Aggregated proteins, or amyloids, are seen in a wide variety of neurodegenerative diseases, including Alzheimer's and Creutzfeldt-Jakob (CJD) disease. Such aggregates are generally considered to be aberrant formations, but a new study suggests they may be an inherent tendency in many proteins. In tomorow's issue of Nature (pp165-166), Christopher Dobson and colleagues, of the University of Oxford, report that the muscle protein myoglobin can be induced to take on a fibrillar structure in certain chemical environments, and suggest that such amyloid structures could be feasible for many proteins, but that organisms have evolved ways to hold them at bay. The finding raises the question of whether protein aggregates develop as a result of the breakdown of normal protective mechanisms.—June Kinoshita

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Primary Papers

  1. . Amyloid fibrils from muscle myoglobin. Nature. 2001 Mar 8;410(6825):165-6. PubMed.