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Fluorescence Correlation Spectroscopy; Protein-Surfactant Interaction; EIS; human serum albumin;

The denaturation of human serum albumin (HSA) upon interaction with the surfactant sodium dodecyl sulphate (SDS) was examined by measuring the diffusion time of fluorophore (RITC) tagged HSA under near single-molecule conditions using fluorescence correlation spectroscopy. The diffusion time showsfour distinct regions as a function of SDS concentration, which corresponds to (I) opening of the tertiary structure, (II) non-specific SDS aggregation, (III) opening of the secondary structure, and (IV) aggregation of SDS around the secondary structure. Diffusion time increases from 383 ls for the free protein to 1002 ls forthe SDS bound protein, which leads to an effective increase in the hydrodynamic radius by a factor of about 2.6

VAISHALI SAMANT¹ ARGHYA DEY G NARESH PATWARI

1. Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai, Maharashtra 400 076, India

Published

18 August 2020

Manuscript received

1 April 2020

Manuscript revised

10 June 2020

Accepted

15 June 2020