2015Journal of Dispersion Science and TechnologyRequires access

Spectroscopic Investigation on the Interactions between Cationic Surfactants and Bovine Serum Albumin

Miao Qin, Tianxiang Yin, Shuzhen Wang, Weiguo Shen

Open publisher page 6 citations

Abstract

Physicochemical studies on the interaction of cationic surfactants dodecyltrimethylammonium bromide (DTAB), N-dodecyl-N-2-hydroxyethyl-N,N-dimethylammonium bromide (C12HDAB), and N-dodecyl-N,N-2-dihydroxyethyl-N-methyl ammonium bromide (C12DHAB) with bovine serum albumin (BSA) were performed by fluorimetry, circular dichroism (CD) spectroscopy, dynamic light scattering, and ξ-potential measurements. The quenching efficiency of the intrinsic fluorescence of BSA and the interaction strength with BSA increased with increasing numbers of hydroxyethyl constituents in the head group. In each of the surfactant/BSA systems studied, the specific binding site was Trp-213 and the hydrophobic interaction was predominant while a contribution of the hydrogen bond was also observed in the presence of hydroxyethyl.

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Physicochemical studies on the interaction of cationic surfactants dodecyltrimethylammonium bromide (DTAB), N-dodecyl-N-2-hydroxyethyl-N,N-dimethylammonium bromide (C12HDAB), and N-dodecyl-N,N-2-dihydroxyethyl-N-methyl ammonium bromide (C12DHAB) with bovine serum albumin (BSA) were performed by fluorimetry, circular dichroism (CD) spectroscopy, dynamic light scattering, and ξ-potential measurements. The quenching efficiency of the intrinsic fluorescence of BSA and the interaction strength with BSA increased with increasing numbers of hydroxyethyl constituents in the head group. In each of the surfactant/BSA systems studied, the specific binding site was Trp-213 and the hydrophobic interaction was predominant while a contribution of the hydrogen bond was also observed in the presence of hydroxyethyl.

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Available abstract

Physicochemical studies on the interaction of cationic surfactants dodecyltrimethylammonium bromide (DTAB), N-dodecyl-N-2-hydroxyethyl-N,N-dimethylammonium bromide (C12HDAB), and N-dodecyl-N,N-2-dihydroxyethyl-N-methyl ammonium bromide (C12DHAB) with bovine serum albumin (BSA) were performed by fluorimetry, circular dichroism (CD) spectroscopy, dynamic light scattering, and ξ-potential measurements. The quenching efficiency of the intrinsic fluorescence of BSA and the interaction strength with BSA increased with increasing numbers of hydroxyethyl constituents in the head group. In each of the surfactant/BSA systems studied, the specific binding site was Trp-213 and the hydrophobic interaction was predominant while a contribution of the hydrogen bond was also observed in the presence of hydroxyethyl.

Key concepts: Chemistry, Bovine serum albumin, Circular dichroism, Cationic polymerization, Ammonium bromide, Hydrogen bond, Bromide, Hydrophobic effect

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