↓ Skip to main content

Surface heterogeneity: a friend or foe of protein adsorption – insights from theoretical simulations

Overview of attention for article published in Faraday Discussions of the Chemical Society, January 2016
Altmetric Badge

Mentioned by

twitter
1 tweeter

Citations

dimensions_citation
9 Dimensions

Readers on

mendeley
22 Mendeley
Title
Surface heterogeneity: a friend or foe of protein adsorption – insights from theoretical simulations
Published in
Faraday Discussions of the Chemical Society, January 2016
DOI 10.1039/c6fd00050a
Pubmed ID
Authors

Matthew Penna, Kamron Ley, Shane Maclaughlin, Irene Yarovsky

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.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Poland 1 5%
Unknown 21 95%

Demographic breakdown

Readers by professional status Count As %
Researcher 6 27%
Student > Ph. D. Student 5 23%
Professor 2 9%
Student > Master 2 9%
Lecturer > Senior Lecturer 1 5%
Other 2 9%
Unknown 4 18%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 5 23%
Physics and Astronomy 4 18%
Chemistry 3 14%
Materials Science 2 9%
Agricultural and Biological Sciences 1 5%
Other 2 9%
Unknown 5 23%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 28 July 2016.
All research outputs
#7,056,636
of 8,148,366 outputs
Outputs from Faraday Discussions of the Chemical Society
#415
of 507 outputs
Outputs of similar age
#218,177
of 257,953 outputs
Outputs of similar age from Faraday Discussions of the Chemical Society
#7
of 10 outputs
Altmetric has tracked 8,148,366 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 507 research outputs from this source. They receive a mean Attention Score of 1.8. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 257,953 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 10 others from the same source and published within six weeks on either side of this one. This one has scored higher than 3 of them.