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催化淀粉样蛋白聚集体氧化行为的筛选

Screening of oxidative behavior in catalytic amyloid assemblies.

作者信息

Marshall Liam R, Korendovych Ivan V

机构信息

Department of Chemistry and Biochemistry, Baylor University, Waco, TX, United States.

Department of Chemistry and Biochemistry, Baylor University, Waco, TX, United States.

出版信息

Methods Enzymol. 2024;697:15-33. doi: 10.1016/bs.mie.2024.01.020. Epub 2024 Mar 19.

Abstract

Once considered a thermodynamic minimum of the protein fold or as simply by-products of a misfolding process, amyloids are increasingly showing remarkable potential for promoting enzyme-like catalysis. Recent studies have demonstrated a diverse range of catalytic behaviors that amyloids can promote way beyond the hydrolytic behaviors originally reported. We and others have demonstrated the strong propensity of catalytic amyloids to facilitate redox reactions both in the presence and in the absence of metal cofactors. Here, we present a detailed protocol for measuring the oxidative ability of supramolecular peptide assemblies.

摘要

淀粉样蛋白曾一度被认为是蛋白质折叠的热力学最小值,或者仅仅是错误折叠过程的副产物,但它们越来越显示出在促进类酶催化方面的显著潜力。最近的研究表明,淀粉样蛋白能促进的催化行为多种多样,远远超出了最初报道的水解行为。我们和其他人已经证明,催化性淀粉样蛋白在有和没有金属辅因子的情况下都有促进氧化还原反应的强烈倾向。在这里,我们提供了一个详细的方案,用于测量超分子肽组装体的氧化能力。

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