Abstract
Several model peptides containing α, β-dehydrophenylalanine (ΔPhe) in both Z and E configurations were studied for β-turn stability at the AM1 level of theory. Both configurations of ΔPhe are well able to stabilize β-turns in the backbone. However, the β-turns for peptides bearing Z-ΔPhe are energetically more stable than the E-counterparts. The difference in energies between the global minima of these peptides having the Z and E configuration of ΔPhe, is dictated by the size and stereochemistry of residues flanking ΔPhe. One distinct feature of E-ΔPhe is that it pushes peptides to adopt a Type II β-turn with the ΔPhe residue in the (i + 1) position of the turn. This unique feature may be exploited in peptide design.
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Desai, P.V., Coutinho, E.C. Effect of Stereochemistry (Z and E) and Position of α,β-Dehydrophenylalanine (ΔPhe) on β-turn Stability. J Mol Model 6, 595–599 (2000). https://doi.org/10.1007/s0089400060595
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DOI: https://doi.org/10.1007/s0089400060595