Open AccessInvestigating the Chaperoning Effect of Nanoparticles in Chemically Denatured zDHFR: An in vitro Study
Author(s) -
Preeti Gupta,
Anita Verma,
Pratima Chaudhuri
Publication year - 2021
Publication title -
asian journal of chemistry/asian journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.145
H-Index - 34
eISSN - 0975-427X
pISSN - 0970-7077
DOI - 10.14233/ajchem.2021.23372
Subject(s) - chemistry , denaturation (fissile materials) , guanidine , dihydrofolate reductase , protein aggregation , biophysics , native state , nanoparticle , circular dichroism , colloidal gold , protein secondary structure , tryptophan , in vitro , protein structure , biochemistry , enzyme , nanotechnology , amino acid , nuclear chemistry , materials science , biology
Maintenance of native structure and function of the protein is a major concern for industrial productionof aggregation prone therapeutically important recombinant proteins. Aggregation may results due tochange in the native conformation of proteins under different stress conditions. To overcome the problemof protein aggregation, role of silver and gold nanoparticles have been investigated. The nanoparticlesowing to their affirmative interaction with the proteins possess chaperoning activities and protect thenative state from denaturation. In the present study, through performing chemical denaturation ofzebrafish dihydrofolate reductase using denaturants like guanidine hydrochloride and urea in thepresence and absence of gold and silver nanoparticles and monitoring the process through enzymeactivity assay and intrinsic tryptophan fluorescence, we have demonstrated the impact of nanoparticlesin maintaining native conformation of proteins. Further, the outcome of refolding studies of DHFRprotein with nanoparticles monitored by UV-visible spectroscopy was also reported.