Molecular Dynamics Simulation of Lysozyme Adsorption/Desorption on Hydrophobic Surfaces

• Published in: The journal of physical chemistry. B Vol. 116; no. 34; pp. 10189 - 10194
• Main Authors: Wei, Tao, Carignano, Marcelo A, Szleifer, Igal
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 30.08.2012
• Subjects: Adsorption; Hydration; Hydrophobic and Hydrophilic Interactions; Lysozyme; Models, Molecular; Molecular dynamics; Molecular Dynamics Simulation; Muramidase - chemistry; Muramidase - metabolism; Polyethylene - chemistry; Polyethylenes; Proteins; Simulation; Surface chemistry; Surface Properties
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/jp304057e

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.