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Amyloids
Amyloid fibers are distinguished by their resistance to proteinase K, tinctorial properties and β-sheet-rich secondary structure.Amyloid fibrils have biochemical and biophysical properties that distinguish them from other biological polymers. Amyloid formation is a hallmark of many human diseases including Alzheimer’s, Huntington’s and the prion diseases. Therefore, understanding amyloidogenesis will provide insights into the development of therapeutics that target these debilitating diseases. The deposition of large amounts of fibrillar material can subvert the tissue architecture and consequently cause organ dysfunction. Amyloid fibrils may also cause organ dysfunction by interacting with local receptors, such as RAGE. In Alzheimer’s disease, an inflammatory response in the cerebral cortex elicited by the progressive accumulation of Ab contributes to the pathogenesis of the disease.At present, the most effective approach to the treatment of the systemic amyloidoses involves shutting down or substantially reducing the synthesis of the amyloid precursor.
References
1.Neal D. Hammer,et al. J Alzheimers Dis. 2008 May; 13(4): 407–419.
2.Merlini G,et al. N Engl J Med. 2003 Aug 7;349(6):583-96.
References
1.Neal D. Hammer,et al. J Alzheimers Dis. 2008 May; 13(4): 407–419.
2.Merlini G,et al. N Engl J Med. 2003 Aug 7;349(6):583-96.
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Amyloids
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