Surface-specific interaction of the extracellular domain of protein L1 with nitrilotriacetic acid-terminated self-assembled monolayers.

We report a study on the interaction of the extracellular domain of trans-membrane proteins N-cadherin and L1 with nitrilotriacetic acid (NTA)-terminated self-assembled monolayers (SAMs) grown on silver and gold surfaces. Quartz crystal microbalance (QCM) and reflection absorption infrared spectroscopy (RAIRS) measurements reveal that upon addition of protein to an NTA-SAM there is a subsequent change in the mass and average chemical structure inside the films formed on the metal substrates. By using vibrational sum frequency generation (VSFG) spectroscopy and making a comparison to SAMs prepared with n-alkanethiols, we find that the formed NTA-SAMs are terminated by ethanol molecules from solution. The ethanol signature vanishes after the addition of L1, which indicates that the L1 proteins can interact specifically with the NTA complex. Although the RAIRS spectra display signatures in the amide and fingerprint regions, the VSFG spectra display only a weak feature at 866 cm(-1), which possibly indicates that some of the abundant phenyl rings in the complex are ordered. Although cell biology experiments suggest the directional complexation of L1, the VSFG experiments suggest that the alpha-helices and beta-sheets of L1 lack any preferential ordering.