite effects on intermolecular interactions among peptides. The weaker correlation of the polar group of ACN than water molecule with the peptide backbone enhances H-bonding interactions between peptides in the proto-fibril. The stronger correlation of the nonpolar group of ACN than water molecule with the peptide side chain leads to the accumulation of ACN molecules around the proto-fibril with their hydrophilic groups exposed to water, which in turn allows more water molecules close to the proto-fibril surface and weakens the inter-sheet interactions. The two opposite effects caused by ACN form a microscopic mechanism clearly explaining our experimental observations.
基金supported by the National Natural Science Foundation of China(Grant Nos.21373270 and 11504431)the Fundamental Research Funds for Central Universities of China(Grant No.15CX02025A)
文摘Under appropriate physicochemical conditions, short peptide fragments and their synthetic mimics have been shown to form elongated cross-fl nanostructures through self-assembly. The self-assembly process and the resultant peptide nanos- tructures are not only related to neurodegenerative diseases but also provide inspiration for the development of novel bionanomaterials. Both experimental and theoretical studies on peptide self-assembly have shown that the self-assembly process spans multiple time and length scales and is hierarchical, β-sheet self-assembly consists of three sub-processes from the microscopic to the mesoscopic level： β-sheet locking, lateral stacking, and morphological transformation. De- tailed atomistic simulation studies have provided insight into the early stages of peptide nanostructure formation and the interplay between different non-covalent interactions at the microscopic level. This review gives a brief introduction of the hierarchical peptide self-assembly process and focuses on the roles of various non-covalent interactions in the sub-processes based on recent simulation, experimental, and theoretical studies.
基金Funded by the National Natural Science Foundation of China(No.30500511)
文摘In order to study the biocompatibility of self-assembled FGL peptide nanofibers scaffold with neural stem cells （NSCs）, FGL pepitide-amphiphile （FGL-PA） was synthesized by solid-phase peptide synthesis technique. The diluted hydrochloric acid was added into FGL-PA solution to reduce the PH value and accordingly induce self-assembly. The morphological features of the assembled material were studied by transmission electron microscope. NSCs were cultured and added with self-assembled FGL-PA. CCK-8 kit was used to test its effect on the proliferation of NSCs. The differentiation of NSCs was also tested after FGL-PA assembled material added. The experimental results showed that FGL-PA could be self-assembled to form a hydrogel. TEM analysis showed the self-assembled hydrogel was nanofibers with diameter of 10-20 nm and length of hundreds nanometers. FGL-PA with concentrations of 50,100, or 200 mg/L could promote the proliferation of NSCs, and absorbance of them was increased （P〈0.05）. The rate of neurons differentiated from NSCs was improved greatly by FGL-PA assembled material compared with control （P〈0.05）. The findings suggested that FGL-PA could self-assemble to nanofiber hydrogel, which had good biocompatibility with NSCs.
基金Supported by grants from the National Natural Science Foundation of China(Nos.21171086 and 81160213)Inner Mongolia Grassland Talent(No.108-108038)+1 种基金Inner Mongolia Autonomous Region Natural Science Foundation(No.2013MS1121)the Inner Mongolia Agricultural University(Nos.211-109003 and 211-206038)
文摘Peptide GAV-9 is derived from 3 different disease related proteins. The self-assembly of GAV-9 in a water nanofilm attracted much attention recently. We studied how the temperature factor influenced the peptide selfassembly in a water nanofilm and found interesting phenomena: 1) the higher the temperature, the faster the nanofilaments grow; 2) the GAV-9 peptide formed double monolayers in a water nanofilm at 60℃, which further supports the hypothesis that the water nanofilm could change the hydrophobicity of mica. We believe these results can help not only the microcontact printing of amyloid peptides, but also a better understanding on how temperature controls the properties of water nanofilm.
