Interfacial adsorption of fibrinogen and its inhibition by RGD peptide: a combined physical study

Abstract

The Arg–Gly–Asp (RGD) peptide sequence is known as a cell recognition site for numerous adhesive proteins present in the extracellular matrix (ECM) and in blood. Whilst surface immobilized RGD groups enhance cell attachment, RGD components present in solution can effectively inhibit cell attachment by competing with endogenous ligands for the same recognition site. In contrast to the widely reported binding to cell integrin, this study demonstrates a new RGD feature: its inhibitive effect on fibrinogen adsorption. Through a combined analysis of spectroscopic ellipsometry, neutron reflection and dual polarization interferometry, we show that the kinetic process of fibrinogen adsorption as a model pro-coagulant at the silica/solution interface and in the absence of any cells can be substantially reduced by the addition of RGD in solution and that the extent of the reduction is dependent on the relative concentration of RGD.

Dual polarization interferometry size and density characterisation of DNA immobilisation and hybridisation

“…Previously, this technique has been demonstrated for the monitoring of proteins Cross et al, 2003;Biehle et al, 2004;Armstrong et al, 2004;Freeman et al, 2004;Lu et al, 2004) and this paper is the first to report the analysis of nucleic acid based biointerfaces.…”

Adsorption and activity of Thermomyces lanuginosus lipase on hydrophobic and hydrophilic surfaces measured with dual polarization interferometry (DPI) and confocal microscopy

“…Two polarization states of the laser are used, which enables a continuous measure of the thickness and refractive index of the single homogeneous equivalent layer deposited on the sensing waveguide. More detailed descriptions about the instrumentation can be found elsewhere [23][24][25][26].…”

Surface enrichment of proteins at quartz/water interfaces: A neutron reflectivity study

“…Recently the specular reflection of neutrons has been used to characterize the adsorbed layer of albumin on lipid bilayers prepared on a silicon substrate [8] on a poly(acrylic acid) brush on silicon substrate [9], on self-assembled monolayers [10][11][12], on quartz [13], on silicon/water interfaces [14][15][16], on a hydrogel polymer [17], at air/water interfaces [18,19] the adsorption of lysozyme on silicon oxide and octadecyltrichlorosilane [20][21][22][23][24], and the adsorption of fibrinogen on silicon [25]. The use of neutron reflectivity in protein adsorption studies is very attractive because it can potentially give information about adsorbed layer profiles at subnanometer resolution.…”