Quantification of differential efficacy of chemical chaperones in ameliorating solubilization and folding of zebrafish dihydrofolate reductase.

Protein aggregation is a major hindrance in many in vivo and in vitro studies of proteins. It results in the formation of inclusion bodies and non-functional aggregates. Chemical chaperones also known as osmolytes which are accumulated during the stress conditions in the cells can influence the protein stability through various mechanisms. They act as osmoprotectants and contribute to the protein folding by enabling the protein to bury the backbone into the core of protein fold. In the current study, we observed the effect of chemical chaperones from four different classes on the stability and functionality of aggregation prone protein zebrafish dihydrofolate reductase (zDHFR). We also used UV-visible and circular dichroism (CD) spectroscopy to explore the protecting action of chemical chaperones on the structure and activity of zDHFR in vitro and in vivo conditions.