Abstract
The first structural investigations were undertaken on a β-hexapeptide 7 in which the peptide backbone is constrained by cis-substituted oxetane rings. Detailed NMR studies in CDCl 3 and C 6D 6 together with molecular mechanics conformational analysis identify a well-defined left-handed helical structure stabilised by 10-membered hydrogen-bonded rings. Comparison with two related hexapeptides 8 and 9 suggests a similar structural preference for these systems.
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