The objective of this study was to isolate and purify DPP-IV inhibitory(DPP-IVi)peptides from rabbit meat hydrolysate(RMH)and explore their mechanism of action,stability,and hypoglycemic effects.Various pro-teases,inc...The objective of this study was to isolate and purify DPP-IV inhibitory(DPP-IVi)peptides from rabbit meat hydrolysate(RMH)and explore their mechanism of action,stability,and hypoglycemic effects.Various pro-teases,including pepsin,alcalase,compound proteinase,flavourzyme,and bromelain,were utilized to prepare RMH,with RMH derived from the compound proteinase demonstrating the highest DPP-IV inhibition activity.Employing gel filtration chromatography,RP-HPLC and UPLC-MS/MS,we identified Leucyl-Leucine(LL),a dipeptide exhibiting potent DPP-IV inhibitory activity(IC_(50)=99.85±5.45μM).LL exhibited resistance to simulated gastrointestinal digestion in vitro and competitively inhibited DPP-IV.Molecular docking analysis revealed LL’s formation of hydrogen bonds and hydrophobic interactions with key amino acid residues of DPP-IV.Furthermore,LL exhibits good inhibitory activity in situ against DPP-IV.,with an IC_(50) value of 207.40±21.50μM.In an oral glucose tolerance test(OGTT),LL displayed significant hypoglycemic effects at 30 min after administration.In conclusion,LL derived from rabbit meat hydrolysate exhibited remarkable DPP-IV inhibition activity and hypoglycemic effects,suggesting its potential as a therapeutic candidate for diabetes treatment.展开更多
In recent years,bioactive peptides targeting dipeptidyl peptidase-IV(DPP-IV)have emerged as promising candidates for managing type 2 diabetes.This study aimed to screen novel DPP-IV inhibitory(DPP-IVi)peptides from ra...In recent years,bioactive peptides targeting dipeptidyl peptidase-IV(DPP-IV)have emerged as promising candidates for managing type 2 diabetes.This study aimed to screen novel DPP-IV inhibitory(DPP-IVi)peptides from rabbit meat proteins using a combined approach of in silico study and in vitro experiments,with a focus on elucidating their molecular mechanisms.Initially,enzymatic simulation and virtual screening identified three potential DPP-IVi peptides.Among these,the tetrapeptide IPVK exhibited the strongest inhibitory activity(IC50=152.9±14.55μM),demonstrating competitive inhibition in vitro.Additionally,IPVK displayed robust resilience under diverse conditions,including variations in temperature,pH,and gastrointestinal digestion.Further analysis using molecular docking revealed IPVK’s interaction with critical residues within the S1,S2 pockets,and catalytic triad of DPP-IV through hydrogen bonds and hydrophobic interactions.Molecular dynamics simulations confirmed the stable formation of the IPVK-DPP-IV complex,providing insight into the peptide’s stability and binding affinity.Moreover,the highest occupied molecular orbital(HOMO)analysis highlighted isoleucine and proline as essential components for IPVK’s bioactivity.Supporting these findings,IPVK effectively inhibited native DPP-IV in Caco-2 cells(IC50=287.40±29.50μM)and exhibited hypoglycemic effects in vivo in mice.In summary,this study presents an efficient method for screening and identifying DPP-IVi peptides.The discovery of IPVK highlights rabbit meat proteins as a potential source of DPP-IV inhibitors,establishing a robust theoretical basis for its application in the management of type 2 diabetes.展开更多
Douchi(DC)is a traditional Chinese condiment renowned for its rich umami flavor.This study aimed to comprehensively investigate the composition,characteristics,potential taste mechanisms,and antioxidant activity of um...Douchi(DC)is a traditional Chinese condiment renowned for its rich umami flavor.This study aimed to comprehensively investigate the composition,characteristics,potential taste mechanisms,and antioxidant activity of umami peptides in DC.The aqueous extract of DC underwent ultrafiltration and gel column chromatography to isolate its high umami components.Three novel umami peptides(EEQEHT,FED,AEPE)were identified using liquid chromatography-tandem mass spectrometry(LC-MS/MS)coupled with bioinformatics analysis.Electronic tongue studies confirmed the high umami activity of these peptides,with scores ranging from 7.64 to 8.72 at a concentration of 0.2 mg/mL,with FED exhibiting the highest umami intensity,minimal bitterness and pronounced saltiness.Molecular docking studies revealed that all three umami peptides were embedded within the T1R1 subunit,facilitating their binding to the umami receptor via hydrogen bonding.Additionally,these peptides demonstrated significant in vitro antioxidant activities,scavenging 2,2-Diphenyl-1-picrylhydrazyl(DPPH)and hydroxyl radicals.In vivo assessments on zebrafish embryos exposed to oxidative stress showed improved survival rates,normalized heart rates,and dose-dependent reductions in reactive oxygen species(ROS)levels.In conclusion,this study provides valuable insights into the umami peptides present in DC,highlighting their potential applications in the food and health supplement industries.展开更多
基金supported by Chongqing Forestry Reform and Development Fund(grant number Yu-lin-ke-tui-2019-2)the Project of Chongqing Science and Technology Bureau(grant number cstc2017chmsxdny0246).
