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Conformational stability of amyloid fibrils of β 2 ‐microglobulin probed by guanidine‐hydrochloride‐induced unfolding
Author(s) -
Narimoto Takehiro,
Sakurai Kazumasa,
Okamoto Azusa,
Chatani Eri,
Hoshino Masaru,
Hasegawa Kazuhiro,
Naiki Hironobu,
Goto Yuji
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.024
Subject(s) - guanidine , fibril , chemistry , beta 2 microglobulin , amyloid (mycology) , biophysics , amyloidosis , amyloid fibril , globular protein , hydrochloride , crystallography , biochemistry , amyloid β , biology , medicine , inorganic chemistry , disease , pathology , immunology
Although the stability of globular proteins has been studied extensively, that of amyloid fibrils is scarcely characterized. β 2 ‐microglobulin (β2‐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 β2‐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.