Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation

Wen Li ¹Shuai Sun ²Wanchao Chen ³Haile Ma ⁴Tingzhao Li ⁵Zhong Zhang ³Di Wu ³Mengqiu Yan ³Yan Yang³

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作者信息

1. Institute of Edible Fungi,Shanghai Academy of Agricultural Sciences,National Engineering Research Center of Edible Fungi,Key Laboratory of Edible Fungi Resources and Utilization(South),Ministry of Agriculture and Rural Affairs,Shanghai 201403,China;School of Food & Biological Engineering,Institute of Food Physical Processing,Jiangsu University,Zhenjiang 212013,China
2. Amway(Shanghai)Innovation & Science Co.,Ltd.,Shanghai 201203,China
3. Institute of Edible Fungi,Shanghai Academy of Agricultural Sciences,National Engineering Research Center of Edible Fungi,Key Laboratory of Edible Fungi Resources and Utilization(South),Ministry of Agriculture and Rural Affairs,Shanghai 201403,China
4. School of Food & Biological Engineering,Institute of Food Physical Processing,Jiangsu University,Zhenjiang 212013,China
5. Amway(Shanghai)Innovation & Science Co.,Ltd.,Shanghai 201203,China;Amway(China)Botanical R&D Center,Wuxi 214115,China
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Abstract

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 specifically recognizes salty peptides,analyzed the receptor-peptide binding interaction,and provided a new idea for understanding the taste receptor perception of salty peptides.

Key words

Salty peptide/Molecular docking/Biolayer interferometry/Isothermal titration calorimetry

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基金项目

上海市自然科学基金(23ZR1426100)

SAAS program for Excellent Research Team(G202203)

出版年

2024

食品科学与人类健康(英文)

CSTPCD

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