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Updated: Apr 11, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
Natural peptides from Vigna radiata protein hydrolysates suppress protein glycation via radical scavenging and
Shengru Yang1, Yinchen Hou2, Yanan Yuan3
1College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.; College of Food and Biological Engineering, Henan University of Animal Husbandry and Economy, Zhengzhou 450046, China.
Abstract:
This study evaluated plant-derived protein hydrolysates from Vigna radiata (VRPHs), corn, and wheat as potential inhibitors of protein glycation and advanced glycation end products (AGEs) formation. Hydrolysates suppressed intermediates formed during fructose-induced bovine serum albumin (BSA) glycation and reduced carbonyl and thiol modifications, oxidation products, and crosslinking. Their antiglycation effects were associated with BSA interaction, methylglyoxal (MGO) trapping and radical scavenging. Following integrated evaluation, VRPHs were fractionated, identified by LC-MS/MS, screened and prioritized via molecular docking against representative targets associated with antiglycation-related processes. Among five synthesized peptides, FDPLG (F5) and LDGWP (L5) showed the strongest in vitro antiglycation activity (IC₅₀ = 1.897 and 2.296 mM, respectively). Docking analyses suggested F5 and L5 interacted with major glycation sites on BSA and showed potential in silico interactions with NOX2 and MGO. These findings revealed the antiglycation potential of plant-derived protein hydrolysates, identifying F5 and L5 as promising peptides for further mechanistic investigation.
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