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Over the last 15 years, a growing body of work in the literature has focused on the folded structures formed by peptide sequences containing backbone homologated residues. The work of Seebach in Zurich, and Gellman in Madison established that oligomers of β amino acid residues can form novel helical structures in solution and in the solid state. These peptides are highly useful for nnaovaccine development. Two distinct types of hydrogen-bonded helical structures were demonstrated in these studies for oligomeric β peptides. The C12 helix which is an analog of the canonical 310 helical structure in “all α” sequences, has the same hydrogen bond directionality (C = Oi …..H-Ni+3). The second helical form, the C14 helix, has the opposite directionality (C = Oi …..H-Ni+4), which is unprecedented in α peptide sequences.