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Journal of Biochemistry Advance Access originally published online on October 30, 2008
Journal of Biochemistry 2009 145(1):67-77; doi:10.1093/jb/mvn141
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© The Authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Spectroscopic Studies on the Comparative Interaction of Cationic Single-Chain and Gemini Surfactants with Human Serum Albumin

Nuzhat Gull1, Priyankar Sen2, Rizwan Hasan Khan2 and Kabir-ud-Din1,*

1Department of Chemistry; and 2Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202 002, India

*To whom correspondence should be addressed. Tel: +91-571-2703515 Extn. 3353, Fax: 0091-571-2708088, E-mail: kabir7{at}rediffmail.com

Received September 17, 2008; Accepted October 18, 2008


  Abstract

To gain insights into the comparative effect of single-chain/gemini surfactants on proteins and the possible implications, the interaction of human serum albumin (HSA) with cationic single-chain surfactant cetyltrimethylammonium bromide (CTAB) and its gemini counterpart bis(cetyldimethylammonium)butane dibromide with spacer –(CH2)4– (designated as G4) using turbidity measurements, far-UV and near-UV circular dichroism (CD), intrinsic fluorescence and extrinsic fluorescence spectroscopy at pH 7.0 are reported in this contribution. A decrease of 33.5% {alpha}-helical content at 22.5 µM G4 was monitored compared to a 15% decrease at 2,250 µM CTAB. Against a 3.5% increase at 11,250 µM CTAB, a rise of 21.1% in the {alpha}-helical content was observed 375 µM G4. The result is related to the stronger electrostatic and hydrophobic forces in G4, owing to the presence of two charged headgroups and two hydrophobic hydrocarbon tails that make it to bind strongly to the protein compared to its single chain counterpart, CTAB, resulting in larger unfolding. The stabilization at higher concentrations is attributed to the highly hydrophobic microdomain of the G4 aggregates formed at such concentrations. The results of the multi-technique approach are consistent with the fact that the gemini surfactants are more efficient than their conventional single-chain counterparts and hence may be used more effectively in the renaturation of proteins produced in the genetically engineered cells via the artificial chaperone protocol, as solubilizing agents to recover proteins from insoluble inclusion bodies and in drug delivery.

Key Words: aggregation, circular dichroism, gemini surfactants, human serum albumin, fluorescence spectroscopy

Abbreviations: CTAB, cetyltrimethylammonium bromide; HAS, Human serum albumin; RFI, relative fluorescence intensities


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