基金funded by the National Research,Development and Inno-vation Office,Hungary(TKP2021-EGA-31,2020-1.1.2-PIACI-KFI-2020-00021,KKP_22 Project no.144180 and FK_23 Project no.146081).Support from Hungarian Research Network(Eötvös Loránd Research Network)grant no.SA-87/2021 and KEP-5/2021 are also acknowledged.Project no.RRF-2.3.1-21-2022-00015+1 种基金supported by the European Union,Recovery and Resilience Facility.The János Bolyai Research Fellowship(A.W.)of the Hungarian Academy of Sciences is greatly acknowledged.The authors acknowledge CF CryoEM of CIISB,Instruct-CZ Centre,supported by Ministry of Education,Youth and Sports,Czech Republic(MEYS CR)(no.LM2023042)European Regional Development Fund-Project"UP CIISB"(n0.CZ.02.1.01/0.0/0.0/18_046/0015974).
文摘Peptide-based assemblies have gained increasing attention in different areas of nanotechnology,drug delivery and molecular biology.Among these,non-natural β-peptide scaffolds are particularly promising,as their programmable and diverse secondary structures,high metabolic stability and strong self-association propensity can be easily exploited to create variable constructs.We have recently demonstrated that heterochiral,acyclic β^(3)-peptides assembled into striped lamellar nanostructures that induced antibacterial activity.The process of this assembly formation could be exploited in diverse areas,however identifying oligomerisation stages,and more importantly,controlling the spontaneous process at different levels is still lacking.In this study,a set of analogues heterochiral hexameric β^(3)-peptide sequences was investigated to understand how systematic,small variations of the sequences,such as single point mutation or N-terminal chemical modification,can influence the resulting assemblies and allow the control of formed morphologies.TEM and cryo-EM combined with molecular dynamics simulation enabled the identification and differentiation of morphological stages throughout the entire multi-step process.Depending on the position of the sequence modifications,the self-assembled structures formed small oligomers,individual protofibrils,extended,flat lamellae,bundles and macroscopic clusters.These results outline how the self-assembly process of short heterochiral β-peptides can be qualitatively fine-tuned by sequence modifications,which contribute to understanding the general peptide assembly processes for their fibrillar morphologies.
基金the National Natural Science Foundation of China(Nos.22004051 and 22072060)the Natural Science Foundation of Jiangsu Province(No.BK20180858)+4 种基金the China Postdoctoral Science Foundation(No.2019M661733)the Scientific Research Starting Foundation for Senior Talent at Jiangsu University(No.18JDG025)Science Foundation of Wuxi Health Committee(No.BJ202220)Top Talent Support Program for young and middle-aged people of WuxiHealth Committee(No.BJ2023105)Opening of Jiangsu Provincial Key Laboratory of Laboratory Medicine(No.JSKLM-T-2024-1).
文摘The simultaneous detection of carcinoembryonic antigen(CEA)and microRNA-21(miR-21)is of significant clinical importance for cancer diagnosis,prognosis evaluation,and therapy monitoring.In this study,we developed a novel electrochemical biosensor utilizing a peptide-self-assembly-engineered signal amplification(PSA-e-SA)nanoarchitectonic strategy to achieve ultrasensitive and simultaneous quantification of these two critical biomarkers.By designing amphiphilic peptides(C_(16)-MB-AptamerCEA and C_(16)-Fc-ssDNA2)as multifunctional probes,the system exploits their dual roles in target recognition and signal amplification.These peptides self-assemble into nanostructures under mild conditions,facilitating enhanced loading of electroactive molecules such as methylene blue(MB)and ferrocene(Fc),thereby significantly amplifying the electrochemical signal.The biosensor achieved detection limits of 0.788 pM for CEA and 0.0357 nM for miR-21,demonstrating remarkable sensitivity enhancements of 18-fold and 3.8-fold compared to unamplified approaches.As a proof-of-concept study,further experiments underscored the excellent reproducibility and stability of the strategy while also demonstrating its applicability when tested with simulated serum samples.Thus,this work not only presents a valuable assay tool for early cancer diagnosis and biomarker analysis but also indicates that this signal amplification strategy based on peptide self-assembly engineering can be extended to detect other disease-related biomarkers,propelling the development of clinical applications for multifunctional biosensors.
