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- W2058925087 abstract "Recent studies on amyloid disease-related proteins such as β-amyloid and prion have pointed out that conformational alternation and subsequent aggregation to form amyloid fibrils play a key role in such fatal diseases. Here, design and synthesis of peptides undergoing a structural transition from α-helix to β-sheet and self-assembly into amyloid fibrils are described. A dimeric peptide was designed to form a coiled-coil α-helix structure and the N-terminus was modified with various kinds of standard hydrophobic amino acids. The self-initiated structural transition to β-sheet was induced by appropriate hydrophobic amino acids attached to the N-termini of the peptides. Moreover, the peptides in β-sheet self-assembled into the amyloid with a well-organized fibrillar structure. Simplified model peptides like those presented here will lead to a better understanding of the process by which conformational alternation and aggregation of proteins occur, as well as to developing novel nanoscale materials." @default.
- W2058925087 created "2016-06-24" @default.
- W2058925087 creator A5031934027 @default.
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- W2058925087 date "2000-09-01" @default.
- W2058925087 modified "2023-09-26" @default.
- W2058925087 title "Construction of Peptides That Undergo Structural Transition from α-Helix to β-Sheet and Amyloid Fibril Formation by the Introduction of N-Terminal Hydrophobic Amino Acids" @default.
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- W2058925087 doi "https://doi.org/10.1016/s0040-4020(00)00524-x" @default.
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