Structure, Function, and Clinical Relevance of Molecular Chaperones – A Review Article

Proteins known as molecular chaperones are essential components of cellular protein homeostasis since these proteins assist others in folding and stabilizing or degrading the polypeptides. The principle is that if misfolded or aggregated proteins—common in many pathologies such as cancer, neurodegenerative, and genetic diseases—are inhibited from forming deposits, then normal pathology can be restored. In general, chaperones have been recognized as significant targets and tools in clinical therapies due to their centrality towards proteostasis and thus provide room for innovation treatment approaches such as pharmacological chaperone therapy, chaperone inhibition, and gene-based enhancement strategies. Therefore, a deep insight into the structure and function of these proteins is paramount for safe and target-specific intervention development. The paper should try to convince the readers regarding the fact that though molecular chaperones possess all the requirements idealized theoretically to be applied clinically as therapeutic agents, there exist several practical obstacles that make this successful clinical application dubious.