Rice-derived peptides are a sustainable protein source with emerging lipid regulation functions.In this study,peptides with novel pancreatic lipase(PL)and cholesterol esterase(CE)inhibition from rice protein hydrolysa...Rice-derived peptides are a sustainable protein source with emerging lipid regulation functions.In this study,peptides with novel pancreatic lipase(PL)and cholesterol esterase(CE)inhibition from rice protein hydrolysates(RPHs)were identified by peptidomics.Then their alleviating effects and mechanisms on lipid accumulation in cells were investigated.55 peptides were identified,showing significant enrichment of Phe,Pro,Arg,and Leu,with hydrophobic/polar amino acids at terminal positions.Among them,five peptides(WQ7,FR6,GF6,GA7,and GY7)exhibited potent inhibitory activity against PL and CE,with IC_(50)values of 0.19-0.70μg/mL and 0.22-0.25μg/mL,respectively.Molecular docking studies revealed that five peptides bind stably to the active sites of PL(Phe77,Tyr114,Phe215,and His263)and CE(Ser194 and His435)through hydrogen bonding,PIalkyl,and PI-PI interactions.Dynamic simulations demonstrated that three peptides(WQ7,FR6,and GF6)form stable complexes with both CE and PL,exhibiting strong binding affinity.In vitro study confirmed that these peptides reduced levels of TC,TG,and LDL-c while increasing HDL-c content,with WQ7 showing superior efficacy.Western blot and qPCR results indicated WQ7 regulated lipid metabolism by suppressing the PPARγpathway and downregulating the protein expression of related factors,such as ACS,FASN,and SREBP-1c.This study showed that the WQ7,a multifunctional bioactive peptide,demonstrates direct enzyme-inhibitory activity and regulates core transcriptional pathways,providing theoretical support for utilizing rice protein in the development of lipid-lowering functional food.展开更多
基金supported by the National Natural Science Foundation of China(32572484)Natural Science Foundation of Hunan Province(2022JJ30587,2022JJ50218)Science and Technology Innovation Program of Hunan Province(2024JK2145).
文摘Rice-derived peptides are a sustainable protein source with emerging lipid regulation functions.In this study,peptides with novel pancreatic lipase(PL)and cholesterol esterase(CE)inhibition from rice protein hydrolysates(RPHs)were identified by peptidomics.Then their alleviating effects and mechanisms on lipid accumulation in cells were investigated.55 peptides were identified,showing significant enrichment of Phe,Pro,Arg,and Leu,with hydrophobic/polar amino acids at terminal positions.Among them,five peptides(WQ7,FR6,GF6,GA7,and GY7)exhibited potent inhibitory activity against PL and CE,with IC_(50)values of 0.19-0.70μg/mL and 0.22-0.25μg/mL,respectively.Molecular docking studies revealed that five peptides bind stably to the active sites of PL(Phe77,Tyr114,Phe215,and His263)and CE(Ser194 and His435)through hydrogen bonding,PIalkyl,and PI-PI interactions.Dynamic simulations demonstrated that three peptides(WQ7,FR6,and GF6)form stable complexes with both CE and PL,exhibiting strong binding affinity.In vitro study confirmed that these peptides reduced levels of TC,TG,and LDL-c while increasing HDL-c content,with WQ7 showing superior efficacy.Western blot and qPCR results indicated WQ7 regulated lipid metabolism by suppressing the PPARγpathway and downregulating the protein expression of related factors,such as ACS,FASN,and SREBP-1c.This study showed that the WQ7,a multifunctional bioactive peptide,demonstrates direct enzyme-inhibitory activity and regulates core transcriptional pathways,providing theoretical support for utilizing rice protein in the development of lipid-lowering functional food.
