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Chem. Commun., 1997, 2015 - 2022, DOI: 10.1039/a704933a

-Peptides: a surprise at every turn

Dieter Seebach and Jennifer L. Matthews

-Peptides, i.e. oligomers of -amino acids, containing as few as six residues may form surprisingly stable helices, with half-lives for the H/D exchange of the central NH protons of up to several days. Furthermore, these -peptides (carrying the side chains of familiar -amino acids such as Ala, Val, Leu, Phe, Lys in the 2- and/or 3-position of their 3-amino carboxylic moieties) have been shown to be stable to common peptidases for at least two days. In this article, a brief account of the results obtained since we started work in this area in early 1995 is given. The synthesis of enantiopure -amino acids can be achieved by homologation of -amino acids. The greater structural variability of -amino acids leads to an even greater multitude of possible -peptide primary and secondary structures. Circular dichroism, NMR and X-ray investigations have unveiled helical, pleated-sheet and tubular arrangements of linear and cyclic -peptides composed of up to twelve -amino acids. The prospects for the use of -peptides as drugs, the construction of large, enzymatically-active -proteins and their interaction with the natural, -peptidic counterparts are discussed.