2. Academic Validation
  3. Targeted discovery of pea protein-derived GLP-1-secreting peptides by CaSR activation-based molecular docking and their digestive stability

Targeted discovery of pea protein-derived GLP-1-secreting peptides by CaSR activation-based molecular docking and their digestive stability

  • Food Chem. 2025 Feb 1;464(Pt 1):141569. doi: 10.1016/j.foodchem.2024.141569.
Mingkai Zhang 1,  Ling Zhu 2,  Hui Zhang 3,  Xingguo Wang 1,  Tongtong Liu 1,  Gangcheng Wu 1
Affiliations

Affiliations

  • 1 National Engineering Research Center for Functional Food, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.
  • 2 National Engineering Research Center for Functional Food, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China. Electronic address: zhuling@jiangnan.edu.cn.
  • 3 National Engineering Research Center for Functional Food, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China. Electronic address: zhanghui@jiangnan.edu.cn.
PMID: 39418954 DOI: 10.1016/j.foodchem.2024.141569
Abstract

Dietary proteins could stimulate Glucagon-like peptide 1 (GLP-1) secretion. However, only a few food-derived GLP-1-secreting Peptides have been identified. Herein, three GLP-1-secreting Peptides were identified from pea protein hydrolysate (PPH) by calcium-sensing receptor (CaSR) activation-based molecular docking. PPH-triggered GLP-1 secretion was mediated by CaSR activation. A total of 4221 Peptides were sequenced from PPH through peptidomic analysis. Subsequently, three GLP-1-secreting Peptides, including RFY, FEPF, and FLFK, were screened by CaSR activation-based molecular docking, and peptide-induced GLP-1 secretion were mediated by CaSR activation. More importantly, FEPF and FLFK exhibited good digestive stability. The molecular docking suggested that binding energy between Peptides and CaSR was negatively correlated with their ability to stimulate GLP-1 secretion, and some binding sites in CaSR, such as Asn102 and Tyr218, play a crucial role in stimulating GLP-1 secretion. Our findings suggest that the targeted discovery of pea protein-derived GLP-1-secreting Peptides through CaSR activation-based molecular docking is an effective strategy.

Keywords

CaSR; GLP-1; Molecular docking; Peptides.

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