Bonding strength of fluorinated and hydrogenated surfactant to bovine serum albumin |
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Authors: | Ling Li Gongwu Song Paul K. Chu |
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Affiliation: | a Ministry-of-Education Key Laboratory for the Synthesis and Application of Organic Function Molecules, Hubei University, Wuhan 430062, China b Department of Physics & Materials Science, City University of Hong Kong, Tat Chee Avenue, Kowloon, Hong Kong, China |
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Abstract: | The interactions between bovine serum albumin (BSA) and different surfactants are investigated by the fluorescence technique. Pairs of fluorinated and hydrogenated surfactants with similar hydrophobic chain lengths including potassium perfluorooctanesulfonate and sodium octanesulfonate are studied in order to determine their interactions with BSA. The binding constants and thermodynamic parameters between BSA and different surfactants are compared and the main binding strength is determined. The mechanism of quenching and change of particle size gives rise to the binding force. Based on the FRET theory, the distances between potassium perfluorooctanesulfonate/sodium octanesulfonate and BSA are calculated and it is found that the fluorinated surfactant exhibits stronger interactions with proteins than the hydrogenated one, which is also proved by zeta potential and TEM. |
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Keywords: | Fluorinated/hydrogenated surfactant BSA Quenching Energy transfer Interaction |
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