基金supported by the National Basic Research Program of China 973 Program(Nos.2021YFA0910803,2021YFC2103900)the National Natural Science Foundation of China(No.21977011)+4 种基金the Natural Science Foundation of Guangdong Province(Nos.2022A1515010996 and 2020A1515011544)the Shenzhen Science and Technology Innovation Committee(Nos.RCJC20200714114433053,JCYJ20180507181527112 and JCYJ20200109140406047)the Shenzhen-Hong Kong Institute of Brain Science-Shenzhen Fundamental Research Institutions(No.2019SHIBS0004)the Shenzhen Fundamental Research Program(No.GXWD20201231165807007–20200827170132001)Tian Fu Jin Cheng Laboratory(Advanced Medical Center)Group Racing Project(No.TFJC2023010008)。
文摘Developing novel building blocks with predictable side-chain orientations and minimal intramolecular interactions is essential for peptide-based self-assembling materials.Traditional structures likeα-helices andβ-sheets rely on such interactions for stability,limiting control over exposed interacting moieties.Here,we reported a novel,frame-like peptide scaffold that maintains exceptional stability without intramolecular interactions.This structure exposes its backbone and orients side chains for hierarchical self-assembly into micron-scale cubes.By introducing mutations at specific sites,we controlled packing orientations,offering new options for tunable self-assembly.Our scaffold provides a versatile platform for designing advanced peptide materials,with applications in nanotechnology and biomaterials.
基金supported by the National Key Research and Development Program of China(2023YFB3810001)the National Natural Science Foundation of China(52333007 and 52273197)+3 种基金the Guangdong Basic and Applied Basic Research Foundation(2023A1515011004)the Shenzhen Key Laboratory of Functional Aggregate Materials(ZDSYS20211021111400001)the Science Technology Innovation Commission of Shenzhen Municipality(GJHZ20210705141810031,KQTD20210811090142053,and JCYJ20220818103007014)the Innovation and Technology Commission of Hong Kong(ITC-CNERC14SC01).
文摘Biopolymer-driven supramolecular chirality in aqueous media has gained significant advancements in hierarchical chiral nanostructures.However,researches on the aqueous circularly polarized luminescence(CPL)induced by supramolecular selfassembly and its mechanism have been rarely reported.Herein,we explore the hierarchical chirality transfer in self-assembled fluorescent homopolypeptide systems showing aqueous CPL,and unveil anα-helix-dominated CPL regulation mechanism.A relationship is established between molecular structure(degree of polymerization,DP),supramolecular assembly(self-assembly temperature,T_(SA)),and resulting CPL properties.The stabilization for the homopolypeptideα-helix by increasing DP and decreasing T_(SA) enables efficient chirality transfer from the polypeptide backbone to its terminal chromophore,thereby improving CPL properties.Our work elucidates the critical role ofα-helix control in aqueous CPL systems,providing insights for designing biocompatible and tunable CPL-active nanomaterials.
基金supported by the National Natural Science Foundation of China(82272145)and the Foundation of Westlake University.
