Diseases associated with the deposition of normally soluble proteins as insoluble amyloid fibrils are a major threat to human health today and are predicted to dominate world health needs in the coming century. Despite major research efforts in this area (with > 58,000 publications on the topics of “amyloid and amyloidosis” over the last 20 years), in all but a few examples, a cure for amyloid disease remains remote. Not all amyloid fibrils are deleterious, however, and recent studies have provided evidence for functional amyloid fibrils in man and higher eukaryotes, for example, in melanin formation, in the storage of secretary hormones, in memory, and, most recently, in the formation of RNA granules. 1–4 Amyloid fibrils are also produced by bacteria (used for biofilm formation), 5 fungi (used for prion formation—thought to provide advantageous fitness to the host organism), 6 and viruses (human immunodeficiency virus and other retroviruses—used to enhance infectivity). 7 The unique physical properties of the cross-β structure of amyloid has also caught the attention of biophysicists and bioengineers, and amyloid fibrils are currently being actively studied as potential new nanomaterials with unique mechanical properties. 8,9 Understanding the molecular mechanisms of protein assembly into amyloid fibrils
Journal of Molecular Biology – Elsevier
Published: Aug 10, 2012
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