Design of peptides undergoing self-catalytic alpha-to-beta transition and amyloidogenesis.
Improved understanding of amyloidogenic peptides and proteins such as prion proteins and Alzheimer's beta peptides has attracted much attention to the elucidation of the molecular mechanisms of such amyloidogenesis. As a representative, in the prion protein, the conformational transitions from alpha-helix to beta-structure undergo along with the amyloidogenesis in a self-catalytic manner. Moreover, recent studies by the de novo design of peptides and proteins as well as the amyloidogenesis of peptides and proteins including pathogenic protein mutants have provided insight into the conformational changes essential to amyloidogenesis and correct folding.
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
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Mihara
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Takahashi
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Ueno
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D001704:Biopolymers / Q000737:chemistry; D015195:Drug Design; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary
D000682:Amyloid; D016229:Amyloid beta-Peptides; D001704:Biopolymers; D010455:Peptides; D011328:Prions