Next Article in Journal
Injectable Systems for Intra-Articular Delivery of Mesenchymal Stromal Cells for Cartilage Treatment: A Systematic Review of Preclinical and Clinical Evidence
Next Article in Special Issue
Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics
Previous Article in Journal
Antagonism of Transient Receptor Potential Ankyrin Type-1 Channels as a Potential Target for the Treatment of Trigeminal Neuropathic Pain: Study in an Animal Model
Previous Article in Special Issue
Exploring Configuration Space and Path Space of Biomolecules Using Enhanced Sampling Techniques—Searching for Mechanism and Kinetics of Biomolecular Functions
Open AccessArticle

Adsorption of Fibronectin Fragment on Surfaces Using Fully Atomistic Molecular Dynamics Simulations

1
School Chemical Engineering, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK
2
Department of Chemical and Process Engineering, University of Strathclyde, James Weir Building, 75 Montrose Street, Glasgow G1 1XJ, UK
3
Department of Biomedical Engineering, University of Strathclyde, 106 Rottenrow, Glasgow G4 0NW, UK
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(11), 3321; https://doi.org/10.3390/ijms19113321
Received: 15 August 2018 / Revised: 15 October 2018 / Accepted: 23 October 2018 / Published: 25 October 2018
(This article belongs to the Special Issue Protein Structural Dynamics)
The effect of surface chemistry on the adsorption characteristics of a fibronectin fragment (FNIII8–10) was investigated using fully atomistic molecular dynamics simulations. Model surfaces were constructed to replicate self-assembled monolayers terminated with methyl, hydroxyl, amine, and carboxyl moieties. It was found that adsorption of FNIII8–10 on charged surfaces is rapid, specific, and driven by electrostatic interactions, and that the anchoring residues are either polar uncharged or of opposing charge to that of the targeted surfaces. On charged surfaces the presence of a strongly bound layer of water molecules and ions hinders FNIII8–10 adsorption. In contrast, adsorption kinetics on uncharged surfaces are slow and non-specific, as they are driven by van der Waals interactions, and the anchoring residues are polar uncharged. Due to existence of a positively charged area around its cell-binding region, FNIII8–10 is available for subsequent cell binding when adsorbed on a positively charged surface, but not when adsorbed on a negatively charged surface. On uncharged surfaces, the availability of the fibronectin fragment’s cell-binding region is not clearly distinguished because adsorption is much less specific. View Full-Text
Keywords: NAMD; self-assembled monolayers; SAMs; protein adsorption; explicit solvent NAMD; self-assembled monolayers; SAMs; protein adsorption; explicit solvent
Show Figures

Figure 1

MDPI and ACS Style

Liamas, E.; Kubiak-Ossowska, K.; Black, R.A.; Thomas, O.R.; Zhang, Z.J.; Mulheran, P.A. Adsorption of Fibronectin Fragment on Surfaces Using Fully Atomistic Molecular Dynamics Simulations. Int. J. Mol. Sci. 2018, 19, 3321.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop