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: protein misfolding and aggregation, protein re-design, protein evolution, amyloid model, amyloid nucleation, amyloid hotspots, polypeptide deposition disorders, amyloidosis
Protein & Peptide Letters
Title: Polypeptide Models to Understand Misfolding and Amyloidogenesis and Their Relevance in Protein Design and Therapeutics
Volume: 12 Issue: 2
Author(s): Jesus Zurdo
Affiliation:
Keywords: protein misfolding and aggregation, protein re-design, protein evolution, amyloid model, amyloid nucleation, amyloid hotspots, polypeptide deposition disorders, amyloidosis
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.
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Cite this article as:
Zurdo Jesus, Polypeptide Models to Understand Misfolding and Amyloidogenesis and Their Relevance in Protein Design and Therapeutics, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005791
DOI https://dx.doi.org/10.2174/0929866053005791 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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