文摘CONSPECTUS:Controlling self-assembled peptide nanostructures has emerged as a significant area of research,offering versatile tools for developing functional materials for various applications.This Account emphasizes the essential role of noncovalent interactions,particularly in peptide-based materials.Key forces,such as aromatic stacking and hydrogen bonding,are crucial for promoting molecular aggregation and stabilizing supramolecular structures.Numerous studies demonstrate how these interactions influence the phase transitions and the morphology of self-assembled structures.Recent advances in computational methodologies,including molecular dynamics simulations and machine learning,have significantly enhanced our understanding of self-assembly processes.These tools enable researchers to predict how molecular properties,such as hydrophobicity,charge distribution,and aromaticity,affect assembly behavior.Simulations uncover the energetic landscapes governing peptide aggregation,providing insights into the kinetic pathways and thermodynamic stabilities.Meanwhile,machine learning facilitates the rapid screening of peptide libraries,identifying sequences with optimal self-assembly characteristics,and accelerating material design with tailored functionalities.Beyond their structural and physicochemical properties,self-assembled peptide nanostructures hold immense potential in biological applications due to their versatility and biocompatibility.By manipulating molecular interactions,researchers have engineered responsive systems that interact with cellular environments to elicit specific biological responses.These peptide nanostructures can mimic extracellular matrices,facilitating cell adhesion,proliferation,and differentiation.They also show promise in modulating immune responses,recruiting immune cells,and regulating signaling pathways,making them valuable tools in immunotherapy and regenerative medicine.Moreover,their ability to disrupt bacterial membranes positions them as innovative alternatives to conventional antibiotics,addressing the urgent need for solutions to antimicrobial resistance.Despite its promise,peptide self-assembly faces several challenges.The assembly process is highly sensitive to environmental conditions,such as pH,temperature,and ionic strength,leading to variability in the morphology and properties.Furthermore,peptide aggregation can result in heterogeneous and poorly defined assemblies,complicating the reproducibility and scalability.Designing peptides with predictable self-assembly behavior remains a significant hurdle.Looking ahead,integrating computational predictions with experimental validations will be crucial in discovering novel peptide sequences with tailored self-assembly properties.Machine learning,combined with high-throughput screening techniques,will enable the rapid identification of optimal peptide sequences.In situ characterization tools,such as cryoelectron microscopy and advanced spectroscopy,will provide deeper insights into assembly mechanisms,aiding the rational design of peptide materials.As research progresses,the dynamic and reversible nature of noncovalent interactions can be leveraged to create adaptive responsive to environmental stimuli.Self-assembled peptide nanostructures are poised for impactful applications in biomedicine including targeted drug delivery,tissue repair,and advanced therapeutic strategies.Ultimately,these nanostructures represent a powerful platform for addressing complex challenges in biomedicine and beyond,paving the way for transformative breakthroughs in science and technology.
基金Project supported by the National Basic Research Program of China(Grant No.2013CB932804)the National Natural Science Foundation of China(Grant Nos.11421063,11647601,11504431,and 21503275)+1 种基金the Scientific Research Foundation of China University of Petroleum(East China)for Young Scholar(Grant Y1304073)financial support through the CAS Biophysics Interdisciplinary Innovation Team Project(Grant No.2060299)
文摘Nanostructures self-assembled by cross-β peptides with ordered structures and advantageous mechanical properties have many potential applications in biomaterials and nanotechnologies. Quantifying the intra-and inter-molecular driving forces for peptide self-assembly at the atomistic level is essential for understanding the formation mechanism and nanomechanics of various morphologies of self-assembled peptides. We investigate the thermodynamics of the intra-and inter-sheet structure formations in the self-assembly process of cross-β peptide KⅢIK by means of steered molecular dynamics simulation combined with umbrella sampling. It is found that the mechanical properties of the intra-and inter-sheet structures are highly anisotropic with their intermolecular bond stiffness at the temperature of 300 K being 5.58 N/m and 0.32 N/m, respectively. This mechanical anisotropy comes from the fact that the intra-sheet structure is stabilized by enthalpy but the inter-sheet structure is stabilized by entropy. Moreover, the formation process of KⅢIK intra-sheet structure is cooperatively driven by the van der Waals （VDW） interaction between the hydrophobic side chains and the electrostatic interaction between the hydrophilic backbones, but that of the inter-sheet structure is primarily driven by the VDW interaction between the hydrophobic side chains. Although only peptide KⅢIK is studied, the qualitative conclusions on the formation mechanism should also apply to other cross-β peptides.
