Protein folding, misfolding, aggregation and their implications in human diseases: discovering therapeutic ways to amyloid-associated diseases.

Protein folding is a very complex process, and recognition of the molecular mechanisms responsible for protein folding is one of the demanding queries in biochemistry. Protein molecules have a fixed propensity either to misfold or unable to sustain their precisely folded states, under assured conditions. Taking into account that the protein misfolding and aggregation are central in the pathogenesis of protein conformational disorders, a therapy focussed to the root of the disease should target to restrain and/or undo the conformational alterations that lead to the development of the pathological protein conformer. In future, an understanding of the causes of protein aggregation and genetic and environmental vulnerability features of an exact individual may offer an enhanced prospect for a successful therapeutic intrusion. Dealing with these and related problems not only provides great prospects for involvement with numerous, presently fatal diseases but will also ultimately disclose the basically essential association between proteostasis and prolonged existence.