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

Abstract

Abstract Interactions between bovine serum albumin (BSA) and cationic gemini surfactant alkanediyl‐α,ω‐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 α‐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. © 2006 Wiley Periodicals, Inc. Biopolymers 83:243–249, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com