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

IF 4.8 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Food Bioscience Pub Date : 2024-09-07 DOI:10.1016/j.fbio.2024.105067
{"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}
引用次数: 0

摘要

为了更好地理解肌球蛋白衍生肽激活苦味受体的苦味效应和分子机制,通过分子对接和分子动力学模拟研究了干腌火腿肌球蛋白衍生肽与苦味受体的相互作用;利用钙成像和转录组学分析,通过HEK-293T细胞探讨了肌球蛋白衍生肽的信号转导机制。与 hT2R4、hT2R5、hT2R8、hT2R14 和 hT2R16 相比,通过分子对接观察到肌球蛋白衍生肽与 hT2R1 的相互作用过程中 CDOCKER 能量较低。氢键和疏水作用是稳定 hT2R1 与肌球蛋白衍生肽相互作用的最重要作用力。与 LEKEKSELK 和 TEELEEAKK 相比,HVLATLGEK 的 RMSF 值和 EC50 值较低,表明 hT2R1 对 HVLATLGEK 的刺激更为敏感。转录组学和KEGG分析表明,HVLATLGEK刺激后发现了767个差异表达基因,主要涉及cAMP信号通路、神经活性配体-受体相互作用、钙信号通路和MAPK信号通路。蛋白质-蛋白质相互作用网络进一步表明,DDIT3、FOS、FOSB、MYC、EGR1 和 CCN2 是连接配体-受体相互作用和信号转导等六个功能簇的关键基因。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

摘要图片

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Food Bioscience
Food Bioscience Biochemistry, 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.
期刊最新文献
Potential applications of antimicrobial peptides from edible insects in the food supply chain: Uses in agriculture, packaging, and human nutrition Electron beam and X-ray irradiation promote extraction of bioactive compounds from walnut green husk: Structural, physicochemical, and functional properties Identification and in silico screening of novel angiotensin-converting enzyme inhibitory peptides from pacific saury: Interaction mechanism, network pharmacology, stability, Caco-2 monolayer transport Pasting, rheology, structural properties and in vitro digestibility of potato starch complexes co-gelatinized with squash polysaccharides Theabrownin, gut microbiota, and obesity: Effects and mechanisms
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1