Albumin Folding Changes Affect the Microfluidic Interfacial Broadening Revealed by Surface Plasmon Resonance

IF 6.1 Q1 CHEMISTRY, MULTIDISCIPLINARY
Damiano Calcagno, Maria Luisa Perina, Alessia Distefano, Mariacristina Parravano, Antonino Licciardello, Nunzio Tuccitto, Giuseppe Grasso
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Abstract

Understanding the conformation and diffusion behavior of proteins in biological fluids is crucial for advancements in conformational disease research. While several experimental techniques are available for probing protein conformations, they often come with limitations, such as the need for fluorophores or specific experimental conditions. Albumin, one of the most abundant proteins in the blood and used as a tear supplement in treating ocular surface disorders, plays a vital role as a transport protein, binding various ligands and facilitating their transport. However, the direct relationship between albumin conformation and diffusion coefficient (D) in water solutions remains unexplored. In this study, we describe a novel Surface Plasmon Resonance technique coupled with Stochastic Gillespie′s algorithm simulations to correlate albumin D values with its conformational states directly. Our findings demonstrate the feasibility of monitoring albumin conformational changes under different environmental conditions, as well as its degradation kinetics by trypsin, by analyzing its diffusion characteristics, presenting a promising avenue for advancing our understanding of conformational diseases.

Abstract Image

白蛋白折叠变化影响表面等离子体共振显示的微流体界面展宽
了解蛋白质在生物体液中的构象和扩散行为对于推进构象疾病的研究至关重要。虽然有几种实验技术可用于探测蛋白质构象,但它们往往有局限性,例如需要荧光团或特定的实验条件。白蛋白是血液中含量最丰富的蛋白质之一,在治疗眼表疾病中被用作泪液补充剂。白蛋白作为一种转运蛋白,结合各种配体并促进其运输,起着至关重要的作用。然而,白蛋白构象与水溶液中扩散系数(D)之间的直接关系尚不清楚。在这项研究中,我们描述了一种新的表面等离子体共振技术,结合随机吉莱斯皮算法模拟,将白蛋白D值与其构象状态直接关联起来。通过分析白蛋白的扩散特性,我们的研究结果证明了在不同环境条件下监测白蛋白构象变化的可行性,以及它被胰蛋白酶降解的动力学,为提高我们对构象疾病的理解提供了一条有希望的途径。
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
CiteScore
7.30
自引率
0.00%
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