Rolf Tünnemann

Small interacting peptides. Part I. Interaction of cyclohexapeptides with an unspecific SiOH surface: comparison of infrared investigations and force field calculations

The interaction of cyclohexapeptides c(X(1)(1)K(2)X(2)(3)K(4)X(3)(5)K(6)) in water with hydrolysed silicon surfaces were studied by attenuated total reflection Fourier transform infrared (ATR FTIR) spectroscopy and by force field calculations. The band sequences (1800-1500 cm(-1)) for dissolved and adsorbed cyclohexapeptides were recorded and compared with those obtained after flushing with distilled water in order to eliminate the background signal of the peptides in solution. Band analyses and principal component analyses were carried out for the characteristic peptide vibrations in order to evaluate the spectra. In addition, force field calculations were performed to study the binding energies to the surface and to illustrate the possible structures of the cyclohexapeptides. The positively charged lysine side chains of the cyclohexapeptides interact with the OH groups of the surface, as indicated by band shifts. This also was verified by the force field calculations. The bonding stability increases with the number of interacting sites (lysine side chains and other peptide residues) to the surface. These sites are determined by structure and polarity of the cyclohexapeptides.