膜结合脂肪酸及其结合蛋白之间相互作用机制的实验和理论研究:研究脂质酰基链与蛋白质接触行为的模型系统

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Shigeru Sugiyama , Daisuke Matsuoka , Toshiaki Hara , Masashi Sonoyama , Shigeru Matsuoka , Michio Murata
{"title":"膜结合脂肪酸及其结合蛋白之间相互作用机制的实验和理论研究:研究脂质酰基链与蛋白质接触行为的模型系统","authors":"Shigeru Sugiyama ,&nbsp;Daisuke Matsuoka ,&nbsp;Toshiaki Hara ,&nbsp;Masashi Sonoyama ,&nbsp;Shigeru Matsuoka ,&nbsp;Michio Murata","doi":"10.1016/j.chemphyslip.2022.105227","DOIUrl":null,"url":null,"abstract":"<div><p><span><span>The interaction of proteins with hydrophobic ligands in biological membranes<span> is an important research topic in the life sciences. The hydrophobic nature of ligands, especially their lack of water solubility, often makes it difficult to experimentally investigate their interactions with proteins, thus hampering quantitative evaluation based on thermodynamic parameters. The fatty acid-binding proteins, particularly FABP3, discussed in this review can recognize fatty acids, a primary component of </span></span>membrane lipids<span><span><span>, with high affinity. The precise three-dimensional structure of fatty acids and related ligands bound in FABP3 and their interaction with the binding pocket will contribute to the understanding of accurately determining physicochemical factors that cause the expression of affinity between protein surfaces and </span>lipids in biological membranes. During the research of FABP3, we encountered many of the problems that were widely implicated in experiments dealing with hydrophobic ligands. To address these issues, we developed experimental methodologies using X-ray crystallography, </span>calorimetry, and </span></span>surface plasmon resonance<span>. Using these methods and computational approaches, we have obtained several insights into the interaction of hydrophobic ligands with protein binding sites. Structural and functional studies of FABP potentially lead to a better understanding of the interaction between lipids and proteins, and thus, this protein may provide one of the model systems for investigating substance transport across cell membranes and inner membrane systems.</span></p></div>","PeriodicalId":275,"journal":{"name":"Chemistry and Physics of Lipids","volume":"247 ","pages":"Article 105227"},"PeriodicalIF":3.4000,"publicationDate":"2022-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Experimental and theoretical investigations into the mechanism of interactions between membrane-bound fatty acids and their binding protein: A model system to investigate the behavior of lipid acyl chains in contact with proteins\",\"authors\":\"Shigeru Sugiyama ,&nbsp;Daisuke Matsuoka ,&nbsp;Toshiaki Hara ,&nbsp;Masashi Sonoyama ,&nbsp;Shigeru Matsuoka ,&nbsp;Michio Murata\",\"doi\":\"10.1016/j.chemphyslip.2022.105227\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span><span>The interaction of proteins with hydrophobic ligands in biological membranes<span> is an important research topic in the life sciences. The hydrophobic nature of ligands, especially their lack of water solubility, often makes it difficult to experimentally investigate their interactions with proteins, thus hampering quantitative evaluation based on thermodynamic parameters. The fatty acid-binding proteins, particularly FABP3, discussed in this review can recognize fatty acids, a primary component of </span></span>membrane lipids<span><span><span>, with high affinity. The precise three-dimensional structure of fatty acids and related ligands bound in FABP3 and their interaction with the binding pocket will contribute to the understanding of accurately determining physicochemical factors that cause the expression of affinity between protein surfaces and </span>lipids in biological membranes. During the research of FABP3, we encountered many of the problems that were widely implicated in experiments dealing with hydrophobic ligands. To address these issues, we developed experimental methodologies using X-ray crystallography, </span>calorimetry, and </span></span>surface plasmon resonance<span>. Using these methods and computational approaches, we have obtained several insights into the interaction of hydrophobic ligands with protein binding sites. Structural and functional studies of FABP potentially lead to a better understanding of the interaction between lipids and proteins, and thus, this protein may provide one of the model systems for investigating substance transport across cell membranes and inner membrane systems.</span></p></div>\",\"PeriodicalId\":275,\"journal\":{\"name\":\"Chemistry and Physics of Lipids\",\"volume\":\"247 \",\"pages\":\"Article 105227\"},\"PeriodicalIF\":3.4000,\"publicationDate\":\"2022-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chemistry and Physics of Lipids\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S000930842200055X\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemistry and Physics of Lipids","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S000930842200055X","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 1

