We report a methodology that permits quantitation of the azimuthal anchoring energy of the nematic liquid crystal 4-cyano-4'-pentyl-biphenyl on surfaces patterned with oligopeptides. The oligopeptide (IYGEFKKKC), an optimized substrate for the Src protein kinase, was covalently immobilized via the terminal cysteine to monolayers of amineterminated tetra(ethylene glycol) formed on gold films. The measurements of anchoring energies, which were based on a torque-balance method, revealed a systematic decrease in anchoring energy from 3.7 +/- 0.6 mu J/m(2) with increasing surface density of oligopeptide. We calculate that a mass density of oligopeptide of less than 1 ng/cm(2) can lead to a measurable change in the anchoring energy of the nematic liquid crystal. These results suggest that measurements of anchoring energies of liquid crystals on surfaces may offer the basis of quantitative and label-free methods for detecting biomolecules on surfaces.