基金supported by the National Key Research and Development Program of China(2022YFC2105003,2022YFC2602500)National Natural Science Foundation of China(92469103,32400769,32300404)+6 种基金Chinese Academy of Sciences(YSBR-111,SAJC202402)Yunnan Provincial Science and Technology Department(202305AH340007,202301AT070343,202502AA310005)Yunnan Characteristic Plant Extraction Laboratory(2025YKZY002)Kunming Science and Technology Bureau(2022SCP007)New Cornerstone Investigator Program from Shenzhen New Cornerstone Science Foundation(NCI202238)Tianfu Jincheng Laboratory Foundation(TFJC2023010007)Chinese Academy of Sciences and World Academy of Sciences(CAS-TWAS)President’s Fellowship Program(2019A8010415001)。
文摘Effective countermeasures against multidrug-resistant nosocomial pathogens,such as carbapenem-resistant Klebsiella pneumoniae and methicillin-resistant Staphylococcus aureus(MRSA),require the development of innovative antimicrobial strategies.This study presents a structure-function approach to antimicrobial peptide(AMP)design through the strategic integration of a cationic backbone with a hydrophobic core.This dual-domain architecture enables robust hydrophobic and electrostatic interactions,promoting spontaneous self-assembly and efficient membrane engagement.The lead peptide,Tryptolycin(TRPY),formed stable,monodisperse nanoparticles and demonstrated broad-spectrum bactericidal activity,with minimum inhibitory concentrations≤1μmol/L against multiple strains of MRSA and K.pneumoniae,while exerting minimal cytotoxicity toward mammalian cells.TRPY achieved rapid bacterial elimination,eradicating 99.9%of both planktonic and persister populations within minutes.Mechanistic investigations revealed that TRPY induced membrane permeabilization,promoted reactive oxygen species(ROS)production,and inhibited biofilm formation.In murine infection models,TRPY effectively eradicated established infections,reducing bacterial burden across target organs by 3-to 5-fold without significant cytotoxicity at therapeutic concentrations.Collectively,these findings establish TRPY as a promising therapeutic agent for clinical translation in the treatment of refractory bacterial infections.
基金supported by the Natural Science Foundation of Jiangsu Province(No.BK20220409)the National Natural Science Foundation of China(No.22401153)+2 种基金the FWO[Fund for Scientific Research-Flanders(Belgium)]for financial support(recipient Erik V.Van der Eycken)the Research Council of the KU Leuven(recipient Erik V.Van der Eycken)the support of the"RUDN University Strategic Academic Leadership Program"(recipient Erik V.Van der Eycken).
文摘Peptides play important roles in chemistry,medicinal chemistry and life science,due to their high efficiency and specificity,unusual biological and therapeutic properties.As naturally occurring peptides often face with their intrinsic limitations including metabolic instability and low membrane permeability,the strategies for synthesizing unnatural amino acids and peptides are explored.Among the methods for modifying amino acids and peptides,chemo-and site-selective approaches are preferred because of the ability to fine-tuning structural features.Recently,transition metal-catalyzed C–H activation has been employed for the functionalization of amino acids and peptides.Through domino C–H activation/annulation,a series of structurally complex and diverse amino acids and peptides is constructed.This review highlights recent advances in the synthesis of unnatural amino acids and peptides via transition metal-catalyzed C–H activation/annulation.