摘要

生物膜中蛋白质与疏水配体的相互作用是生命科学领域的一个重要研究课题。由于配体的疏水性,尤其是它们缺乏水溶性,因此很难通过实验研究它们与蛋白质的相互作用,从而阻碍了基于热力学参数的定量评价。本文讨论的脂肪酸结合蛋白,特别是FABP3,可以识别膜脂的主要成分脂肪酸,具有很高的亲和力。结合在FABP3上的脂肪酸和相关配体的精确三维结构及其与结合袋的相互作用将有助于准确确定导致生物膜中蛋白质表面与脂质亲和性表达的理化因素。在FABP3的研究过程中,我们遇到了许多在疏水配体实验中广泛涉及的问题。为了解决这些问题,我们开发了使用x射线晶体学、量热法和表面等离子体共振的实验方法。利用这些方法和计算方法,我们对疏水配体与蛋白质结合位点的相互作用有了一些了解。FABP的结构和功能研究可能有助于更好地理解脂质与蛋白质之间的相互作用,因此,该蛋白可能为研究物质跨细胞膜和内膜系统的转运提供一个模型系统。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Experimental and theoretical investigations into the mechanism of interactions between membrane-bound fatty acids and their binding protein: A model system to investigate the behavior of lipid acyl chains in contact with proteins

The interaction of proteins with hydrophobic ligands in biological membranes is an important research topic in the life sciences. The hydrophobic nature of ligands, especially their lack of water solubility, often makes it difficult to experimentally investigate their interactions with proteins, thus hampering quantitative evaluation based on thermodynamic parameters. The fatty acid-binding proteins, particularly FABP3, discussed in this review can recognize fatty acids, a primary component of membrane lipids, with high affinity. The precise three-dimensional structure of fatty acids and related ligands bound in FABP3 and their interaction with the binding pocket will contribute to the understanding of accurately determining physicochemical factors that cause the expression of affinity between protein surfaces and lipids in biological membranes. During the research of FABP3, we encountered many of the problems that were widely implicated in experiments dealing with hydrophobic ligands. To address these issues, we developed experimental methodologies using X-ray crystallography, calorimetry, and surface plasmon resonance. Using these methods and computational approaches, we have obtained several insights into the interaction of hydrophobic ligands with protein binding sites. Structural and functional studies of FABP potentially lead to a better understanding of the interaction between lipids and proteins, and thus, this protein may provide one of the model systems for investigating substance transport across cell membranes and inner membrane systems.

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
Chemistry and Physics of Lipids
Chemistry and Physics of Lipids 生物-生化与分子生物学
CiteScore
7.60
自引率
2.90%
发文量
50
审稿时长
40 days
期刊介绍: Chemistry and Physics of Lipids publishes research papers and review articles on chemical and physical aspects of lipids with primary emphasis on the relationship of these properties to biological functions and to biomedical applications. Accordingly, the journal covers: advances in synthetic and analytical lipid methodology; mass-spectrometry of lipids; chemical and physical characterisation of isolated structures; thermodynamics, phase behaviour, topology and dynamics of lipid assemblies; physicochemical studies into lipid-lipid and lipid-protein interactions in lipoproteins and in natural and model membranes; movement of lipids within, across and between membranes; intracellular lipid transfer; structure-function relationships and the nature of lipid-derived second messengers; chemical, physical and functional alterations of lipids induced by free radicals; enzymatic and non-enzymatic mechanisms of lipid peroxidation in cells, tissues, biofluids; oxidative lipidomics; and the role of lipids in the regulation of membrane-dependent biological processes.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信