Surface heterogeneity: A friend or foe of protein adsorption-insights from theoretical simulations

Penna, M, Ley, K, MacLaughlin, S and Yarovsky, I 2016, 'Surface heterogeneity: A friend or foe of protein adsorption-insights from theoretical simulations', Faraday Discussions, vol. 191, pp. 435-464.


Document type: Journal Article
Collection: Journal Articles

Title Surface heterogeneity: A friend or foe of protein adsorption-insights from theoretical simulations
Author(s) Penna, M
Ley, K
MacLaughlin, S
Yarovsky, I
Year 2016
Journal name Faraday Discussions
Volume number 191
Start page 435
End page 464
Total pages 30
Publisher Royal Society of Chemistry
Abstract A lack in the detailed understanding of mechanisms through which proteins adsorb or are repelled at various solid/liquid interfaces limits the capacity to rationally design and produce more sophisticated surfaces with controlled protein adsorption in both biomedical and industrial settings. To date there are three main approaches to achieve anti biofouling efficacy, namely chemically adjusting the surface hydrophobicity and introducing various degrees of surface roughness, or a combination of both. More recently, surface nanostructuring has been shown to have an effect on protein adsorption. However, the current resolution of experimental techniques makes it difficult to investigate these three phase systems at the molecular level. In this molecular dynamics study we explore in all-atom detail the adsorption process of one of the most surface active proteins, EAS hydrophobin, known for its versatile ability to self-assemble on both hydrophobic and hydrophilic surfaces forming stable monolayers that facilitate further biofilm growth. We model the adsorption of this protein on organic ligand protected silica surfaces with varying degrees of chemical heterogeneity and roughness, including fully homogenous hydrophobic and hydrophilic surfaces for comparison. We present a detailed characterisation of the functionalised surface structure and dynamics for each of these systems, and the effect the ligands have on interfacial water, the adsorption process and conformational rearrangements of the protein. Results suggest that the ligand arrangement that produces the highest hydrophilic chain mobility and the lack of significant hydrophobic patches shows the most promising anti-fouling efficacy toward hydrophobin. However, the presence on the protein surface of a flexible loop with amphipathic character (the Cys3-Cys4 loop) is seen to facilitate EAS adsorption on all surfaces by enabling the protein to match the surface pattern.
Subject Theory and Design of Materials
Nanomaterials
Theoretical and Computational Chemistry not elsewhere classified
DOI - identifier 10.1039/c6fd00050a
Copyright notice © The Royal Society of Chemistry 216
ISSN 1359-6640
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 13 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 2 times in Scopus Article | Citations
Altmetric details:
Access Statistics: 90 Abstract Views  -  Detailed Statistics
Created: Tue, 20 Dec 2016, 10:12:00 EST by Catalyst Administrator
© 2014 RMIT Research Repository • Powered by Fez SoftwareContact us