文摘The objective of this study was to isolate and purify DPP-IV inhibitory(DPP-IVi)peptides from rabbit meat hydrolysate(RMH)and explore their mechanism of action,stability,and hypoglycemic effects.Various pro-teases,including pepsin,alcalase,compound proteinase,flavourzyme,and bromelain,were utilized to prepare RMH,with RMH derived from the compound proteinase demonstrating the highest DPP-IV inhibition activity.Employing gel filtration chromatography,RP-HPLC and UPLC-MS/MS,we identified Leucyl-Leucine(LL),a dipeptide exhibiting potent DPP-IV inhibitory activity(IC_(50)=99.85±5.45μM).LL exhibited resistance to simulated gastrointestinal digestion in vitro and competitively inhibited DPP-IV.Molecular docking analysis revealed LL’s formation of hydrogen bonds and hydrophobic interactions with key amino acid residues of DPP-IV.Furthermore,LL exhibits good inhibitory activity in situ against DPP-IV.,with an IC_(50) value of 207.40±21.50μM.In an oral glucose tolerance test(OGTT),LL displayed significant hypoglycemic effects at 30 min after administration.In conclusion,LL derived from rabbit meat hydrolysate exhibited remarkable DPP-IV inhibition activity and hypoglycemic effects,suggesting its potential as a therapeutic candidate for diabetes treatment.
基金supported by Chongqing Forestry Reform and Development Fund(grant number Yu-lin-ke-tui-2019-2)Chongqing Normal University Fund projects(grant number 19XLB006).
文摘In recent years,bioactive peptides targeting dipeptidyl peptidase-IV(DPP-IV)have emerged as promising candidates for managing type 2 diabetes.This study aimed to screen novel DPP-IV inhibitory(DPP-IVi)peptides from rabbit meat proteins using a combined approach of in silico study and in vitro experiments,with a focus on elucidating their molecular mechanisms.Initially,enzymatic simulation and virtual screening identified three potential DPP-IVi peptides.Among these,the tetrapeptide IPVK exhibited the strongest inhibitory activity(IC50=152.9±14.55μM),demonstrating competitive inhibition in vitro.Additionally,IPVK displayed robust resilience under diverse conditions,including variations in temperature,pH,and gastrointestinal digestion.Further analysis using molecular docking revealed IPVK’s interaction with critical residues within the S1,S2 pockets,and catalytic triad of DPP-IV through hydrogen bonds and hydrophobic interactions.Molecular dynamics simulations confirmed the stable formation of the IPVK-DPP-IV complex,providing insight into the peptide’s stability and binding affinity.Moreover,the highest occupied molecular orbital(HOMO)analysis highlighted isoleucine and proline as essential components for IPVK’s bioactivity.Supporting these findings,IPVK effectively inhibited native DPP-IV in Caco-2 cells(IC50=287.40±29.50μM)and exhibited hypoglycemic effects in vivo in mice.In summary,this study presents an efficient method for screening and identifying DPP-IVi peptides.The discovery of IPVK highlights rabbit meat proteins as a potential source of DPP-IV inhibitors,establishing a robust theoretical basis for its application in the management of type 2 diabetes.
基金supported by Chongqing Forestry Reform and Development Fund(grant number Yu-lin-ke-tui-2019-2)the Project of Chongqing Science and Technology Bureau(grant number cstc2017chmsxdny0246).
文摘Douchi(DC)is a traditional Chinese condiment renowned for its rich umami flavor.This study aimed to comprehensively investigate the composition,characteristics,potential taste mechanisms,and antioxidant activity of umami peptides in DC.The aqueous extract of DC underwent ultrafiltration and gel column chromatography to isolate its high umami components.Three novel umami peptides(EEQEHT,FED,AEPE)were identified using liquid chromatography-tandem mass spectrometry(LC-MS/MS)coupled with bioinformatics analysis.Electronic tongue studies confirmed the high umami activity of these peptides,with scores ranging from 7.64 to 8.72 at a concentration of 0.2 mg/mL,with FED exhibiting the highest umami intensity,minimal bitterness and pronounced saltiness.Molecular docking studies revealed that all three umami peptides were embedded within the T1R1 subunit,facilitating their binding to the umami receptor via hydrogen bonding.Additionally,these peptides demonstrated significant in vitro antioxidant activities,scavenging 2,2-Diphenyl-1-picrylhydrazyl(DPPH)and hydroxyl radicals.In vivo assessments on zebrafish embryos exposed to oxidative stress showed improved survival rates,normalized heart rates,and dose-dependent reductions in reactive oxygen species(ROS)levels.In conclusion,this study provides valuable insights into the umami peptides present in DC,highlighting their potential applications in the food and health supplement industries.
