Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-β region

Masatoshi Saiki, Kohei Shiba, Masaki Okumura

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Amyloid fibrils are fibrous protein assemblies with distinctive cross-β structures. For amyloidosis, there are disease-associated mutations outside of the cross-β structures. Thus, it is necessary to elucidate the role of peripheral sequences outside the cross-β structure. Amyloid fibrils are generally 10 nm in width; however, the amyloid fibrils of truncated barnase M1 peptides missing the C-terminal sequence outside the cross-β structure are 20 nm in width. In this study, we performed comparative analysis of the structural stability of amyloids formed by the respective peptides. We found that the C-terminal amino acids dramatically affect the conformational instability in the presence of a denaturing reagent.

Original languageEnglish
Pages (from-to)3541-3547
Number of pages7
JournalFEBS Letters
Volume589
Issue number23
DOIs
Publication statusPublished - 2015 Nov 30

Keywords

  • Amyloid
  • Cross-β
  • Dynamic light scattering
  • Peripheral
  • Thioflavin T

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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