Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-β region.
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 10nm 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.
Department of Applied Chemistry, Faculty of Engineering, Tokyo University of Science, Yamaguchi, Sanyo-Onoda, Yamaguchi, Japan. Electronic address: saiki@rs.tus.ac.jp.
Masatoshi
M
Saiki
Malvern Instruments, a Division of Spectris Co. Ltd., Chuo-ku, Kobe, Japan.
Kohei
K
Shiba
School of Science and Technology, Kwansei Gakuin University, Gakuen 2-1, Sanda, Hyogo, Japan.
Masaki
M
Okumura
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011489:Protein Denaturation / Q000187:drug effects; D055550:Protein Stability; D017433:Protein Structure, Secondary
D000682:Amyloid; D010446:Peptide Fragments
Amyloid; Cross-β; Dynamic light scattering; Peripheral; Thioflavin T