Circular dichroism analysis of cyclic β-helical peptides adsorbed on planar fused quartz.

Conformational changes of three cyclic β-helical peptides upon adsorption onto planar fused-quartz substrates were detected and analyzed by far-ultraviolet (UV) circular dichroism (CD) spectroscopy. In trifluoroethanol (TFE), hydrophobic peptides, Leu β and Val β, form left- and right-handed helices, respectively, and water-soluble peptide WS β forms a left-handed helix. Upon adsorption, CD spectra showed a mixture of folded and unfolded conformations for Leu β and Val β and predominantly unfolded conformations for WS β. X-ray photoelectron spectroscopy (XPS) provided insight about the molecular mechanisms governing the conformational changes, revealing that ca. 40% of backbone amides in Leu β and Val β were interacting with the hydrophilic substrate, while only ca. 15% of the amines/amides in WS β showed similar interactions. In their folded β-helical conformations, Leu β and Val β present only hydrophobic groups to their surroundings; hydrophilic surface groups can only interact with backbone amides if ...