Hydroxyl Density Affects the Interaction of Fibrinogen with Silica Nanoparticles at Physiological Concentration

Document Type



Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence

Publication Details

Journal of Colloid and Interface Sciences Available online 21 December 2013,

ISSN 0021-9797, http://dx.doi.org/10.1016/j.jcis.2013.12.025.

Access published version here


An increasing interest in the interaction between blood serum proteins and nanoparticles has emerged over the last years. In fact, this process plays a key role in the biological response to nanoparticles. The behavior of proteins at the biofluid/material interface is driven by the physico-chemical properties of the surface. However, much research is still needed to gain insight into the process at a molecular level.

In this study, the effect of silanol density on the interaction of fibrinogen at physiological concentrations with silica nanoparticle/flat surfaces has been studied.

Silica nanoparticles and silica wafers were modified and characterized to obtain a set of samples with different silanols density. The interaction with fibrinogen has been studied by evaluating the extent of coverage (bicinchoninic acid assay) and the irreversibility of adsorption (shift of the ζ potential). To clarify the molecular mechanism of fibrinogen/surface interactions, confocal micro-Raman spectroscopy (nanoparticles) and atomic force microscopy (wafers) were used. Finally the effect of fibrinogen on the agglomeration of nanoparticles has been evaluated by Flow Particle Image Analysis.

The data reported here show that a minimal variation in the state of the silica surface modifies the adsorption behavior of fibrinogen, which appears mediated by a competition between protein/protein and protein/surface interactions. By comparing the data obtained on nanoparticles and silicon-supported silica layers, we found that hydrophilicity increases the tendency of fibrinogen molecules to interact with the surface rather than with other molecules, thus inhibiting fibrinogen self-assembly.

This study contributes to the knowledge of the processes occurring at the surface/biological fluids interface, needed for the design of new biocompatible materials.




European Science Foundation

This document is currently not available here.