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Protein Aggregation and Its Consequences for Human Disease

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Abstract:

Protein molecules have emerged through evolution so that they are able to remain in their functional and soluble states under normal physiological conditions, although in other situations they often have a high propensity to aggregate. Aggregation in vivo is associated with a wide range of human disorders, including Alzheimer's disease and type II diabetes, medical conditions that are becoming increasingly common in the modern world. In such diseases, aggregated proteins can often be observed as highly intractable thread-like species known as amyloid fibrils. This article provides an overview of our present knowledge of the nature of these fibrillar aggregates and the manner in which they form, and discusses the origins and potential means of suppression of the pathogenic properties with which they and their precursors are associated.





Keywords: Amyloid; amyloidosis; neurodegenerative disease; protein fibrils; protein misfolding

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775338362

Affiliations: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

Publication date: March 1, 2006

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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