文献类型：期刊文献

英文题名：Screening of salty peptides from enzymatic hydrolysates of Meretrix lyrata based on interaction with the TMC4 receptor

作者：Song, Chunyong[1,2];Zhao, Zhihang[1,2];Tan, Mingtang[1,2];Chen, Zhongqin[1,2];Zheng, Huina[1,2];Gao, Jialong[1,2];Lin, Haisheng[1,2];Qin, Xiaoming[1,2];Cao, Wenhong[1,2]

机构：[1]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Natl Res & Dev Branch Ctr Shellfish Proc Zhanjiang, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China

年份：2025

卷号：218

外文期刊名：FOOD RESEARCH INTERNATIONAL

收录：SCI-EXPANDED(收录号：WOS:001521512800006)、、EI(收录号：20252518650452)、Scopus(收录号：2-s2.0-105008514233)、WOS

基金：This work was supported by the Shenzhen Science and Technology Program (JCYJ20230807120316033) and the Modern Agricultural In-dustry Technology Research System of China (CARS-49) . We gratefully acknowledge the anonymous referees for the comments and construc-tive suggestions provided for improving the manuscript.

语种：英文

外文关键词：Meretrix lyrata; Salty peptides; Salty receptor; Molecular docking; Key binding sites; Thermodynamic interactions

外文摘要：To elucidate the salty mechanism of salty peptides, 152 salty peptides were rapidly screened from enzymatic hydrolysates of Meretrix lyrata based on interaction with the TMC4 receptor. The results revealed that these salty peptides are enriched in residues of Leu, Asp and Glu, with their N- and C-terminals primarily composed of hydrophobic and polar amino acid residues, which caused the acidic amino acid residues and their related sequences to become vital "salty sequences" within the peptides. Furthermore, salty peptides could notably alter TMC4 receptor's surface morphology, characterized by enhanced surface roughness. Salty peptides could primarily interact with TMC4 receptor via hydrogen and hydrophobic bonds, averaging binding energy of -7.3 kcal/mol. The residues Arg506, Leu520, Gln524, Glu525 and Gln527 were the key binding sites for hydrogen bonds, while Ile426 and Leu520 residues were the key binding sites for hydrophobic bonds. Similar to NaCl, four salty peptides demonstrated strong-affinity interaction with the TMC4 receptor, with affinity (Kd) ranging from 1.766 x 10- 7 to 3.427 x 10-6 M. Moreover, three salty peptides (TWDLL, EDFLLA and VDEVLRL) exhibited exceptional saltiness, equivalent in strength to the same NaCl concentration. These findings provide new perspectives for studying the interaction between salty peptides and salty receptors.