来自牛巩膜的肽-蛋白质复合物：结构方面及伴侣活性。

Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity.

作者信息

Ilyina Anna P, Sidorsky Egor V, Tregubov Artem V, Chekova Valeria M, Elistratov Pavel A, Yamskova Viktoria P, Yamskov Igor A

机构信息

Institute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, Russia.

A.N.Nesmeyanov Institute of Organoelement Compounds of Russian Academy of Sciences, Russian Federation, St. Vavilova, 28, 119991, Moscow, Russia.

出版信息

Biochem Biophys Rep. 2020 Nov 25;24:100851. doi: 10.1016/j.bbrep.2020.100851. eCollection 2020 Dec.

DOI:10.1016/j.bbrep.2020.100851

PMID:33294633

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7701135/

Abstract

The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of conformational thermal transition (65 °C) was determined, after which the peptide-protein complex passes into a denatured stable state. It was found that the peptide-protein complex in aqueous solutions forms thermostable nanosized particles. It was shown that the peptide-protein complex isolated from cattle sclera shows the properties of chaperone, an inhibitor of model protein aggregation induced by dithiothreitol.

摘要

通过紫外光谱、圆二色光谱和动态光散射研究了温度和离液剂对从牛巩膜分离的肽 - 蛋白质复合物二级结构水平空间组织的影响。结果表明，该复合物具有高构象热稳定性。确定了构象热转变点（65°C），在此之后肽 - 蛋白质复合物转变为变性稳定状态。发现该肽 - 蛋白质复合物在水溶液中形成热稳定的纳米颗粒。结果表明，从牛巩膜分离的肽 - 蛋白质复合物具有伴侣蛋白的特性，是二硫苏糖醇诱导的模型蛋白聚集的抑制剂。