Orientation of Oligopeptides in Self-Assembled Monolayers Inferred from Infrared Reflection-Absorption Spectroscopy

A series of a single tryptophan containing oligo-alanine peptides were recently characterized as conductive molecules that enable electron transport between electrodes. IR reflection-absorption of self-assembled monolayers of such peptides on gold surfaces revealed that the relative intensities of amide I and II bands in the respective spectra depend on the tryptophan residue position in the oligopeptide sequence. This indicates different average peptide orientations with respect to the normal onto the carrying gold surface. We developed a model which calculates the polarized reflectivities of the amide I and II bands as function of the angle of the incident light, the average peptide orientation and the relative orientations of peptide group at the N-terminal. The orientation and strength of vibrational transition dipole moments were calculated by employing an excitonic coupling approach which considers probable conformational distributions of the disordered peptides. Our results revealed that the position of the tryptophan can affect the effective tilt angle of the peptide as well as the orientation of transition dipole moments with respect to the reflection plane. We have also calculated the average end to end distances of the examined peptides and found them to be in reasonable agreement with experimental values determined by ellipsometry. Some evidence is obtained for the notion that increasing the tilt angle of the investigated peptides reduces their conductivity.