TY - JOUR
T1 - Hydroxyl density affects the interaction of fibrinogen with silica nanoparticles at physiological concentration
AU - Marucco, Arianna
AU - Turci, Francesco
AU - O'Neill, Luke
AU - Byrne, Hugh J.
AU - Fubini, Bice
AU - Fenoglio, Ivana
N1 - Funding Information:
The authors gratefully acknowledge the European Science Foundation for the Grant used for performing the AFM data at the FOCAS Research Institute in Dublin. The grant is linked with the Research Networking Programmes in Physical and Engineering Sciences entitled: “Mapping the detailed composition (epitope exposure) of surface-adsorbed protein layers on biomaterials and nanoparticles – an alternative approach to biocompatibility and nanotoxicity (EpitopeMap)”.
PY - 2014/4/1
Y1 - 2014/4/1
N2 - 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.
AB - 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.
KW - Amorphous silica
KW - Fibrinogen interactions
KW - Silanol density
KW - Surface hydrophilicity
UR - http://www.scopus.com/inward/record.url?scp=84892466552&partnerID=8YFLogxK
U2 - 10.1016/j.jcis.2013.12.025
DO - 10.1016/j.jcis.2013.12.025
M3 - Article
C2 - 24491335
AN - SCOPUS:84892466552
SN - 0021-9797
VL - 419
SP - 86
EP - 94
JO - Journal of Colloid and Interface Science
JF - Journal of Colloid and Interface Science
ER -