The rigid, rodlike polypeptide poly(gamma-benzyl L-glutamate) (PBLG) labeled at its N-terminus with a disulfide moiety (PBLGSS) was self-assembled (SA) on gold. In an attempt to influence PBLGSS alignment in situ, the orientation of the dipole moment along the PBLGSS helix axis was biased during self-assembly by applying a voltage between two gold electrodes in a solution of PBLGSS and electrolyte to generate a strong field (the electrical double layer) at the electrode interfaces. The resulting SA films were analyzed with X-ray photoelectron spectroscopy (XPS) and reflection-absorption Fourier transform infrared spectroscopy (RA-FTIRS). Both techniques indicated that greater polypeptide film coverage-more chemisorption-was present on the negative gold electrode compared with either the positive electrode or a SA control without a voltage applied. This is suggestive of helix orientation during poling, whereby the PBLGSS disulfide moiety is exposed preferentially to the negative electrode. However, there is minimal evidence of polypeptide order in the SA film (the poling field and solvent were removed prior to film analysis); the helix axes appeared to be Gaussian distributed about the substrate normal according to the RA-FTIRS analysis. Elemental percentages determined with XPS on the electrically-poled films were essentially identical to the unpoled control, indicating no redox processes had altered the PBLG molecular composition. Chemisorption was also seen on the positive electrode and is believed to he the result of solvent-mediated lateral-aggregation of PBLGSS into (apolar) species with disulfide moieties on both ends.