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Understanding how natural sequence variation in serum albumin proteins affects conformational stability and protein adsorption

圆二色性 吸附 化学 牛血清白蛋白 蛋白质吸附 衰减全反射 人血清白蛋白 石英晶体微天平 高分子 血清白蛋白 表面等离子共振 生物物理学 动态光散射 结晶学 蛋白质结构 红外光谱学 生物化学 材料科学 物理化学 生物 纳米技术 有机化学 纳米颗粒
作者
Gamaliel Junren,Abdul Rahim Ferhan,Tun Naw Sut,Joshua A. Jackman,Nam‐Joon Cho
出处
期刊:Colloids and Surfaces B: Biointerfaces [Elsevier]
卷期号:194: 111194-111194 被引量:22
标识
DOI:10.1016/j.colsurfb.2020.111194
摘要

Serum albumins are evolutionary conserved proteins that are found in many animal species, and purified forms are widely used in biotechnology applications, such as components within surface passivation coatings and drug delivery systems. As such, there has long been interest in studying how serum albumins adsorb onto solid supports, although existing studies are limited to one or two species. Herein, we comprehensively investigated three serum albumins of bovine (BSA), human (HSA), and rat (RSA) origin, and discovered striking differences in their conformational stabilities and adsorption properties. Together with bioinformatics analysis, dynamic light scattering (DLS) and circular dichroism (CD) spectroscopy measurements revealed that the proteins form different types of macromolecular assemblies in solution. BSA and HSA existed as individual monomers while RSA formed multimers, and each protein exhibited sequence-dependent variations in conformational stability as well. Quartz crystal microbalance-dissipation (QCM-D) and localized surface plasmon resonance (LSPR) experiments further showed that BSA and HSA proteins adsorb to form well-packed adlayers, and the extent of protein uptake and spreading depended on their unique conformational stabilities. Conversely, RSA adsorption resulted in sparse adlayers and appreciably less spreading of the adsorbed multimers, as confirmed by attenuated total reflection Fourier-transform infrared (ATR-FTIR) spectroscopy experiments. Together, our findings demonstrate that significant differences in conformational stability and adsorption behavior exist even between evolutionary conserved serum albumins with high sequence and structural similarity and illustrate how rational engineering of protein structures and stabilities, guided by insights from nature, might be useful to design protein-based coatings for various biointerfacial science applications.
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