Construction of a chemically and conformationally self-replicating system of amyloid-like fibrils.
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.
Takahashi
Yuta
Y
Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Mihara
Hisakazu
H
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D020836:Protein Structure, Quaternary; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared
D000682:Amyloid; D010455:Peptides