| Literature DB >> 14759730 |
Yuta Takahashi1, Hisakazu Mihara.
Abstract
The amyloid-like fibril is considered to be a macromolecular self-assemblage with a highly-ordered quaternary structure, in which numerous beta-stranded polypeptide chains align regularly. Therefore, this kind of fibril has the potential to be engineered into proteinaceous materials, although conformational alteration of proteins from their native form to the amyloid form is a misfolding and undesirable process related to amyloid diseases. In this study, we have attempted to design an artificial system to explore applicability of using the amyloid-like fibril as a construct possessing self-recognition and self-catalytic abilities. A peptide self-replicating system based on the beta-structure of the amyloid-like fibril was designed and constructed. The beta-stranded peptide was self-replicated by the native chemical ligation reaction, and the newly generated peptide was self-assembled into amyloid-like fibrils. Thus, the constructed system was of both chemical and conformational self-replicating fibrils.Entities:
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Year: 2004 PMID: 14759730 DOI: 10.1016/j.bmc.2003.11.022
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641