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Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region
Author(s) -
Saiki Masatoshi,
Shiba Kohei,
Okumura Masaki
Publication year - 2015
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.2015.10.015
Subject(s) - sequence (biology) , fibril , core (optical fiber) , amyloid fibril , chemistry , biophysics , peripheral , amyloid (mycology) , stability (learning theory) , materials science , amyloid β , biochemistry , biology , medicine , computer science , pathology , composite material , inorganic chemistry , disease , machine learning
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.