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Polypeptide Models to Understand Misfolding and Amyloidogenesis and Their Relevance in Protein Design and Therapeutics

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Abstract:

The study of amyloid polypeptide models (polypeptides able to generate amyloid structures not necessarily connected with any pathology) provides an excellent tool to increase the understanding of the generic aspects of misfolding and aggregation as well as the details of the mechanism of polypeptide deposition in disease. This knowledge can be integrated and applied to different problems in therapy and biotechnology, and in particular to re-designing bioactive polypeptides (biopharmaceuticals) with improved properties.

Keywords: amyloid hotspots; amyloid model; amyloid nucleation; amyloidosis; polypeptide deposition disorders; protein evolution; protein misfolding and aggregation; protein re-design

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866053005791

Affiliations: Leverhulme Centre for Biological Complexity. Department of Chemistry, University of Cambridge. Lensfield Road, Cambridge CB2 1EW, UK.

Publication date: February 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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