Self-assembled monolayers with different terminating groups as model substrates for cell adhesion studies

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

  • N. Faucheux - , Helmholtz-Zentrum Hereon (Autor:in)
  • R. Schweiss - , Leibniz Institute of Polymer Research Dresden (Autor:in)
  • K. Lützow - , Helmholtz-Zentrum Hereon (Autor:in)
  • C. Werner - , Leibniz Institute of Polymer Research Dresden (Autor:in)
  • T. Groth - , Helmholtz-Zentrum Hereon (Autor:in)

Abstract

Cell shapes induced by cell-substratum interactions are linked with proliferation, differentiation or apoptosis of cells. To clarify the relevance of specific surface characteristics, we applied self-assembled monolayers (SAM) of alkyl silanes exhibiting a variety of terminating functional groups. We first characterised the SAMs on glass or silicon wafers by measuring wettability, layer thickness and roughness. Water contact angle data revealed that methyl (CH3), bromine (Br), and vinyl (CH=CH2) groups lead to hydrophobic surfaces, while amine (NH2) and carboxyl (COOH) functions lead to moderately wettable surfaces, and polyethylene glycol (PEG) and hydroxyl (OH) groups created wettable substrata. The surfaces were found to be molecular smooth except for one type of NH2 surface. The SDS-PAGE analysis of proteins adsorbed from bovine serum to the SAMs showed less protein adsorption to PEG and OH than to CH3, NH2 and COOH. Immunoblotting revealed that a key component of adsorbed proteins is vitronectin while fibronectin was not detectable. The interaction of human fibroblasts with CH3, PEG and OH terminated SAMs was similarly weak while strong attachment, spreading, fibronectin matrix formation and growth were observed on COOH and NH2. The strong interaction of fibroblasts with the latter SAMs was linked to an enhanced activity of integrins as observed after antibody-tagging of living cells.

Details

OriginalspracheEnglisch
Seiten (von - bis)2721-2730
Seitenumfang10
FachzeitschriftBiomaterials
Jahrgang25
Ausgabenummer14
PublikationsstatusVeröffentlicht - Juni 2004
Peer-Review-StatusJa
Extern publiziertJa

Externe IDs

PubMed 14962551
ORCID /0000-0003-0189-3448/work/162347729

Schlagworte

Schlagwörter

  • Fibronectin, Integrins, Protein adsorption, Self-assembled monolayers, Vitronectin