Engineering peptides and proteins that undergo alpha-to-beta transitions
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
Published on: January 26, 2016
1Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo, Institute of Technology, Yokohama, Japan. hmihara@bio.titech.ac.jp
Abstract:
In the 'protein-only' hypothesis, prion diseases are proposed to be the result of conformational changes of the normal form of the prion protein (PrPC) with a highly alpha-helical conformation to a pathogenic scrapie form (PrPSc) with a predominantly beta-sheet conformation. Recent studies examining the folding process of proteins, as well as the amyloidogenesis of peptides and proteins including prion proteins, Alzheimer's beta-peptides and other pathogenic protein mutants, have provided insight into the conformational changes essential to fibrillogenesis and correct folding.
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