Oyster-derived peptides as pancreatic lipase inhibitors: Kinetics, molecular interactions, and gastrointestinal stability
文献类型： 外文期刊
作者： Chen, Hui 1 ; Dong, Xiting 1 ; Zhao, Yongqiang 2 ; Zhou, Xuxia 1 ; Zhou, Mengyuan 1 ; Xu, Zhihao 1 ; Xu, Zhe 5 ;
作者机构： 1.Zhejiang Univ Technol, Coll Food Sci & Technol, Hangzhou 310014, Zhejiang, Peoples R China
2.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China
3.Zhejiang Key Lab Green Low carbon & Efficient Dev, Hangzhou 310014, Peoples R China
4.Natl R&D Branch Ctr Pelag Aquat Prod Proc Hangzhou, Hangzhou 310014, Peoples R China
5.Dalian Minzu Univ, Coll Life Sci, Key Lab Biotechnol & Bioresources Utilizat, Minist Educ, Dalian 116600, Peoples R China
关键词： Oyster peptide; pancreatic lipase; inhibition mechanism; Molecular docking
期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）
ISSN： 2212-4292
年卷期： 2025 年 63 卷
页码：
收录情况： SCI
摘要： In this study, oyster peptide sequences with potential inhibitory activity against pancreatic lipase were screened using molecular docking. Inhibition kinetics, ultraviolet and fluorescence spectroscopy, circular dichroism, and in vitro simulated digestion were employed to investigate the inhibitory mechanism and gastrointestinal stability of the peptides NGDAGMV (P-N) and EAGAGGL (P-E) on pancreatic lipase (PL). The results demonstrated that both P-N and P-E could effectively inhibit PL activity, with IC50 values of 3.122 and 5.781 mmol/L, respectively. The inhibition type was non-competitive. P-N can alter the covalent structure of PL through charge interactions, hydrogen bonding, C-H bonds, pi-sulfur bonds, and pi-alkyl bonds. Meanwhile, P-E can efficiently quench the intrinsic fluorescence of PL and change its secondary structure primarily through static quenching mediated by salt bridges, hydrogen bonds, C-H bonds, and alkyl bonds. This study provides a theoretical basis for using oyster peptides as natural PL inhibitors.
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