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Conformational stability of amyloid fibrils of β2-microglobulin probed by guanidine-hydrochloride-induced unfolding

Conformational stability of amyloid fibrils of β2-microglobulin probed by guanidine-hydrochloride-induced unfolding

Authors :
Yuji Goto
Hironobu Naiki
Azusa Okamoto
Takehiro Narimoto
Eri Chatani
Masaru Hoshino
Kazumasa Sakurai
Kazuhiro Hasegawa
Source :
FEBS Letters. (3):313-319
Publisher :
Federation of European Biochemical Societies. Published by Elsevier B.V.

Abstract

Although the stability of globular proteins has been studied extensively, that of amyloid fibrils is scarcely characterized. Beta2-microglobulin (beta2-m) is a major component of the amyloid fibrils observed in patients with dialysis-related amyloidosis. We studied the effects of guanidine hydrochloride on the amyloid fibrils of beta2-m, revealing a cooperative unfolding transition similar to that of the native state. The stability of amyloid fibrils increased on the addition of ammonium sulfate, consistent with a role of hydrophobic interactions. The results indicate that the analysis of unfolding transition is useful to obtain insight into the structural stability of amyloid fibrils.

Details

Language :
English
ISSN :
00145793
Issue :
3
Database :
OpenAIRE
Journal :
FEBS Letters
Accession number :
edsair.doi.dedup.....af58761f1b2b74699b5971c28ce37ec4
Full Text :
https://doi.org/10.1016/j.febslet.2004.09.024