Interacting Behaviour of Bovine Serum Albumin at CMCs of Aqueous Tweens 20-80 Studied with UV Spectroscopy

Abstract

Protein-surfactant interactions in aqueous liquid mixtures have been industrially effective interface for understanding of protein unfolding dynamics. Thereby, UV absorbance (abs) study for 0.01 to 0.12% (w/v) BSA with aqueous Tweens (Tws) 20 to 80 at pre-critical micelle concentration (pre-CMC), CMC, post-CMC (CMCs) are reported at 298.15 K. The CMCs found as Tw 60 > Tw 80 > Tw 40 > Tw 20, were determined by the surface tension of Tws, and the pre- and post-CMC were derived from CMC. With Tws the abs at 200 to 320 nm depicts the structural changes in BSA due to unfolding it on account of hydrophilic and hydrophobic interactions (HH_bI). A higher abs at λ_max within 200 to 230 nm and lower abs at 280 nm infer BSA interactions with Tws via peptide bonds and amino acid groups respectively. The UV of 280 nm predicts a link between the states of BSA and their interaction with Tws for study of BSA activity.