PET is Wonderful Annual Meeting 2020 Oct 27, 2020 02:00 PM - 05:40 PM — Virtual Meeting (online)
Through the Looking Glass: Breaking Barriers in STEM Oct 28, 2020 12:00 PM - 03:30 PM — Virtual Meeting (online)
NRS Mental Health Network Annual Scientific Meeting 2020 Nov 04, 2020 09:00 AM - 05:30 PM — Virtual Meeting (online)
Scottish Radiological Society Annual General Meeting 2020 Nov 06, 2020 09:30 AM - 03:30 PM — Virtual Meeting (online)


SINAPSE experts from around Scotland have developed ten online modules designed to explain medical imaging. They are freely available and are intended for non-specialists.

Edinburgh Imaging Academy at the University of Edinburgh offers the following online programmes through a virtual learning environment:

Neuroimaging for Research MSc/Dip/Cert

Imaging MSc/Dip/Cert

PET-MR Principles & Applications Cert

Applied Medical Image Analysis Cert

Online Short Courses

Protein adsorption onto CF3-terminated oligo(ethylene glycol) containing self-assembled monolayers (SAMs): the influence of ionic strength and electrostatic forces

Author(s): N. Bonnet, D. O'Hagan, G. Hahner

Oligo( ethylene glycol) (OEG) containing self-assembled monolayers (SAMs) on gold are known for their protein resistant properties. The underlying molecular mechanisms and the contributions of the interactions involved, however, are still not completely understood. It is known that electrostatic, van der Waals, hydrophobic, and hydration forces all play a role in the interaction between proteins and surfaces, but it is difficult to study their influence separately and to quantify their contributions. In the present study we investigate five different OEG containing SAMs and the influence of the ionic strength and the electrostatic component on the amount of a negatively charged protein (fibrinogen) that adsorbs onto them. Atomic force microscopy (AFM) was employed to record force-distance curves with hydrophobic probes depending on the ion concentration, and the amount of the protein that adsorbs relative to a hydrophobic surface was quantified using ellipsometry. The findings suggest that electrostatic forces can create a very low energy barrier thus only slightly decreasing the number of negatively charged proteins in solution with sufficient energy to approach the surface closely, and have a rather small influence on the amount that adsorbs. The films we investigated were not protein resistant. This supports other studies, reporting that a strong short-range repulsion as for example caused by hydration forces is required to make these films resistant to the non-specific adsorption of proteins.

Full version: Available here

Click the link to go to an external website with the full version of the paper

ISBN: 1463-9076
Publication Year: 2010
Periodical: Physical Chemistry Chemical Physics
Periodical Number: 17
Volume: 12
Pages: 4367-4374
Author Address: