Immobilisation of cell-binding peptides on poly-ε-caprolactone (PCL) films: A comparative XPS study of two chemical surface functionalisation methods

Successful interaction between cells and biomaterial surfaces is crucial for biomedical devices, and incorporation of peptides such as RGD (Arg-Gly-Asp) at the polymer interface can substantially promote cell adhesion and proliferation. X-ray photoelectron spectroscopy (XPS) has been used to characterise poly-epsilon-caprolactone (PCL) films modified by aminolysis and the introduction of RGD peptides via carbodiimide (CDI) and thiol-halogen 'click' chemistry. The nitrogen signal acts as an elemental indicator for successful attachment, and changes in the chemical environment are reflected in the carbon and oxygen spectra. Chlorine and sulfur provide additional chemical indicators of reaction progress in the thiol method, with the selective nature of the Cl-S reaction reflected in the complete loss of Cl signal and appearance of S, avoiding potential amine-peptide side-reactions. Comparison of the XPS elemental concentrations indicated an estimate of 2-3% peptide functionalisation on the PCL surface for both methods, correlating with the improvement in Schwann cell response observed after peptide immobilisation. The enhanced selectivity of peptide attachment to the polymer surface demonstrated with XPS for the novel method based on thiol chemistry shows its potential for development as a biomimetic scaffold for peripheral nerve injury. Copyright (C) 2014 John Wiley & Sons, Ltd.