文摘The escalating global crisis of antibiotic resistance necessitates urgent development of novel antimicrobial agents.In this context,antimicrobial peptides(AMPs)derived from fish emerge as a highly promising strategic resource,owing to their unique structural diversity and the exceptional adaptability and tolerance conferred by evolutionary pressures in aquatic environments.This review systematically synthesizes key advances in fish-derived AMP research.It details their diverse sourcing avenues,encompassing tissues from live fish(e.g.,skin,mucus,gills,intestines)and processing byproducts(e.g.,scales,skins,viscera).The discussion covers efficient isolation,purification,and synthesis strategies,and critically examines their defining feature:unique multi-target synergistic antimicrobial mechanisms(including microbial membrane disruption,intracellular targeting,and immunomodulation),which contribute to a reduced propensity for resistance development.To address inherent limitations of natural AMPs(such as susceptibility to proteolysis and potential toxicity),the review highlights innovative optimization approaches,including computational-aided rational design,amino acid modification,cyclization,and hybrid peptide construction.Furthermore,the review elaborates on their significant application potential across crucial domains:food preservation(inhibiting spoilage organisms,extending shelf-life),sustainable aquaculture(as antibiotic alternatives,enhancing disease resistance,improving water quality),and the development of novel anti-infective therapeutics(particularly against drug-resistant infections).Therefore,this work aims to provide a comprehensive theoretical foundation and innovative strategic insights to foster in-depth research and the sustainable exploitation of this vital strategic biological resource.
基金the research grant from the Youth Fund of the National Natural Science Foundation of China(62305340)the financial support from the Hong Kong Research Grant Council via STEM Postdoctoral Fellowship(Project no.9446002)+6 种基金the Alexander von Humboldt Foundation and the support during his stay in Christoph J.Brabec’s group at Friedrich-Alexander-Universität Erlangen-Nürnberg and Helmholtz-Institute Erlangen-Nürnberg(HI ERN)the research grant from KAUST global fellowship postdocfinancial support from the Innovation and Technology Commission(Grant no.MHP/104/21)Shenzhen Science and Technology Innovation Commission(JCYJ20210324125612035,R-IND12303,and R-IND12304)the National Key Research and Development Program of China(no.2021YFA1500900)the National Natural Science Foundation of China(no.52071174)the support from the Hong Kong Jockey Club under the research work Hong Kong JC STEM Lab for Circular Bio-economy(Project No.2023-0078)。
文摘Sustainability and scalability remain critical hurdles for the commercialization of organic solar cells(OSCs).However,addressing both poses challenge.Herein,we introduce a simple yet effective strategy utilizing 3,5-dichloropyridine(PDCC)as a solid additive to fine-tune the self-assembly behavior of Y-series non-fullerene acceptors(NFAs)to tackle the upscaling limitations in green-solvent-processed OSCs.PDCC predominantly interacts with Y-series NFAs,facilitating molecular crystallization and thereby driving the self-assembly of Y-series NFAs during film-forming dynamics,leading to more uniform active layers with improved molecular packing and reduced charge recombination.As a result,PDCC-driven self-assembly strategy enables high-performance OSCs with a power conversion efficiency(PCE)of 20.47%.When translated to sustainable fabrication,this strategy significantly boosts the PCE of large-area green-solvent-processed OSC modules(19.3 cm^(2))from 13.87%to 15.79%,ranking it among the best-performing green-solvent-processed large-area OSC modules(>18 cm^(2)).Beyond its impact on PCE enhancement,PDCC serves as a multifunctional additive to improve long-term stability and exhibits strong universality across multiple material systems.This work establishes a promising approach for advancing sustainable and scalable OSCs,paving the way for their commercialization.
基金supported by the National Natural Science Foundation of China(32571991)Guangxi Natural Science Foundation of China(2023GXNSFGA026001&2025GXNSFAA069870)the Foundation of State Key Laboratory of Biobased Material and Green Papermaking.(No.GZKF202323)。
文摘The rapid advancement of flexible electronics technology has placed higher demands on the structural design and performance regulation of elastic materials.Cellulosic elastomers,with their biodegradability,renewability,and tunability,emerge as ideal candidate materials.Entropy-driven self-as sembly promotes the spontaneous formation of ordered structures,serving as a crucial pathway for optimizing cellulose elastomer properties.However,the structure-property relationship between the self-assembled ordered structures of cellulose elastomers and their mechanical and electrical properties remains insufficiently explored.It hinders the expansion of their applications in electronic devices.This paper systematically reviews the structure-property regulation mechanisms of self-assembled cellulosic elastomers from an entropy-driven perspective.It elucidates the application principles and performance optimization strategies for mechanical energy harvesting and self-powered sensing,while also exploring the challenges and prospects for performance enhancement.This work provides a reference for the development of self-assembled cellulosic elastomers in the field of energy devices.
