Modulation of protein oligomerization: An overview

A large section of cellular proteins in both prokaryotic and eukaryotic systems have oligomeric property. Intently, oligomerization of protein is an invaluable phenomenon from the point of view of protein evolution. This review comprises an overview on modulation of protein oligomerization. The comprehensive modulation of protein oligomerization can be supportive for effective drug designing in the future. The common mechanisms of protein oligomerization are domain swapping and ligand induced dimerization. Infrequent mechanism of protein oligomerization involves point mutations at the dimer interface, post-translational modification and insertion/deletion at the interface. Predominantly, ligand induced oligomerization is the most useful method to regulate the protein oligomerization that can act as a modulator. Thus, functional modulation of oligomeric proteins can be done, both in-vitro and in-vivo, using various artificial and natural modulators, respectively. Though, the biophysical methods, like microscopy and spectroscopy, have strong potential to characterize the oligomeric proteins. Oligomeric proteins can be characterized biochemically too. Hence, this review illustrates the regulation of protein oligomerization using several modulators, in the future, these can be used for effective drug designing to cure several diseases associated with oligomeric proteins.