Refolding of denatured gold nanoparticles-conjugated bovine serum albumin through formation of catanions between gemini surfactant and sodium dodecyl sulphate.

The present work elucidates binding interactions of sodium dodecyl sulphate (SDS) with the conjugated gold nanoparticles (AuNPs)-bovine serum albumin (BSA), unfolded by each of two gemini surfactants, 1,4-bis(dodecyl- N , N -dimethylammonium bromide)-butane (12-4-12,2Br - ) or 1,8-bis(dodecyl- N , N -dimethylammonium bromide)-octane (12-8-12,2Br - ). Initially, at a low concentration of SDS there is a relaxation of bioconjugates from their compressed form due to the formation of catanions between SDS and gemini surfactants. On moving towards higher concentrations of SDS, these relaxed unfolded bioconjugates renature by removal of residual bound gemini surfactants. Mixed assemblies of SDS and gemini surfactants formed during refolding of bioconjugates are characterized by DLS and FESEM measurements. A step-by-step process of refolding observed for these denatured protein bioconjugates is exactly the inverse of their unfolding phenomenon. Parameters concerning nanometal surface energy transfer (NSET) and Förster's resonance energy transfer (FRET) phenomenon were employed to develop a binding isotherm. Moreover, there remains an inverse relationship between α-helix and β-turns of bioconjugates during the refolding process. Significantly, in the presence of 12-8-12,2Br - , SDS induces more refolding as compared to that for 12-4-12,2Br - . Bioconjugation shows an effect on the secondary structures of refolded BSA, which has been explored in detail through various studies such as Fourier transform infrared spectroscopy, fluorescence, and circular dichroism (CD). Therefore, this approach vividly describes the refolding of denatured bioconjugates, exploring structural information regarding various catanions formed during the process that would help in understanding distance-dependent optical biomolecular detection methodologies and physicochemical properties.