Conformational analysis reveals folded turn structures in protonated reduced dipeptides, indicating that modified amide bonds can mimic natural protein folds.
Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R" (rXbb, reduced analogue of residue Xbb: NH-C alpha HR1-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i+2 or i+3-->i interaction. The resulting conformation is similar to the y- or beta-turn structure found in peptides and proteins.
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Grand et al. (1996) studied this question.
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