Thioflavin T-silent denaturation intermediates support the main-chain-dominated architecture of amyloid fibrils

Sayaka Noda, Masatomo So, Masayuki Adachi, J. Kardos, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yuji Goto

Research output: Contribution to journalArticle

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Abstract

Ultrasonication is considered one of the most effective agitations for inducing the spontaneous formation of amyloid fibrils. When we induced the ultrasonication-dependent fibrillation of β2-microglobulin and insulin monitored by amyloid-specific thioflavin T (ThT) fluorescence, both proteins showed a significant decrease in ThT fluorescence after the burst-phase increase. The decrease in ThT fluorescence was accelerated when the ultrasonic power was stronger, suggesting that this decrease was caused by the partial denaturation of preformed fibrils. The possible intermediates of denaturation retained amyloid-like morphologies, secondary structures, and seeding potentials. Similar denaturation intermediates were also observed when fibrils were denatured by guanidine hydrochloride or sodium dodecyl sulfate. The presence of these denaturation intermediates is consistent with the main-chain-dominated architecture of amyloid fibrils. Moreover, in the three types of denaturation experiments conducted, insulin fibrils were more stable than β2-microglobulin fibrils, suggesting that the relative stability of various fibrils is independent of the method of denaturation.

Original languageEnglish
Pages (from-to)3937-3948
Number of pages12
JournalBiochemistry
Volume55
Issue number28
DOIs
Publication statusPublished - Jul 19 2016

Fingerprint

Denaturation
Amyloid
Fluorescence
Insulin
Guanidine
Ultrasonics
Sodium Dodecyl Sulfate
thioflavin T
Proteins
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Thioflavin T-silent denaturation intermediates support the main-chain-dominated architecture of amyloid fibrils. / Noda, Sayaka; So, Masatomo; Adachi, Masayuki; Kardos, J.; Akazawa-Ogawa, Yoko; Hagihara, Yoshihisa; Goto, Yuji.

In: Biochemistry, Vol. 55, No. 28, 19.07.2016, p. 3937-3948.

Research output: Contribution to journalArticle

Noda, Sayaka ; So, Masatomo ; Adachi, Masayuki ; Kardos, J. ; Akazawa-Ogawa, Yoko ; Hagihara, Yoshihisa ; Goto, Yuji. / Thioflavin T-silent denaturation intermediates support the main-chain-dominated architecture of amyloid fibrils. In: Biochemistry. 2016 ; Vol. 55, No. 28. pp. 3937-3948.
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