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Multiprotein interactions during surface adsorption : a molecular dynamics study of lysozyme aggregation at a charged solid surface

Kubiak-Ossowska, Karina and Mulheran, Paul A. (2011) Multiprotein interactions during surface adsorption : a molecular dynamics study of lysozyme aggregation at a charged solid surface. Journal of Physical Chemistry B, 115 (28). pp. 8891-8900. ISSN 1520-6106

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Abstract

Multiprotein adsorption of hen egg white lysozyme at a model charged ionic surface is studied using fully atomistic molecular dynamics simulations. Simulations with two, three, and five proteins, in various orientations with respect the surface, are performed over a 100 ns time scale. Mutated proteins with point mutations at the major (Arg128 and Arg125) and minor (Arg68) surface adsorption sites are also studied. The 100 ns time scale used is sufficient to observe protein translations, rotations, adsorption, and aggregation. Two competing processes of particular interest are observed, namely surface adsorption and protein-protein aggregation. At low protein concentration, the proteins first adsorb in isolation and can then reorientate on the surface to aggregate. At high concentration, the proteins aggregate in the solution and then adsorb in nonspecific ways. This work demonstrates the role of protein concentration in adsorption, indicates the residues involved in both types of interaction (protein-protein and protein-surface), and gives an insight into processes to be considered in the development of new functionalized material systems.

Item type: Article
ID code: 34011
Keywords: egg white lysozyme, protein adsorption, Brownian dynamics, ionic strength, association, mechanisms, simulation, kinetics, mica, Physical and theoretical chemistry, Materials Chemistry, Surfaces, Coatings and Films, Physical and Theoretical Chemistry
Subjects: Science > Chemistry > Physical and theoretical chemistry
Department: Faculty of Engineering > Chemical and Process Engineering
Related URLs:
    Depositing user: Pure Administrator
    Date Deposited: 11 Oct 2011 05:21
    Last modified: 28 Mar 2014 05:41
    URI: http://strathprints.strath.ac.uk/id/eprint/34011

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