基金Financial support from the National Natural Science Foundation of China(32502106)One health Interdisciplinary Research Project,Institute of One Health Science,Ningbo University(NBUOH202502)the Ningbo Top Talent Project(215-432094250).
文摘The antioxidant activity of selenium-containing soybean peptides(SePPs)has been previously demonstrated,despite their limited absorption in the small intestine.This study investigates the antioxidant mechanism of a selenium-containing tetrapeptide,Ser-Phe-Gln-SeM(SFQSeM),identified from SePPs,with particular emphasis on its interaction with the intestinal microbiota and its role in modulating host antioxidant defenses.The effects of SFQSeM were evaluated in a D-galactose-induced oxidative stress model and an antibiotictreated mouse model.SFQSeM supplementation significantly reduced the oxidative stress in D-galactosetreated mice.It also promoted the growth of beneficial bacteria and increased the levels of acetate,butyrate and lactate in the intestine(P<0.05).In the antibiotic-treated mouse model,depletion of the intestinal microbiota significantly reduced hepatic glutathione peroxidase(GSH-Px)activity(26.6%)and glutathione peroxidase 1(GPx-1)expression(48.77%)compared to normal mice supplemented with SFQSeM(P<0.05).In contrast to Na_(2)SeO_(3)and selenomethionine,SFQSeM effectively restored the diversity of the intestinal microbiota disrupted by antibiotics.Lactobacillus,Lachnospiraceae_NK4A136_group,and Muribaculaceae were identified as predominant bacteria in the SFQSeM group,and were strongly associated with increased hepatic GSH-Px activity and GPx-1 mRNA expression(P<0.05).In conclusion,intestinal microbiota enhances the antioxidant efficacy of SFQSeM by modulating microbial composition,producing active metabolites,and converting SFQSeM into a bioactive form of selenium.
文摘Peroxymonosulfate(PMS)-assisted visible-light photocatalytic degradation of organic pollutants using graphitic carbon nitride(g-C_(3)N_(4))presents a promising and environmentally friendly approach.However,pristine g-C_(3)N_(4) suffers from limited visible-light absorption and low charge-carrier mobility.In this study,a phosphorus-doped tubular carbon nitride(5P-TCN)was synthesized via a precursor self-assembly method using phosphoric acid and melamine as raw materials,eliminating the need for organic solvents or templates.The 5P-TCN catalyst demonstrated enhanced visible-light absorption,improved charge transfer capability,and a 5.25-fold increase in specific surface area(31.092 m^(2)/g),which provided abundant active sites to efficiently drive the PMS-assisted photocatalytic reaction.The 5P-TCN/vis/PMS system exhibited exceptional degradation performance for organic pollutants across a broad pH range(3–9),achieving over 92%degradation of Rhodamine B(RhB)within 15 min.Notably,the system retained>98%RhB degradation efficiency after three consecutive operational cycles,demonstrating robust operational stability and reusability.Moreover,key parameters influencing,active radi-cals,degradation pathways,and potential mechanisms for RhB degradation were systematically investigated.This work proposes a green and cost-effective strategy for developing high-efficiency photocatalysts,while demon-strating the exceptional capability of a PMS-assisted photocatalytic system for rapid degradation of RhB.
