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

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Abstract

Although the stability of globular proteins has been studied extensively, that of amyloid fibrils is scarcely characterized. β2- 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. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Narimoto, T., Sakurai, K., Okamoto, A., Chatani, E., Hoshino, M., Hasegawa, K., … Goto, Y. (2004). Conformational stability of amyloid fibrils of β2- microglobulin probed by guanidine-hydrochloride-induced unfolding. FEBS Letters, 576(3), 313–319. https://doi.org/10.1016/j.febslet.2004.09.024

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