Interactions between adsorbed layers of αS1-Casein with covalently bound side chains : a self-consistent field study

Akinshina, A, Ettelaie, R, Dickinson, E and Smyth, G 2008, 'Interactions between adsorbed layers of αS1-Casein with covalently bound side chains : a self-consistent field study' , Biomacromolecules, 9 (11) , pp. 3188-3200.

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Abstract

The effect on the adsorbed layer properties of the modification of αS1-casein by covalent bonding with an uncharged polysaccharide side chain has been investigated using lattice-based self-consistent field (SCF) theory. Interactions between two hydrophobic planar surfaces coated by a layer of adsorbed modified αS1-casein have been studied as a function of pH and ionic strength. While the interactions of the unmodified αS1-casein layers become attractive at high ionic strength, it has been shown that the presence of polysaccharide attachment to the αS1-casein molecule can confer net repulsive interactions over a wide range of salt concentration. The disordered protein is represented as a linear flexible polyampholyte with a sequence of hydrophobic, polar, and charged units based on the known αS1-casein primary structure. The hydrophilic side chain is attached at various fixed positions along the casein backbone. Different lengths and locations of the attached polysaccharide side chain are examined. Interfacial structures and colloidal stability properties of the system are determined, including the surface−surface interaction potential, the extent of protein bridging, and the distribution of protein segments from the surface under different conditions of pH and ionic strength. It has been found that the covalent bonding of short hydrophilic chains may not only enhance but can also worsen the colloidal stabilizing properties of the modified protein, depending on the position of the attachment.

Item Type: Article
Schools: Schools > School of Environment and Life Sciences > Biomedical Research Centre
Journal or Publication Title: Biomacromolecules
Publisher: American Chemical Society
ISSN: 1525-7797
Related URLs:
Depositing User: A Akinshina
Date Deposited: 03 Mar 2017 09:29
Last Modified: 08 Aug 2017 11:58
URI: http://usir.salford.ac.uk/id/eprint/41435

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