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肌球蛋白结合蛋白-C 在体外形成类淀粉样聚集物。

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.

机构信息

Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.

Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.

出版信息

Int J Mol Sci. 2021 Jan 13;22(2):731. doi: 10.3390/ijms22020731.

DOI:10.3390/ijms22020731
PMID:33450960
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7828380/
Abstract

This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) found a rapid (5-10 min) formation of large (>2 μm) aggregates. sMyBP-C oligomers formed both at the initial 5-10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7-10 monomers. TEM and atomic force microscopy (AFM) showed sMyBP-C to form amorphous aggregates (and, to a lesser degree, fibrillar structures) exhibiting no toxicity on cell culture. X-ray diffraction of sMyBP-C aggregates registered reflections attributed to a cross-β quaternary structure. Circular dichroism (CD) showed the formation of the amyloid-like structure to occur without changes in the sMyBP-C secondary structure. The obtained results indicating a high in vitro aggregability of sMyBP-C are, apparently, a consequence of structural features of the domain organization of proteins of this family. Formation of pathological amyloid or amyloid-like sMyBP-C aggregates in vivo is little probable due to amino-acid sequence low identity (<26%), alternating ordered/disordered regions in the protein molecule, and S-S bonds providing for general stability.

摘要

这项工作研究了骨骼肌肌球蛋白结合蛋白-C（sMyBP-C）与肌节 A 盘内粗丝和细丝蛋白相互作用的体内聚集和淀粉样特性。动态光散射（DLS）和透射电子显微镜（TEM）发现，大（> 2μm）聚集体迅速（5-10 分钟）形成。在最初的 5-10 分钟和聚合 16 小时后，均形成 sMyBP-C 低聚物。小角度 X 射线散射（SAXS）和 DLS 表明 sMyBP-C 低聚物由 7-10 个单体组成。TEM 和原子力显微镜（AFM）显示 sMyBP-C 形成无毒性的无定形聚集体（以及在较小程度上形成纤维状结构）。sMyBP-C 聚集体的 X 射线衍射记录到归因于交叉-β四级结构的反射。圆二色性（CD）表明，在 sMyBP-C 二级结构没有变化的情况下，淀粉样结构的形成发生。显然，获得的表明 sMyBP-C 体外高聚集性的结果是由于该家族蛋白的结构域组织的结构特征所致。由于氨基酸序列低同一性（<26%）、蛋白分子中有序/无序区域的交替以及提供整体稳定性的 S-S 键，体内病理性淀粉样或淀粉样 sMyBP-C 聚集体的形成可能性很小。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/808f/7828380/060f729ec777/ijms-22-00731-g010.jpg
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