Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis

The antioxidant activity of natural products is closely related to their antiglycation effects. This study aimed to examine the antiglycation activity and elucidate the underlying mechanisms of two specific peptides, EDYGA (Glu-Asp-Tyr-Gly-Ala) and DLLCIC (Asp-Leu-Leu-Cys-Ile-Val), derived from prot...

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Main Authors: Nuo Chen, Nan Wang, Qiaoyun Fang, Zuolong Yu, Yiyuan Hu, Jiancang Jin, Shengli Yang
Format: Article
Language:English
Published: Frontiers Media S.A. 2025-01-01
Series:Frontiers in Nutrition
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Online Access:https://www.frontiersin.org/articles/10.3389/fnut.2025.1537338/full
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author Nuo Chen
Nan Wang
Qiaoyun Fang
Zuolong Yu
Yiyuan Hu
Jiancang Jin
Shengli Yang
author_facet Nuo Chen
Nan Wang
Qiaoyun Fang
Zuolong Yu
Yiyuan Hu
Jiancang Jin
Shengli Yang
author_sort Nuo Chen
collection DOAJ
description The antioxidant activity of natural products is closely related to their antiglycation effects. This study aimed to examine the antiglycation activity and elucidate the underlying mechanisms of two specific peptides, EDYGA (Glu-Asp-Tyr-Gly-Ala) and DLLCIC (Asp-Leu-Leu-Cys-Ile-Val), derived from protein hydrolysates of the Pelodiscus sinensis. Both EDYGA and DLLCIC were efficient in bovine serum albumin (BSA)/glucose model to inhibit BSA glycation, while DLLCIC showed higher antiglycation activity than EDYGA. Firstly, it was found that EDYGA and DLLCIC could inhibit the formation of NEG and AGEs. Moreover, EDYGA and DLLCIC were able to maintain the protein secondary structure and stabilize the band positions (amide I & II). Additionally, molecular simulations indicated that DLLCIC can spontaneously interact with the central site of BSA, specifically at Lys114 and Glu424 residues, through hydrogen bonds with an energy strength of −0.7 kcal/mol. Furthermore, CCK-8 and morphological experiments confirmed that EDYGA and DLLCIC improved cell survival against AGEs-induced cytotoxicity, with EC50 values of 17.64 μM for EDYGA and 15.08 μM for DLLCIC. These findings serve as a significant reference for the development of EDYGA and DLLCIC as effective antiglycation agents in the prevention of glycation-mediated diseases.
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spelling doaj-art-8d576f0445b7486e9cc96cf5ee70124a2025-08-20T03:11:15ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2025-01-011210.3389/fnut.2025.15373381537338Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensisNuo Chen0Nan Wang1Qiaoyun Fang2Zuolong Yu3Yiyuan Hu4Jiancang Jin5Shengli Yang6The College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, ChinaCollege of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, ChinaCollege of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, ChinaCollege of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, ChinaCollege of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, ChinaCollege of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, ChinaThe College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, ChinaThe antioxidant activity of natural products is closely related to their antiglycation effects. This study aimed to examine the antiglycation activity and elucidate the underlying mechanisms of two specific peptides, EDYGA (Glu-Asp-Tyr-Gly-Ala) and DLLCIC (Asp-Leu-Leu-Cys-Ile-Val), derived from protein hydrolysates of the Pelodiscus sinensis. Both EDYGA and DLLCIC were efficient in bovine serum albumin (BSA)/glucose model to inhibit BSA glycation, while DLLCIC showed higher antiglycation activity than EDYGA. Firstly, it was found that EDYGA and DLLCIC could inhibit the formation of NEG and AGEs. Moreover, EDYGA and DLLCIC were able to maintain the protein secondary structure and stabilize the band positions (amide I & II). Additionally, molecular simulations indicated that DLLCIC can spontaneously interact with the central site of BSA, specifically at Lys114 and Glu424 residues, through hydrogen bonds with an energy strength of −0.7 kcal/mol. Furthermore, CCK-8 and morphological experiments confirmed that EDYGA and DLLCIC improved cell survival against AGEs-induced cytotoxicity, with EC50 values of 17.64 μM for EDYGA and 15.08 μM for DLLCIC. These findings serve as a significant reference for the development of EDYGA and DLLCIC as effective antiglycation agents in the prevention of glycation-mediated diseases.https://www.frontiersin.org/articles/10.3389/fnut.2025.1537338/fullpeptidesinhibitionAGEsmolecular dockingantiglycation
spellingShingle Nuo Chen
Nan Wang
Qiaoyun Fang
Zuolong Yu
Yiyuan Hu
Jiancang Jin
Shengli Yang
Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
Frontiers in Nutrition
peptides
inhibition
AGEs
molecular docking
antiglycation
title Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
title_full Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
title_fullStr Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
title_full_unstemmed Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
title_short Inhibition effect of AGEs formation in vitro by the two novel peptides EDYGA and DLLCIC derived from Pelodiscus sinensis
title_sort inhibition effect of ages formation in vitro by the two novel peptides edyga and dllcic derived from pelodiscus sinensis
topic peptides
inhibition
AGEs
molecular docking
antiglycation
url https://www.frontiersin.org/articles/10.3389/fnut.2025.1537338/full
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