PROTEIN MONOLAYER FORMATION AT AIR–ELECTROLYTE INTERFACE: A LANGMUIR–BLODGETT STUDY

Prabir Pal, Tapanendu Kamilya, Mrityunjoy Mahato and G. B. Talapatra ()
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Prabir Pal: Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India
Tapanendu Kamilya: Department of Physics, Narajole Raj College, Narajole, Paschim Medinipur-721 211, India
Mrityunjoy Mahato: Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India
G. B. Talapatra: Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India

Surface Review and Letters (SRL), 2011, vol. 18, issue 06, 267-279

Abstract: The interfacial surface activity of a protein, ovalbumin (OVA) at bare air/water interface in presence and also in absence of electrolyte (KCl) in subphase has been investigated. The surface activity was measured as a function of time. It has been found that, the presence of KCl in aqueous subphase enhances the adsorption rate of the protein. The changes of area/molecule, compressibility, rigidity and unfolding of OVA are trivial up to 10 mM KCl concentration. These properties of OVA, above 10 mM KCl concentration are significant and have been explained in the perspective of DLVO theory and many-body ion–protein dispersion potentials. The presence of high concentration of electrolyte increases the β-structure of OVA, resulting into larger unfolding as well as larger intermolecular aggregates. The overall study indicates that KCl perturbs the OVA monolayer.

Keywords: Protein; surface activity; electrolytes; monolayer; unfolding; intermolecular aggregates (search for similar items in EconPapers)
Date: 2011
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DOI: 10.1142/S0218625X11014758

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