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大球盖菇肽基料中肽分子分布特性及特征呈味结构解析
图1 大球盖菇合成肽质谱及呈咸强度评价
大球盖菇咸味肽呈味及受体感知机制预测
图2 咸味肽ESPERPFL与TRPV1受体的分子对接结果
图3 大球盖菇咸味肽与TRPV1受体的分子对接3D空间构象图
大球盖菇咸味肽呈味及受体感知机制验证
图4 大球盖菇咸味肽与TRPV1受体分子互作动力学反应
图5 大球盖菇咸味肽与TRPV1受体分子互作热力学反应
Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation
Wen Lia,b,1, Shuai Sunc,1, Wanchao Chena, Haile Mab,*, Tingzhao Lic,d, Zhong Zhanga, Di Wua, Mengqiu Yana, Yan Yanga,*
a 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
b School of Food & Biological Engineering, Institute of Food Physical Processing, Jiangsu University, Zhenjiang 212013, China
c Amway (Shanghai) Innovation & Science Co., Ltd., Shanghai 201203, China
d Amway (China) Botanical R&D Center, Wuxi 214115, China
1 Both authors contributed equally.
*Corresponding author.
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.
LI W, SUN S, CHEN W C, et al. Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation[J]. Food Science and Human Wellness, 2024, 13(4): 2277-2288. DOI:10.26599/FSHW.2022.9250190.
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