Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation
文献类型： 外文期刊
作者： Li, Wen 1 ; Sun, Shuai 2 ; Chen, Wanchao 1 ; Ma, Haile 2 ; Li, Tingzhao 3 ; Zhang, Zhong 1 ; Wu, Di 1 ; Yan, Mengqiu 1 ; Yang, Yan 1 ;
作者机构： 1.Shanghai Acad Agr Sci, Inst Edible Fungi, Natl Engn Res Ctr Edible Fungi, Minist Agr & Rural Affairs,Key Lab Edible Fungi Re, Shanghai 201403, Peoples R China
2.Jiangsu Univ, Inst Food Phys Proc, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China
3.Amway Shanghai Innovat & Sci Co Ltd, Shanghai 201203, Peoples R China
4.Amway China Bot R&D Ctr, Wuxi 214115, Peoples R China
关键词： Salty peptide; Molecular docking; Biolayer interferometry; Isothermal titration calorimetry
期刊名称：FOOD SCIENCE AND HUMAN WELLNESS （ 影响因子：7.0； 五年影响因子：8.3 ）
ISSN：
年卷期： 2024 年 13 卷 4 期
页码：
收录情况： SCI
摘要： The taste presentation and receptor perception mechanism of the salty peptide of Stropharia rugosoannulata were predicted and verified using peptide omics and molecular interaction techniques. The combination of aspartic acid (D) and glutamic acid (E), or peptide fragments composed of arginine (R), constitute the characteristic taste structural basis of salty peptides of S. rugosoannulata. The taste intensity of the salty peptide positively correlates with its concentration within a specific concentration range (0.25-1.0 mg/mL). The receptor more easily recognizes the first amino acid residue at the N-terminal of salty peptides and the aspartic acid residue in the peptides. GLU513, ASP707, and VAL508 are the critical amino acid residues for the receptor to recognize salty peptides. TRPV1 is specifically the receptor for recognizing salty peptides. Hydrogen bonds and electrostatic interactions are the main driving forces for the interactions between salty peptides and TRPV1 receptors. KSWDDFFTR has the most potent binding capacity with the receptor and has tremendous potential for application in sodium salt substitution. This study confirmed the taste receptor that specifi cally recognizes salty peptides, analyzed the receptor-peptide binding interaction, and provided a new idea for understanding the taste receptor perception of salty peptides. (c) 2024 Beijing Academy of Food Sciences. Publishing services by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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