Table of Contents
Conference Papers in Science
Volume 2014, Article ID 601546, 5 pages
Conference Paper

Dynamic Assessment of Fibrinogen Adsorption and Secondary Structure Perturbation

1Faculty of Bionics, Hochschule Rhine-Waal University of Applied Sciences, Marie-Curie-Straße 1, 47533 Kleve, Germany
2The Guy Hilton Research Centre, Keele University, Staffordshire ST4 7QB, UK

Received 22 November 2013; Accepted 12 February 2014; Published 7 April 2014

Academic Editors: J. Gough and R. Sammons

This Conference Paper is based on a presentation given by Gaurang Khot at “UK Society for Biomaterials Annual Conference 2013” held from 24 June 2013 to 25 June 2013 in Birmingham, United Kingdom.

Copyright © 2014 Gaurang Khot et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Fibrinogen is a protein being of prime importance for the initiation of clotting and thrombus formation, readily adsorbed onto surfaces presenting both hydrophilic and hydrophobic nature. The mechanism of adsorption, and thus the final presentation of this protein are therefore important for subsequent involvement for, for example, platelet adhesion. Biological activity can be controlled through careful consideration of material design; here we report kinetic assessment of fibrinogen adsorption onto plasma polymerised allylamine (hydrophilic) and hexane (hydrophobic) surfaces, using FTIR-ATR to inform on kinetics of adsorption, secondary structure evaluation, and orientational variation. Fibrinogen was found to respond differently to these two surfaces, adsorbing more rapidly to hydrophilic surfaces and losing an ordered secondary structure over a much longer timescale compared to hydrophobic surfaces.