Publication Type : Journal Article
Publisher : RSC Adv., The Royal Society of Chemistry
Source : RSC Adv., The Royal Society of Chemistry, Volume 3, p.8016-8020 (2013)
Url : http://dx.doi.org/10.1039/C3RA00061C
Campus : Amritapuri
School : School of Arts and Sciences
Department : Chemistry
Year : 2013
Abstract : Peptide dendrimers are screened for “artificial chaperone” (protein refolding) activity by a sensitive fluorescence based assay. The refolding with largest dendrimer is found to help in recovering biological activity of >90% in the case of unfolded lipases and amylases. The refolding yields decrease down to 14% with a decrease in the complexity and hydrophobicity of the dendron/dendrimer. CD spectroscopy confirms the correct refolding in terms of secondary structure contents of the proteins. The DLS data indicates that presence of the dendrons/dendrimers facilitates protein refolding by preventing the aggregation of proteins.
Cite this Research Publication : P. Dubey, Gautam, S., Kumar, P. P. Praveen, Sandhya Sadanandan, Haridas, V., and Gupta, M. N., “Dendrons and dendrimers as pseudochaperonins for refolding of proteins”, RSC Adv., vol. 3, pp. 8016-8020, 2013.