Biophysics and Biochemistry of Protein Aggregation PDF
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Protein self-assembly is a common process in nature. It generates functional polymers, such as actin filaments and microtubules in the cytoskeleton of cells. However, the recent explosion of interest in protein aggregation arises from the recognition that many diseases are caused by the conversion of soluble, often intrinsically disordered, peptides and proteins into amyloid fibrils, which in turn form extracellular deposit or intra-cellular tangles. A few well-known examples among dozens of diseases are alzheimer’s disease (ad) associated with amyloid-β peptide (aβ) and tau protein, parkinson’s disease with α-synuclein, type ii diabetes with amylin, and creutzfeldt–jakob disease (mad cow disease) with prion. In recent years, the number of ad patients has risen with an increase in the ageing population and diabetes has become more wide-spread in developed and developing countries. These diseases pose a serious threat to the general health of the public and are a financial burden to patients, their families and society. Therefore, we cannot over-emphasize the importance of studying protein aggregation in order to curtail the spread of such diseases and, we hope, one day to cure them. Even natively folded functional proteins under abnormal conditions can selfassemble into aggregated states; for example, the amyloid state. The amyloid state, also with a well-defined structure, is an alternative state to the native structure. To gain a complete picture of different states of a protein, one should understand under what conditions a functional protein can misfold and assemble into the amyloid state and how in general functional proteins avoid such conversion. The story is different for intrinsically disordered peptides and proteins, often responsible for neurodegenerative diseases, where “misfolding” refers to the peptides/proteins adopting aggregation-prone conformations.
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