Please use this identifier to cite or link to this item: https://doi.org/10.1002/bip.20552
Title: Interactions between bovine serum albumin and gemini surfactant alkanediyl-α, ω-bis(dimethyldodecyl-ammonium bromide)
Authors: Pi, Y.
Shang, Y.
Peng, C.
Liu, H.
Hu, Y.
Jiang, J. 
Keywords: Gemini surfactant
Interaction
Protein
Secondary structure
Issue Date: 15-Oct-2006
Citation: Pi, Y., Shang, Y., Peng, C., Liu, H., Hu, Y., Jiang, J. (2006-10-15). Interactions between bovine serum albumin and gemini surfactant alkanediyl-α, ω-bis(dimethyldodecyl-ammonium bromide). Biopolymers 83 (3) : 243-249. ScholarBank@NUS Repository. https://doi.org/10.1002/bip.20552
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.
Source Title: Biopolymers
URI: http://scholarbank.nus.edu.sg/handle/10635/89264
ISSN: 00063525
DOI: 10.1002/bip.20552
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