Amyloidosis consist of diseases characterised by the accumulation of misfolded proteins in various organs throughout the body. These misfolded protein aggregates, called amyloids, are formed due to overridden biochemical defences and defects in the normal protein folding processes.
This narrative literature review aims to provide a robust overview of the role of protein misfolding in amyloidosis, highlighting the biochemistry of molecular stages of amyloid formation, structural and molecular features of amyloid and their contribution to disease pathogenesis.
The review explores the fundamental process of protein folding and describes the factors that can lead to misfolding. By describing the structural changes that occur when proteins adopt abnormal conformations, the review delineates the formation of amyloid precursor proteins such as oligomers and protofilaments in the amyloid cascade. The review further elucidates the generic molecular and structural features of amyloid protein in its final aggregated state. It also explores the pathophysiology of cellular dysfunction and tissue damage in amyloidosis.
In a nutshell, protein misfolding plays a crucial role in the pathogenesis of amyloidosis by initiating a cascade of events that ultimately lead to tissue damage and functional impairment. Understanding the role of each precursor molecule in the protein misfolding cascade of amyloidosis is sacrosanct for the development of effective therapeutic interventions. Further research in this field can provide avenues for the development of novel treatments which can help potentially prevent or halt the progression of amyloid-related diseases.
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