期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 21, 页码 -出版社
MDPI
DOI: 10.3390/ijms232113441
关键词
human cystatin C; oligomer; amyloid; small-angle X-ray scattering; dynamic light scattering
资金
- National Science Centre (Poland) [2017/27/B/ST4/00485]
This study characterized the oligomeric states of human cystatin C in different pH conditions, revealing the ability to form tetramers at low pH and dissociate into dimers at neutral pH.
Human cystatin C (HCC), an amyloidogenic protein, forms dimers and higher oligomers (trimers, tetramers and donut like large oligomers) via a domain-swapping mechanism. The aim of this study was the characterization of the HCC oligomeric states observed within the pH range from 2.2 to 10.0 and also in conditions promoting oligomerization. The HCC oligomeric forms obtained in different conditions were characterized using size exclusion chromatography, dynamic light scattering and small-angle X-ray scattering. The marked ability of HCC to form tetramers at low pH (2.3 or 3.0) and dimers at pH 4.0-5.0 was observed. HCC remains monomeric at pH levels above 6.0. Based on the SAXS data, the structure of the HCC tetramer was proposed. Changes in the environment (from acid to neutral) induced a breakdown of the HCC tetramers to dimers. The tetrameric forms of human cystatin C are formed by the association of the dimers without a domain-swapping mechanism. These observations were confirmed by their dissociation to dimers at pH 7.4.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据