Discovery and functional mechanism of novel dipeptidyl peptidase IV inhibitory peptides from Chinese traditional fermented fish (Chouguiyu)
文献类型： 外文期刊
作者： Yang, Daqiao 1 ; Li, Chunsheng 1 ; Li, Laihao 1 ; Wang, Yueqi 1 ; Chen, Shengjun 1 ; Zhao, Yongqiang 1 ; Hu, Xiao 1 ; Rong, Hui 1 ;
作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Natl R&D Ctr Aquat Prod Proc, Key Lab Aquat Prod Proc,Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China
2.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China
3.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China
4.Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China
关键词： Chouguiyu; Dipeptidyl peptidase-IV; Peptide; Molecular docking; Hydrophobicity; Hydrogen bond
期刊名称：CURRENT RESEARCH IN FOOD SCIENCE （ 影响因子：6.269； 五年影响因子：6.288 ）
ISSN：
年卷期： 2022 年 5 卷
页码：
收录情况： SCI
摘要： Dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides from fermented foods exhibit great potential to alleviate type 2 diabetes mellitus (T2DM). In this study, the DPP-IV inhibition activity of peptide extract from Chouguiyu was obviously enhanced after 4-8 d fermentation. A total of 125 DPP-IV inhibitory peptides in Chouguiyu were identified by peptidomics and were obtained from 46 precursor proteins, mainly including nebulin, titin, muscle -type creatine kinase, hemoglobin, and actin. After molecular docking with DPP-IV, four novel DPP-IV inhibitory peptides possessing the lowest docking energy were selected, including EPAEAVGDWR (D37), IPHESVDVIK (D22), PDLSKHNNHM (D35), and PFGNTHNNFK (D1). The DPP-IV inhibition activity of D37, D22, D35, and D1 were further verified after synthesis with the IC50 of 0.10 mM, 2.69 mM, 3.88 mM, and 8.51 mM, respectively, in accordance with their docking energies. Energy interaction showed that the structures of EP-, IPH-,-NHM, and PF-in these peptides were easy to connect with DPP-IV enzyme through hydrogen bond, salt bridge, and alkyl. The surface force including the H-bond interaction, hydrophobicity, aromatic interaction, and SAS, played a major role in the interaction between DPP-IV enzyme and peptides. The peptides that possess high hydropho-bicity and can form strong hydrogen bond and salt bridge are potential DPP-IV inhibitory peptides using for T2DM remission.
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