羟乙基淀粉130/0.4引起的载脂蛋白A-I结构变化揭示潜在的毒性机制

IF 1.4 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Lingyan Qu, Liqun Jia, Jianzhong Zhang, Shuqin Ni
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引用次数: 0

摘要

6%羟乙基淀粉(HES 130/0.4)经常用于解决低血容量,确保足够的器官灌注和氧气运输。在280、295和310 k三种温度下,通过几种光谱技术研究了载脂蛋白A-I (ApoA-I)的影响,以探索其与静脉中主要蛋白的可能相互作用。实验结果表明,HES 130/0.4有效地抑制了APOA-I的固有荧光。我们还评估了结合位点、结合常数和热力学参数,结果表明HES 130/0.4在体温下可以通过氢键和范德华作用(ΔG = - 1.93 × 104 J·mol-1, ΔH = - 5.63 × 104 J·mol-1, ΔS = - 119 J·mol-1 K -1)与apoa -1自发结合,结合位点单一,结合力(n = 1.03和KA = 1.78 × 103 M-1)。此外,在HES 130/0.4的存在下,APOA-I的结构也发生了显著变化。血液中Ca2+和Fe3+会缩短贮藏时间。本研究为阐明HES 130/0.4与APOA-I的体外结合机制提供了准确、全面的基础数据,有助于理解其在血液转运和分布过程中对蛋白质功能的影响和毒性机制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Structural Changes of Apolipoprotein A-I Caused by Hydroxyethyl Starch 130/0.4 Reveals Potential Toxic Mechanisms

Structural Changes of Apolipoprotein A-I Caused by Hydroxyethyl Starch 130/0.4 Reveals Potential Toxic Mechanisms

6% hydroxyethyl starch (HES 130/0.4) is frequently employed to address hypovolemia, ensuring sufficient organ perfusion and oxygen transport. The effects on Apolipoprotein A-I (ApoA-I) were examined at three temperatures—280, 295, and 310 K—through several spectroscopic techniques to explore its possible interaction with the predominant protein in veins. The experimental findings indicated that HES 130/0.4 efficiently extinguished the intrinsic fluorescence of APOA-I. We also assessed the binding sites, binding constant, and thermodynamic parameters, which indicated that HES 130/0.4 can spontaneously associate with APOA-I via hydrogen bonds and van der Waals interactions (ΔG =  − 1.93 × 104 J·mol−1, ΔH =  − 5.63 × 104 J mol⁻1, and ΔS =  − 119 J mol⁻1 K⁻1) with a single binding site and week binding forces (n = 1.03 and KA = 1.78 × 103 M−1) at body temperature. Moreover, the structure of APOA-I was significantly altered in the presence of HES 130/0.4. Blood Ca2+ and Fe3+ will diminish the storage duration. The study provides accurate and thorough foundational data to clarify the binding mechanisms of HES 130/0.4 with APOA-I in vitro, which may help the comprehension of its impact on protein function and toxic mechanism during transit and distribution in the bloodstream.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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