What governs protein adsorption and immobilization at a charged solid surface?

Karina Kubiak-Ossowska, Paul A. Mulheran

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The adsorption alien egg white lysozyme at a model charged surface is studied using fully atomistic molecular dynamics simulations. The simulations are performed over a 90 ns time scale which is sufficient to observe rotational and translational steps in the adsorption process. Electrostatics is found to play a key role in guiding the protein to the favorable binding orientation with the N,C-terminal face against the substrate. However, full immobilization appears to only occur through the strong interaction of Arg128 with the surface, facilitated by the protein's flexibility at the terminal face. Simulated mutation at this residue confirms its crucial role. This work demonstrates that electrostatics alone might not be sufficient to guide the development of material systems that exploit protein adsorption and immobilization.

LanguageEnglish
Pages7690-7694
Number of pages5
JournalLangmuir
Volume26
Issue number11
DOIs
Publication statusPublished - 1 Jun 2010

Fingerprint

immobilization
solid surfaces
proteins
Proteins
Adsorption
adsorption
Electrostatics
electrostatics
eggs
lysozyme
Muramidase
mutations
Molecular dynamics
flexibility
Enzymes
simulation
molecular dynamics
Computer simulation
Substrates

Keywords

  • egg white lysozyme
  • nanoparticles
  • orientation
  • mechanisms
  • simulation
  • dynamics
  • MICA

Cite this

Kubiak-Ossowska, Karina ; Mulheran, Paul A. / What governs protein adsorption and immobilization at a charged solid surface?. In: Langmuir. 2010 ; Vol. 26, No. 11. pp. 7690-7694.
@article{7b72e732d64346ea9b7ab409cbf2cb7e,
title = "What governs protein adsorption and immobilization at a charged solid surface?",
abstract = "The adsorption alien egg white lysozyme at a model charged surface is studied using fully atomistic molecular dynamics simulations. The simulations are performed over a 90 ns time scale which is sufficient to observe rotational and translational steps in the adsorption process. Electrostatics is found to play a key role in guiding the protein to the favorable binding orientation with the N,C-terminal face against the substrate. However, full immobilization appears to only occur through the strong interaction of Arg128 with the surface, facilitated by the protein's flexibility at the terminal face. Simulated mutation at this residue confirms its crucial role. This work demonstrates that electrostatics alone might not be sufficient to guide the development of material systems that exploit protein adsorption and immobilization.",
keywords = "egg white lysozyme, nanoparticles, orientation, mechanisms, simulation, dynamics, MICA",
author = "Karina Kubiak-Ossowska and Mulheran, {Paul A.}",
year = "2010",
month = "6",
day = "1",
doi = "10.1021/la101276v",
language = "English",
volume = "26",
pages = "7690--7694",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "11",

}

What governs protein adsorption and immobilization at a charged solid surface? / Kubiak-Ossowska, Karina; Mulheran, Paul A.

In: Langmuir, Vol. 26, No. 11, 01.06.2010, p. 7690-7694.

Research output: Contribution to journalArticle

TY - JOUR

T1 - What governs protein adsorption and immobilization at a charged solid surface?

AU - Kubiak-Ossowska, Karina

AU - Mulheran, Paul A.

PY - 2010/6/1

Y1 - 2010/6/1

N2 - The adsorption alien egg white lysozyme at a model charged surface is studied using fully atomistic molecular dynamics simulations. The simulations are performed over a 90 ns time scale which is sufficient to observe rotational and translational steps in the adsorption process. Electrostatics is found to play a key role in guiding the protein to the favorable binding orientation with the N,C-terminal face against the substrate. However, full immobilization appears to only occur through the strong interaction of Arg128 with the surface, facilitated by the protein's flexibility at the terminal face. Simulated mutation at this residue confirms its crucial role. This work demonstrates that electrostatics alone might not be sufficient to guide the development of material systems that exploit protein adsorption and immobilization.

AB - The adsorption alien egg white lysozyme at a model charged surface is studied using fully atomistic molecular dynamics simulations. The simulations are performed over a 90 ns time scale which is sufficient to observe rotational and translational steps in the adsorption process. Electrostatics is found to play a key role in guiding the protein to the favorable binding orientation with the N,C-terminal face against the substrate. However, full immobilization appears to only occur through the strong interaction of Arg128 with the surface, facilitated by the protein's flexibility at the terminal face. Simulated mutation at this residue confirms its crucial role. This work demonstrates that electrostatics alone might not be sufficient to guide the development of material systems that exploit protein adsorption and immobilization.

KW - egg white lysozyme

KW - nanoparticles

KW - orientation

KW - mechanisms

KW - simulation

KW - dynamics

KW - MICA

U2 - 10.1021/la101276v

DO - 10.1021/la101276v

M3 - Article

VL - 26

SP - 7690

EP - 7694

JO - Langmuir

T2 - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 11

ER -