Abstract
An extracellular matrix protein, fibronectin (Fn), was covalently immobilized on 316L stainless steel, L605 cobalt chromium (CoCr), and nickel titanium (NiTi) surfaces through an 11-mercaptoundecanoic acid (MUA) self-assembled monolayer (SAM) pre-formed on these surfaces. Polarization modulation infrared reflection adsorption spectroscopy (PM-IRRAS) confirmed the presence of Fn on the surfaces. The Fn monolayer attached to the SAM was found to be stable under fluid shear stress. Deconvolution of the Fn amide I band indicated that the secondary structure of Fn changes significantly upon immobilization to the SAM-functionalized metal substrate. Scanning electron microscopy and energy dispersive X-ray analysis revealed that the spacing between Fn molecules on a modified commercial stent surface is approximately 66 nm, which has been reported to be the most appropriate spacing for cell/surface interactions.