基于静电相互作用和疏水相互作用的羧基苯硼酸修饰壳聚糖低聚糖抑制胰岛素纤维化

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Biophysical chemistry Pub Date : 2024-04-08 DOI:10.1016/j.bpc.2024.107236
Xiangyuan Zhao , Chunyan Yang , Wei Liu , Ke Lu , Hao Yin
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引用次数: 0

摘要

通过将羧基苯硼酸(CPBA)与壳聚糖寡糖(COS)偶联,开发出了一种新型抑制剂--羧基苯硼酸修饰壳聚糖寡糖(COS-CPBA),用于抑制胰岛素纤维化。广泛的生物物理实验表明,COS-CPBA能减缓胰岛素的聚集,阻碍胰岛素从α-螺旋结构向β-片状结构的构象转变,改变胰岛素聚集体的形态,改变胰岛素的纤溶途径。研究人员提出了 COS-CPBA 抑制胰岛素纤维化的机制。它认为胰岛素分子通过疏水作用与 COS-CPBA 结合,而 COS-CPBA 中的正电荷基团对结合的胰岛素分子产生静电排斥力。这两种相反的作用力使胰岛素分子呈现扩展构象,阻碍了胰岛素从α-螺旋结构向纤维化所需的β-片状结构的构象转变,从而减缓了胰岛素的聚集,改变了胰岛素的纤维化途径。这些研究为开发更有效的淀粉样蛋白纤维化抑制剂提供了新思路。
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Inhibition of insulin fibrillation by carboxyphenylboronic acid-modified chitosan oligosaccharide based on electrostatic interactions and hydrophobic interactions

A novel inhibitor, carboxyphenylboronic acid-modified chitosan oligosaccharide (COS-CPBA), was developed by coupling carboxyphenylboronic acid (CPBA) with chitosan oligosaccharide (COS) to inhibit insulin fibrillation. Extensive biophysical assays indicated that COS-CPBA could decelerate insulin aggregation, hinder the conformational transition from α-helix to β-sheet structure, change the morphology of insulin aggregates and alter fibrillation pathway. A mechanism for the inhibition of insulin fibrillation by COS-CPBA was proposed. It considers that insulin molecules bind to COS-CPBA via hydrophobic interactions, while the positively charged groups in COS-CPBA exert electrostatic repulsion on the bound insulin molecules. These two opposite forces cause the insulin molecules to display extended conformations and hinder the conformational transition of insulin from α-helix to β-sheet structure necessary for fibrillation, thus decelerating aggregation and altering the fibrillation pathway of insulin. The studies provide novel ideas for the development of more effective inhibitors of amyloid fibrillation.

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来源期刊
Biophysical chemistry
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.
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