Interactions between bovine serum albumin and gemini surfactant alkanediyl‐α, ω‐bis(dimethyldodecyl‐ammonium bromide)

Abstract

Interactions between bovine serum albumin (BSA) and cationic gemini surfactant alkanediyl-alpha,omega-bis(dimethyldodecyl-ammonium bromide) (12-n-12, n=3, 4, 6) in aqueous solution have been investigated by measuring fluorescence, UV-vis transmittance, dynamic lighting scattering, and circular dichroism. Compared to a traditional surfactant dodecyltrimethylammonium bromide (DTAB), 12-n-12 interacts with BSA more strongly. With increasing concentration, 12-n-12 first binds specifically onto BSA leading to the unfolding and aggregation of BSA, and the decrease in alpha-helix content; and then forms micelle-like complexes along the unfolded BSA chains. A gemini surfactant with a longer spacer has a larger effect on BSA unfolding due to a stronger hydrophobic interaction.

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

“…The theoretical and experimental studies on the adsorption behaviour of proteinsurfactant mixtures have been covered by a number of papers [72][73][74][75][76], and different mechanisms for the displacement of protein molecules from the interface by the surfactants have been suggested such as orogenic displacement [75] or competitive adsorption [76]. In many investigations [77][78][79][80][81], interaction of cationic gemini surfactants with proteins have exposed that such surfactants interact more competently with proteins as compared to conventional single-chain surfactants because of their distinctive aggregation properties such as lower critical micelle concentration (CMC) and Krafft temperature, special aggregation morphology, strong hydrophobic microdomains and so forth [82][83][84][85]. Cationic surfactants, being antimicrobial, have attracted attention with respect to their interaction with deoxyribonucleic acid (DNA) and lipids [86].…”

Reversibility of the interactions between a novel surfactant derived from lysine and biomolecules

“…Following the procedure of Pi et al [39], the average number of LYCl molecules bound to a BSA molecule, , was calculated for the different surfactant concentrations. Fig.…”

Unfolding of rabbit serum albumin by cationic surfactants: Surface tensiometry, small-angle neutron scattering, intrinsic fluorescence, resonance Rayleigh scattering and circular dichroism studies

“…In a recent study [12] we had reported the interaction of a cationic gemini and its monomeric counterpart CTAB at low surfactant concentrations (which is a common practice for studying protein-surfactant interactions) wherein the conformational changes and saturation points in the proteins (BSA, HSA, RSA) were found to occur at much lower [gemini] in comparison to [CTAB]. Some other investigations [13][14][15][16][17][18] on the interaction of cationic gemini surfactants with proteins have revealed that these surfactants interact more efficiently with proteins as compared to conventional single chain surfactants because of their unique aggregation properties [19]. In order to further explore and acquire detailed knowledge of the phenomenon, it is, therefore, of interest to study the protein-surfactant interaction at higher cationic surfactant concentrations.…”