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

Karina Kubiak-Ossowska, Paul A. Mulheran

Research output: Contribution to journalArticle

25 Citations (Scopus)

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.
LanguageEnglish
Pages8891-8900
Number of pages10
JournalJournal of Physical Chemistry B
Volume115
Issue number28
Early online date14 Jun 2011
DOIs
Publication statusPublished - 21 Jul 2011

Fingerprint

lysozyme
Muramidase
solid surfaces
surface reactions
Molecular dynamics
Agglomeration
Enzymes
molecular dynamics
proteins
Proteins
Adsorption
adsorption
eggs
mutations
Membrane Proteins
isolation
simulation

Keywords

  • egg white lysozyme
  • protein adsorption
  • Brownian dynamics
  • ionic strength
  • association
  • mechanisms
  • simulation
  • kinetics
  • mica

Cite this

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title = "Multiprotein interactions during surface adsorption: a molecular dynamics study of lysozyme aggregation at a charged solid surface",
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.",
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Multiprotein interactions during surface adsorption : a molecular dynamics study of lysozyme aggregation at a charged solid surface. / Kubiak-Ossowska, Karina; Mulheran, Paul A.

In: Journal of Physical Chemistry B, Vol. 115, No. 28, 21.07.2011, p. 8891-8900.

Research output: Contribution to journalArticle

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T2 - Journal of Physical Chemistry B

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AU - Mulheran, Paul A.

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AB - 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.

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