Different organization of type: collagen immobilized on silanized and nonsilanized titanium surfaces affects fibroblast adhesion and fibronectin secretion

Marín-Pareja, N., Cantini, M. , Gonzalez-Garcia, C., Salvagni, E., Salmeron-Sanchez, M. and Ginebra, M.-P. (2015) Different organization of type: collagen immobilized on silanized and nonsilanized titanium surfaces affects fibroblast adhesion and fibronectin secretion. ACS Applied Materials and Interfaces, 7(37), 20667. (doi:10.1021/acsami.5b05420) (PMID:26322620)

[img]
Preview
Text
111456.pdf - Accepted Version

3MB

Abstract

Silanization has emerged in recent years as a way to obtain a stronger and more stable attachment of biomolecules to metallic substrates. However, its impact on protein conformation, a key aspect that influences cell response, has hardly been studied. In this work, we analyzed by atomic force microscopy (AFM) the distribution and conformation of type I collagen on plasma-treated surfaces before and after silanization. Subsequently, we investigated the effect of the different collagen conformations on fibroblasts adhesion and fibronectin secretion by immunofluorescence analyses. Two different organosilanes were used on plasma-treated titanium surfaces, either 3-chloropropyl-triethoxy-silane (CPTES) or 3-glycidyloxypropyl-triethoxy-silane (GPTES). The properties and amount of the adsorbed collagen were assessed by contact angle, X-ray photoelectron spectroscopy, optical waveguide lightmode spectroscopy, and AFM. AFM studies revealed different conformations of type I collagen depending on the silane employed. Collagen was organized in fibrillar networks over very hydrophilic (plasma treated titanium) or hydrophobic (silanized with CPTES) surfaces, the latter forming little globules with a beads-on-a-string appearance, whereas over surfaces presenting an intermediate hydrophobic character (silanized with GPTES), collagen was organized into clusters with a size increasing at higher protein concentration in solution. Cell response was strongly affected by collagen conformation, especially at low collagen density. The samples exhibiting collagen organized in globular clusters (GPTES-functionalized samples) favored a faster and better fibroblast adhesion as well as better cell spreading, focal adhesions formation, and more pronounced fibronectin fibrillogenesis. In contrast, when a certain protein concentration was reached at the material surface, the effect of collagen conformation was masked, and similar fibroblast response was observed in all samples.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Salmeron-Sanchez, Professor Manuel and Cantini, Dr Marco and Gonzalez Garcia, Dr Cristina
Authors: Marín-Pareja, N., Cantini, M., Gonzalez-Garcia, C., Salvagni, E., Salmeron-Sanchez, M., and Ginebra, M.-P.
College/School:College of Science and Engineering > School of Engineering > Biomedical Engineering
Journal Name:ACS Applied Materials and Interfaces
Publisher:American Chemical Society
ISSN:1944-8244
ISSN (Online):1944-8252
Copyright Holders:Copyright © 2015 American Chemical Society
First Published:First published in ACS Applied Materials and Interfaces 7(37):20667
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

University Staff: Request a correction | Enlighten Editors: Update this record

Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
626901HEALINSYNERGY - Material-driven fibronectin fibrillogenesis to engineer synergistic growth factor microenvironmentsManuel Salmeron-SanchezEuropean Research Council (ERC)306990ENG - BIOMEDICAL ENGINEERING