title: Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding.
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.
authors.affiliation: Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Corporation, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
authors.forename: Takehiro
authors.initials: T
authors.lastname: Narimoto
authors.forename: Kazumasa
authors.initials: K
authors.lastname: Sakurai
authors.forename: Azusa
authors.initials: A
authors.lastname: Okamoto
authors.forename: Eri
authors.initials: E
authors.lastname: Chatani
authors.forename: Masaru
authors.initials: M
authors.lastname: Hoshino
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Hasegawa
authors.forename: Hironobu
authors.initials: H
authors.lastname: Naiki
authors.forename: Yuji
authors.initials: Y
authors.lastname: Goto
mesh_terms: 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*
chemical_list: D011994:Recombinant Proteins; D001613:beta 2-Microglobulin; D019791:Guanidine; D000645:Ammonium Sulfate