蛋白质单层的形成:表面特征和蛋白质-蛋白质相互作用的综合作用。

IF 2.8 3区 化学 Q3 CHEMISTRY, PHYSICAL
Soft Matter Pub Date : 2025-04-29 DOI:10.1039/D4SM00912F
Paola Campione, Grazia ML Messina, Micaela Giannetti, Claudia Mazzuca and Antonio Palleschi
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引用次数: 0

摘要

蛋白质在固液界面的吸附研究是一个被广泛研究的研究领域,因为它与生物材料的应用有着重要的关系。在这篇文章中,我们详细描述了溶菌酶和人血清白蛋白之间的相互作用,这两种蛋白具有不同的电荷和结构,具有不同的表面,金或聚甲基丙烯酸甲酯,它们的疏水性和极化性不同。利用实验石英晶体微天平进行了吸附过程的实验,并进行了耗散监测和原子力显微镜结果的分子动力学模拟。在这篇文章中,实际上,分子动力学模拟已经通过考虑几种蛋白质在随机方向上,从溶液接近表面来进行。这样,在逼近过程中,不仅考虑了蛋白质与表面的相互作用,还考虑了溶剂分子和其他蛋白质的相互作用。此外,为了充分模拟表面,对于金表面,考虑了表面极化和化学吸附,同时提出了一个合适的新模型来描述聚甲基丙烯酸甲酯表面。所获得的数据使我们能够解释带负电荷的人血清白蛋白蛋白与金表面(带负电荷)的优先相互作用主要是由化学吸附和极化性驱动的,而带正电荷的溶菌酶则由于静电和疏水相互作用而优先吸附在聚甲基丙烯酸甲酯上。有趣的是,利用这些信息,我们已经阐明了关于两种蛋白质在由纳米孔阵列组成的纳米结构表面上的位移的具有挑战性的实验结果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Protein monolayer formation: the combined role of the surface features and protein–protein interactions†

Protein monolayer formation: the combined role of the surface features and protein–protein interactions†

The study of protein adsorption at solid–liquid interfaces is a widely investigated research field because of its crucial relevance in biomaterial applications. In this article we provide detailed characterization of the interaction between two proteins, lysozyme and human serum albumin, characterized by different charge and structures, with two surfaces, gold or poly(methyl methacrylate), which differ in hydrophobicity and polarizability. The adsorption process has been performed by implementing experimental quartz crystal microbalance with dissipation monitoring and atomic force microscopy results with tuned molecular dynamics simulations. In this article, in fact, molecular dynamic simulations have been performed by considering several proteins in random orientations, approaching the surface from the solution. In this way, during the approaching process, not only protein interaction with the surface but also solvent molecules and the other proteins have been taken into account. Furthermore, to adequately simulate the surfaces, with regard to the gold surface, surface polarization and chemisorption have been taken into account, while a suitable new model has been proposed to describe the poly(methyl methacrylate) surface. The data obtained enable us to explain that the preferred interaction of the negatively charged human serum albumin protein with the gold surface (negatively charged) is mainly driven by chemisorption and polarizability, while the positively charged lysozyme preferentially adsorbs on poly(methyl methacrylate) because of both electrostatic and hydrophobic interactions. Interestingly, using this information, we have elucidated the challenging experimental results concerning the displacement of the two proteins on nanostructured surfaces made up of nanowell arrays.

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来源期刊
Soft Matter
Soft Matter 工程技术-材料科学:综合
CiteScore
6.00
自引率
5.90%
发文量
891
审稿时长
1.9 months
期刊介绍: Soft Matter is an international journal published by the Royal Society of Chemistry using Engineering-Materials Science: A Synthesis as its research focus. It publishes original research articles, review articles, and synthesis articles related to this field, reporting the latest discoveries in the relevant theoretical, practical, and applied disciplines in a timely manner, and aims to promote the rapid exchange of scientific information in this subject area. The journal is an open access journal. The journal is an open access journal and has not been placed on the alert list in the last three years.
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