{"title":"分子对接和转录组分析揭示肌球蛋白衍生肽激活 hT2R1 苦味受体的机制","authors":"","doi":"10.1016/j.fbio.2024.105067","DOIUrl":null,"url":null,"abstract":"<div><p>To better understand the bitterness effect and molecule mechanism of myosin-derived peptides activating bitter receptors, the interaction between myosin-derived peptides of dry-cured ham and bitter receptors was investigated by molecular docking and molecular dynamics simulation; the signal transduction mechanism of myosin-derived peptides was explored by HEK-293T cells using calcium imaging and transcriptomics analysis. Lower CDOCKER energy was observed during the interaction between myosin-derived peptides and hT2R1 by molecular docking compared with hT2R4, hT2R5, hT2R8, hT2R14 and hT2R16. Hydrogen bonds and hydrophobic interaction were the most important interaction forces which stabilized the interaction of hT2R1 and myosin-derived peptides. Compared with LEKEKSELK and TEELEEAKK, the RMSF values and EC<sub>50</sub> values of HVLATLGEK were lower, indicating that hT2R1 was more sensitive to HVLATLGEK stimulation. Transcriptomics and KEGG analyses showed that 767 differentially expressed genes were found and mainly involved in cAMP signaling pathway, neuroactive ligand-receptor interaction, calcium signaling pathway and MAPK signaling pathway after stimulating of HVLATLGEK. Protein-protein interaction network further demonstrated that DDIT3, FOS, FOSB, MYC, EGR1 and CCN2 were the key genes to connect the six functional clusters including ligand-receptor interaction and signal transduction.</p></div>","PeriodicalId":12409,"journal":{"name":"Food Bioscience","volume":null,"pages":null},"PeriodicalIF":4.8000,"publicationDate":"2024-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Molecular docking and transcriptomic analysis reveal the mechanism of myosin-derived peptides activating bitter receptor of hT2R1\",\"authors\":\"\",\"doi\":\"10.1016/j.fbio.2024.105067\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>To better understand the bitterness effect and molecule mechanism of myosin-derived peptides activating bitter receptors, the interaction between myosin-derived peptides of dry-cured ham and bitter receptors was investigated by molecular docking and molecular dynamics simulation; the signal transduction mechanism of myosin-derived peptides was explored by HEK-293T cells using calcium imaging and transcriptomics analysis. Lower CDOCKER energy was observed during the interaction between myosin-derived peptides and hT2R1 by molecular docking compared with hT2R4, hT2R5, hT2R8, hT2R14 and hT2R16. Hydrogen bonds and hydrophobic interaction were the most important interaction forces which stabilized the interaction of hT2R1 and myosin-derived peptides. Compared with LEKEKSELK and TEELEEAKK, the RMSF values and EC<sub>50</sub> values of HVLATLGEK were lower, indicating that hT2R1 was more sensitive to HVLATLGEK stimulation. Transcriptomics and KEGG analyses showed that 767 differentially expressed genes were found and mainly involved in cAMP signaling pathway, neuroactive ligand-receptor interaction, calcium signaling pathway and MAPK signaling pathway after stimulating of HVLATLGEK. Protein-protein interaction network further demonstrated that DDIT3, FOS, FOSB, MYC, EGR1 and CCN2 were the key genes to connect the six functional clusters including ligand-receptor interaction and signal transduction.</p></div>\",\"PeriodicalId\":12409,\"journal\":{\"name\":\"Food Bioscience\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2024-09-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Bioscience\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2212429224014974\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Bioscience","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2212429224014974","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Molecular docking and transcriptomic analysis reveal the mechanism of myosin-derived peptides activating bitter receptor of hT2R1
To better understand the bitterness effect and molecule mechanism of myosin-derived peptides activating bitter receptors, the interaction between myosin-derived peptides of dry-cured ham and bitter receptors was investigated by molecular docking and molecular dynamics simulation; the signal transduction mechanism of myosin-derived peptides was explored by HEK-293T cells using calcium imaging and transcriptomics analysis. Lower CDOCKER energy was observed during the interaction between myosin-derived peptides and hT2R1 by molecular docking compared with hT2R4, hT2R5, hT2R8, hT2R14 and hT2R16. Hydrogen bonds and hydrophobic interaction were the most important interaction forces which stabilized the interaction of hT2R1 and myosin-derived peptides. Compared with LEKEKSELK and TEELEEAKK, the RMSF values and EC50 values of HVLATLGEK were lower, indicating that hT2R1 was more sensitive to HVLATLGEK stimulation. Transcriptomics and KEGG analyses showed that 767 differentially expressed genes were found and mainly involved in cAMP signaling pathway, neuroactive ligand-receptor interaction, calcium signaling pathway and MAPK signaling pathway after stimulating of HVLATLGEK. Protein-protein interaction network further demonstrated that DDIT3, FOS, FOSB, MYC, EGR1 and CCN2 were the key genes to connect the six functional clusters including ligand-receptor interaction and signal transduction.
Food BioscienceBiochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
6.40
自引率
5.80%
发文量
671
审稿时长
27 days
期刊介绍:
Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.