基金RGM is grateful to CNPq for the PDE fellowship(200437/2025-9),MTM acknowledges CNPq research scholarship(314470/2023-9)FAPESP fundings(2022/01825-22025/063196).
文摘Peptide-and drug-protected gold nanoclusters(Au NCs)with atomic precision have attracted research attention in the last few years owing to their ultrasmall size(<2 nm),well-defined structures,tunable photoluminescence from the visible to near-infrared range,water solubility,and good biocompatibility.These features,combined with low toxicity and efficient renal clearance,make such Au NCs promising candidates for biomedical use,including diagnosis,therapy,and theranostic.The incorporation of peptides or drugs into Au NCs enhances the stability,targeting specificity,cellular uptake,and prolonged circulation,enabling precise modulation of biological responses.Despite notable advances in achieving atomic precision employing complex ligands such as peptides or drugs,the synthetic methods of this new class of NCs remain a challenge.Careful control of molar ratio(Au:peptide/drug),reducing agent,temperature,and reaction time is required,because these factors directly influence the cluster size,optical properties,and in vivo performance.In this review,we highlight different synthetic approaches of atomically precise peptide-and drug-protected Au NCs,emphasizing the role of rational ligand design and reaction conditions,as well as the challenges associated with structural determination.We further discuss the optical and photoluminescence properties of peptide-protected Au NCs-the mostly explored features for biomedical applications.Finally,we conclude by outlining the current challenges,opportunities for scale-up synthesis,and future design perspectives for these emerging nanomaterials.
基金supported by the following grants:National Natural Science Foundation of China(Grant Nos.92354305 and 32271428),National Key R&D Program of China(Grant No.2022YFC3401100)Young Talent Program of Hubei Provincial Health Commission(WJ2025Q037)+1 种基金Interdisciplinary Research Program of HUST(Grant No.2023JCY5045)Director Fund of WNLO.
文摘Fluorescent probes,with their superior optical properties and labeling versatility,have greatly advanced the visualization of intracellular molecules and subcellular structures.However,poor cytoplasmic delivery,caused by charge,size,or targeting groups,limits the effective use of many fluorescent probes in live cells.Recently,cell-penetrating peptides(CPPs)have emerged as efficient carriers,offering great potential for the cytoplasmic delivery of fluorescent probes in live cells.This review provides a comprehensive overview of CPPs as vehicles for probe delivery,outlining advances in their development,conjugation chemistries,and intracellular delivery mechanisms.Recent applications in live-cell imaging are highlighted and organized according to major CPP modification strategies,including sequence engineering,cyclization,hybrid design and enhancement by chemical reagents.Finally,the challenges that remain and the future outlook of this rapidly evolvingfield are discussed.
基金supported by the National Natural Science Foundation of China(22378368).
文摘The blood-brain barrier(BBB)is a major challenge in drug delivery for the treatment of central nervous system diseases.Walnut derived peptide TWLPLPR(TW-7)has been proved to promote neuronal mitochondrial autophagy and enhance hippocampal neuronal synaptic plasticity,thereby improving learning and memory abilities in mice.We investigated the internalization mechanism and intracellular transport pathway for the walnut-derived peptide,TW-7,using b End.3 cells in an in vitro BBB model system.TW-7 was taken up by the b End.3 cells in a concentration-,temperature-,and energy-dependent manner;this involved increases in caveolin-1 and caveolin-2 protein expression and phosphorylation and inhibition of P-glycoprotein-mediated efflux.Subcellular localization of TW-7 in b End.3 cells was observed,indicating that the plasma membrane,endoplasmic reticulum,Golgi apparatus,lysosomes,and mitochondria participated in intracellular trafficking and that the peptide escaped from lysosomes over time.Caveolae may be critical for TW-7 uptake by brain microvascular endothelial cells,assisting TW-7 to cross the BBB.The results of this study provide a theoretical basis for the mechanism of active peptide penetrating the BBB,and provide a reference for developing neuroprotective active peptide products.
