Protein–lipid acyl chain interactions: Depth-dependent changes of segmental mobility of phospholipid in contact with bacteriorhodopsin

IF 3.3 3区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biophysical chemistry Pub Date : 2024-02-22 DOI:10.1016/j.bpc.2024.107204

Yuichi Umegawa , Sho Kato , Sangjae Seo , Wataru Shinoda , Satoshi Kawatake , Shigeru Matsuoka , Michio Murata

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Abstract

Boundary lipids surrounding membrane proteins play an essential role in protein function and structure. These protein–lipid interactions are mainly divided into electrostatic interactions between the polar amino acids of proteins and polar heads of phospholipids, and hydrophobic interactions between protein transmembrane sites and phospholipid acyl chains. Our previous report (Kawatake et al., Biochim. Biophys. Acta 1858 [2016] 2106–2115) covered a method for selectively analyzing boundary lipid interactions and showed differences in membrane protein–peripheral lipid interactions due to differences in their head group. Interactions in the hydrophobic acyl chains of phospholipids are relatively consistent among proteins, but the details of these interactions have not been elucidated. In this study, we reconstituted bacteriorhodopsin as a model protein into phospholipid membranes labeled with ²H and ¹³C for solid-state NMR measurement to investigate the depth-dependent effect of the head group structure on the lipid bilayer. The results showed that the position of the phospholipid near the carbonyl carbon was affected by the head group in terms of selectivity for protein surfaces, whereas in the deep interior of the bilayer near the leaflet interface, there was little difference between the head groups, indicating that the dependence of their interactions on the head group was much reduced.

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蛋白质与脂质酰基链的相互作用：磷脂与细菌眼色素接触时段移动性随深度的变化。

膜蛋白周围的边界脂质对蛋白质的功能和结构起着至关重要的作用。这些蛋白质与脂质的相互作用主要分为蛋白质极性氨基酸与磷脂极性头之间的静电相互作用，以及蛋白质跨膜位点与磷脂酰基链之间的疏水相互作用。我们之前的报告（Kawatake 等人，Biochim. Biophys. Acta 1858 [2016] 2106-2115）介绍了一种选择性分析边界脂质相互作用的方法，并显示了膜蛋白与外围脂质相互作用因其头基团的不同而存在差异。磷脂疏水酰基链上的相互作用在蛋白质之间相对一致，但这些相互作用的细节尚未阐明。在本研究中，我们将细菌眼色素作为模型蛋白质重构到标记有 2H 和 13C 的磷脂膜中进行固态核磁共振测量，以研究头基结构对脂质双分子层的深度依赖性影响。结果表明，在靠近羰基碳的磷脂位置，头基对蛋白质表面的选择性受到影响，而在靠近小叶界面的双分子层深层内部，头基之间的差异不大，这表明它们之间的相互作用对头基的依赖性大大降低。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biophysical chemistry 生物-生化与分子生物学

CiteScore

6.10

自引率

10.50%

发文量

121

审稿时长

20 days

期刊介绍： Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.