Peptide design 310-helical conformation of a linear pentapeptide containing two dehydrophenylalanines, Boc-Gly-ΔZPhe-Leu-ΔZPhe-Ala-NHCH3

Chauhan, V. S. ; Bhandary, Krishna K. (1993) Peptide design 310-helical conformation of a linear pentapeptide containing two dehydrophenylalanines, Boc-Gly-ΔZPhe-Leu-ΔZPhe-Ala-NHCH3 Biopolymers, 33 (2). pp. 209-217. ISSN 0006-3525

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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/bip.360...

Related URL: http://dx.doi.org/10.1002/bip.360330203

Abstract

α,β-Dehydroamino acids are expected to provide conformational constraint to the peptide backbone. A pentapeptide containing two dehydrophenylalanines (ΔZPhe) separated by one L-amino acid has been synthesized and its solid state conformation determined. The pentapeptide, Boc-Gly-ΔZPhe-Leu-ΔZPhe-Ala-NHCH3, crystallizes from aqueous methanol in the orthorhombic space group P212121. There are four formula units, C35H46N6O7, in a unit cell of dimensions a = 10.155(3), b = 15.175(1), and c = 23.447(2) Å, at room temperature. The structure was solved by direct methods program, SIR88, and refined to a final R = 0.038 based on 3049 reflections with I >2σ(I). All the peptide links are trans and the backbone conformation of the pentapeptide can be described as a 310-helix, with mean Φ, ψ values of −65.1° and −22.8° (the value is averaged over the first four residues). There are four intramolecular 4 → 1 type hydrogen bonds characteristic of 310-type helices. In the crystal, the helices are held together by intermolecular N-H...O=C head-to-tail and lateral hydrogen bonding between symmetry related molecules. This mode of packing is similar to the packing motifs observed so often in other oligopeptides that adopt a 310-helical structure.

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Deposited On:26 Oct 2010 12:12
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