Protein adsorption mechanisms on solid surfaces: lysozyme-on-mica

P.A. Mulheran, K. Kubiak

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

A methodology for discovering the mechanisms and dynamics of protein clustering on solid surfaces is reviewed and complemented by atomistic molecular dynamics (MD) simulations. In situ atomic force microscopy images of the early stages of protein film formation are quantitatively compared with Monte Carlo simulations, using cluster statistics to differentiate various growth models. We have studied lysozyme adsorption on mica as a model system, finding that all surface-supported clusters are mobile with diffusion constant inversely related to cluster size. Furthermore, our results suggest that protein monomers diffusing to the surface from solution only adhere to the bare surface with a finite probability. Fully atomistic MD simulations reveal that the lysozyme does indeed have a preferred orientation for binding to the surface, so that proteins with incorrect orientations move away from the surface rather than towards it. Agreement with experimental studies in the literature for the residues involved in the surface adsorption is found.
LanguageEnglish
Pages561-566
Number of pages5
JournalMolecular Simulation
Volume35
Issue number7
DOIs
Publication statusPublished - Jun 2009

Fingerprint

lysozyme
Mica
Muramidase
mica
Adsorption
solid surfaces
Enzymes
proteins
Proteins
Protein
adsorption
Molecular Dynamics Simulation
Molecular dynamics
molecular dynamics
simulation
Atomic Force Microscopy
Computer simulation
Growth Model
Differentiate
monomers

Keywords

  • biomaterials and biological interfaces
  • proteins
  • theory and modelling
  • computer simulation
  • diffusion of adsorbates
  • kinetics of coarsening and aggregation

Cite this

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abstract = "A methodology for discovering the mechanisms and dynamics of protein clustering on solid surfaces is reviewed and complemented by atomistic molecular dynamics (MD) simulations. In situ atomic force microscopy images of the early stages of protein film formation are quantitatively compared with Monte Carlo simulations, using cluster statistics to differentiate various growth models. We have studied lysozyme adsorption on mica as a model system, finding that all surface-supported clusters are mobile with diffusion constant inversely related to cluster size. Furthermore, our results suggest that protein monomers diffusing to the surface from solution only adhere to the bare surface with a finite probability. Fully atomistic MD simulations reveal that the lysozyme does indeed have a preferred orientation for binding to the surface, so that proteins with incorrect orientations move away from the surface rather than towards it. Agreement with experimental studies in the literature for the residues involved in the surface adsorption is found.",
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Protein adsorption mechanisms on solid surfaces: lysozyme-on-mica. / Mulheran, P.A.; Kubiak, K.

In: Molecular Simulation, Vol. 35, No. 7, 06.2009, p. 561-566.

Research output: Contribution to journalArticle

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KW - biomaterials and biological interfaces

KW - proteins

KW - theory and modelling

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KW - kinetics of coarsening and aggregation

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