Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding.
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.
Narimoto
Takehiro
T
Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Corporation, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
Sakurai
Kazumasa
K
Okamoto
Azusa
A
Chatani
Eri
E
Hoshino
Masaru
M
Hasegawa
Kazuhiro
K
Naiki
Hironobu
H
Goto
Yuji
Y
D000645:Ammonium Sulfate; D000686:Amyloidosis; D019791:Guanidine; D006801:Humans; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D001613:beta 2-Microglobulin / Q000737:chemistry* / Q000378:metabolism*
D011994:Recombinant Proteins; D001613:beta 2-Microglobulin; D019791:Guanidine; D000645:Ammonium Sulfate