C12-Helix development in ()n sequences - spectroscopic characterization of Boc-Aib-4(R)Val]-OMe oligomers

The solution conformations of the -hybrid oligopeptides Boc-Aib-4(R)Val]n-OMe (n = 1-8) in organic solvents have been probed by NMR, IR, and CD spectroscopic methods. In the solid state, this peptide series favors C12-helical conformations, which are backbone-expanded analogues of 310 helices in -peptide sequences. NMR studies of the six- (n = 3) and 16-residue (n = 8) peptides reveal that only two NH protons attached the N-terminus residues Aib(1) and 4(R)Val(2) are solvent-exposed. Sequential NiH-Ni+1H NOEs characteristic of local helical conformations are also observed at the residues. IR studies establish that chain extension leads to a large enhancement in the intensities of the hydrogen-bonded NH stretching bands (3343-3280 cm-1), which suggest elongation of intramolecularly hydrogen-bonded structures. The development of C12-helical structures upon lengthening of the sequence is supported by the NMR and IR observations. The CD spectra of the ()n peptides reveal a negative maximum at ca. 206 nm and a positive maximum at ca. 192 nm, spectral feature that are distinct from those of 310 helices in -peptides.