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Small angle neutron scattering studies on the interaction of cationic surfactants with bovine serum albumin

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Abstract

The structure of the protein-surfactant complex of bovine serum albumin (BSA) and cationic surfactants has been studied by small angle neutron scattering. At low concentrations, the CTAB monomers are observed to bind to the protein leading to an increase in its size. On the other hand at high concentrations, surfactant molecules aggregate along the unfolded polypeptide chain of the protein resulting in the formation of a fractal structure representing a necklace model of micelle-like clusters randomly distributed along the polypeptide chain. The fractal dimension as well as the size and number of micelles attached to the complex have been determined.

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Authors and Affiliations

  1. Department of Chemistry, Aligarh Muslim University, Aligarh, 202 002, India

    Nuzhat Gull &  Kabir-Ud-Din

  2. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai, 400 085, India

    S. Chodankar & V. K. Aswal

Authors
  1. Nuzhat Gull
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  2. S. Chodankar
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  3. V. K. Aswal
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  4. Kabir-Ud-Din
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Correspondence to Kabir-Ud-Din.

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Gull, N., Chodankar, S., Aswal, V.K. et al. Small angle neutron scattering studies on the interaction of cationic surfactants with bovine serum albumin. Pramana - J Phys 71, 1027–1031 (2008). https://doi.org/10.1007/s12043-008-0218-6

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  • DOI: https://doi.org/10.1007/s12043-008-0218-6

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