Abstract
Amyloid fibrils are highly ordered protein assemblies known to contribute to the pathology of a variety of genetic and aging-associated diseases. More recently, these fibrils have been shown to be useful as structural scaffolds in both natural biological systems and nanotechnology applications. The intense interest in amyloid fibrils has led to the investigation of well-characterized proteins, such as hen egg white lysozyme (HEWL), as model systems to examine structural and mechanistic principles that may be generally applicable to all amyloid fibrils. The purpose of this review is to critically examine the fibril-formation literature of proteins in the lysozyme family with respect to the known structure and folding properties of these proteins. The goal is to identify similarities and differences within the family, examine general misfolding / aggregation principles, and identify key areas of importance for future work on the fibril formation of these proteins.
Keywords: Lysozyme, α-lactalbumin, amyloid, fibril, protein misfolding, aggregation, chemical modification
Current Protein & Peptide Science
Title: The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family
Volume: 8 Issue: 6
Author(s): Adam J. Trexler and Melanie R. Nilsson
Affiliation:
Keywords: Lysozyme, α-lactalbumin, amyloid, fibril, protein misfolding, aggregation, chemical modification
Abstract: Amyloid fibrils are highly ordered protein assemblies known to contribute to the pathology of a variety of genetic and aging-associated diseases. More recently, these fibrils have been shown to be useful as structural scaffolds in both natural biological systems and nanotechnology applications. The intense interest in amyloid fibrils has led to the investigation of well-characterized proteins, such as hen egg white lysozyme (HEWL), as model systems to examine structural and mechanistic principles that may be generally applicable to all amyloid fibrils. The purpose of this review is to critically examine the fibril-formation literature of proteins in the lysozyme family with respect to the known structure and folding properties of these proteins. The goal is to identify similarities and differences within the family, examine general misfolding / aggregation principles, and identify key areas of importance for future work on the fibril formation of these proteins.
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Cite this article as:
Trexler J. Adam and Nilsson R. Melanie, The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family, Current Protein & Peptide Science 2007; 8 (6) . https://dx.doi.org/10.2174/138920307783018659
DOI https://dx.doi.org/10.2174/138920307783018659 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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