Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-β region
作者:, Masaki Okumura
摘要:Abstract Amyloid fibrils are fibrous protein assemblies with distinctive cross-β structures. For amyloidosis, there are disease-associated mutations outside of the cross-β structures. Thus, it is necessary to elucidate the role of peripheral sequences outside the cross-β structure. Amyloid fibrils are generally 10 nm in width; however, the amyloid fibrils of truncated barnase M1 peptides missing the C-terminal sequence outside the cross-β structure are 20 nm in width. In this study, we performed comparative analysis of the structural stability of amyloids formed by the respective peptides. We found that the C-terminal amino acids dramatically affect the conformational instability in the presence of a denaturing reagent.
关键词:Amyloid; Dynamic light scattering; Peripheral; Cross-β; Thioflavin T
论文方向:[{"id":13,"name":"细胞生物学"},{"id":879,"name":"生物化学"}]
发表期刊:FEBS Letters Volume 589, Issue 23
发表时间:Mon Nov 30 00:00:00 CST 2015
数字识别码:10.1016/j.febslet.2015.10.015
是否作者本人: 否
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