Molecular dynamics simulation of lysozyme adsorption/desorption on hydrophobic surfaces

Tao Wei, Marcelo Carignano, Igal Szleifer

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

In this work, we present a series of fully atomistic molecular dynamics (MD) simulations to study lysozyme's orientation-dependent adsorption on polyethylene (PE) surface in explicit water. The simulations show that depending on the orientation of the initial approach to the surface the protein may adsorb or bounce from the surface. The protein may completely leave the surface or reorient and approach the surface resulting in adsorption. The success of the trajectory to adsorb on the surface is the result of different competing interactions, including protein-surface interactions and the hydration of the protein and the hydrophobic PE surface. The difference in the hydration of various protein sites affects the protein's orientation-dependent behavior. Side-on orientation is most likely to result in adsorption as the protein-surface exhibits the strongest attraction. However, adsorption can also happen when lysozyme's longest axis is tilted on the surface if the protein-surface interaction is large enough to overcome the energy barrier that results from dehydrating both the protein and the surface. Our study demonstrates the significant role of dehydration process on hydrophobic surface during protein adsorption.

Original languageEnglish
Pages (from-to)10189-10194
Number of pages6
JournalJournal of Physical Chemistry B
Volume116
Issue number34
DOIs
Publication statusPublished - 30 Aug 2012
Externally publishedYes

Fingerprint

lysozyme
Muramidase
Molecular dynamics
Desorption
Enzymes
desorption
molecular dynamics
Adsorption
proteins
adsorption
Computer simulation
Proteins
Membrane Proteins
simulation
Polyethylene
Hydration
surface reactions
hydration
polyethylenes
Energy barriers

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Molecular dynamics simulation of lysozyme adsorption/desorption on hydrophobic surfaces. / Wei, Tao; Carignano, Marcelo; Szleifer, Igal.

In: Journal of Physical Chemistry B, Vol. 116, No. 34, 30.08.2012, p. 10189-10194.

Research output: Contribution to journalArticle

@article{02e981ac63e34eddaf98643f911b860b,
title = "Molecular dynamics simulation of lysozyme adsorption/desorption on hydrophobic surfaces",
abstract = "In this work, we present a series of fully atomistic molecular dynamics (MD) simulations to study lysozyme's orientation-dependent adsorption on polyethylene (PE) surface in explicit water. The simulations show that depending on the orientation of the initial approach to the surface the protein may adsorb or bounce from the surface. The protein may completely leave the surface or reorient and approach the surface resulting in adsorption. The success of the trajectory to adsorb on the surface is the result of different competing interactions, including protein-surface interactions and the hydration of the protein and the hydrophobic PE surface. The difference in the hydration of various protein sites affects the protein's orientation-dependent behavior. Side-on orientation is most likely to result in adsorption as the protein-surface exhibits the strongest attraction. However, adsorption can also happen when lysozyme's longest axis is tilted on the surface if the protein-surface interaction is large enough to overcome the energy barrier that results from dehydrating both the protein and the surface. Our study demonstrates the significant role of dehydration process on hydrophobic surface during protein adsorption.",
author = "Tao Wei and Marcelo Carignano and Igal Szleifer",
year = "2012",
month = "8",
day = "30",
doi = "10.1021/jp304057e",
language = "English",
volume = "116",
pages = "10189--10194",
journal = "Journal of Physical Chemistry B Materials",
issn = "1089-5647",
publisher = "American Chemical Society",
number = "34",

}

TY - JOUR

T1 - Molecular dynamics simulation of lysozyme adsorption/desorption on hydrophobic surfaces

AU - Wei, Tao

AU - Carignano, Marcelo

AU - Szleifer, Igal

PY - 2012/8/30

Y1 - 2012/8/30

N2 - In this work, we present a series of fully atomistic molecular dynamics (MD) simulations to study lysozyme's orientation-dependent adsorption on polyethylene (PE) surface in explicit water. The simulations show that depending on the orientation of the initial approach to the surface the protein may adsorb or bounce from the surface. The protein may completely leave the surface or reorient and approach the surface resulting in adsorption. The success of the trajectory to adsorb on the surface is the result of different competing interactions, including protein-surface interactions and the hydration of the protein and the hydrophobic PE surface. The difference in the hydration of various protein sites affects the protein's orientation-dependent behavior. Side-on orientation is most likely to result in adsorption as the protein-surface exhibits the strongest attraction. However, adsorption can also happen when lysozyme's longest axis is tilted on the surface if the protein-surface interaction is large enough to overcome the energy barrier that results from dehydrating both the protein and the surface. Our study demonstrates the significant role of dehydration process on hydrophobic surface during protein adsorption.

AB - In this work, we present a series of fully atomistic molecular dynamics (MD) simulations to study lysozyme's orientation-dependent adsorption on polyethylene (PE) surface in explicit water. The simulations show that depending on the orientation of the initial approach to the surface the protein may adsorb or bounce from the surface. The protein may completely leave the surface or reorient and approach the surface resulting in adsorption. The success of the trajectory to adsorb on the surface is the result of different competing interactions, including protein-surface interactions and the hydration of the protein and the hydrophobic PE surface. The difference in the hydration of various protein sites affects the protein's orientation-dependent behavior. Side-on orientation is most likely to result in adsorption as the protein-surface exhibits the strongest attraction. However, adsorption can also happen when lysozyme's longest axis is tilted on the surface if the protein-surface interaction is large enough to overcome the energy barrier that results from dehydrating both the protein and the surface. Our study demonstrates the significant role of dehydration process on hydrophobic surface during protein adsorption.

UR - http://www.scopus.com/inward/record.url?scp=84865697706&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84865697706&partnerID=8YFLogxK

U2 - 10.1021/jp304057e

DO - 10.1021/jp304057e

M3 - Article

VL - 116

SP - 10189

EP - 10194

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1089-5647

IS - 34

ER -