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Conformational variability in short acyclic peptides. Stabilization of multiple ss-turn structures in organic solvents

DOI: 10.1039/P29960002701

Source and publish data:

Journal of the Chemical Society. Perkin Transactions 2 (2001) p. 2701 - 2706 (1996)

Update date:2022-08-29

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Authors:

Awasthi, Satish KumarAwasthi, Satish Kumar

Raghothama, Srinivasa RaoRaghothama, Srinivasa Rao

Balaram, PadmanabhanBalaram, Padmanabhan

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Article abstract of DOI:10.1039/P29960002701

The conformational characteristics of three hexapeptides Boc-Leu-Xxx-Val-Leu-Aib-Val-OMe (Xxx - Ala 1, D-Ala 2, Gly 3; Aib = α-aminoisobutyryl) have been probed in CDCl3 solution by NMR methods using solvent perturbation of chemical shifts and radical broadening of NH resonances to delineate intramolecularly hydrogen bonded NH groups. Nuclear Overhauser effects (NOEs) provide additional information on preferred backbone conformations. The substituent at position 2 acts as a major conformational determinant. While a continuous 310 helical conformation is favoured for the peptide with Xxx = Ala, a multiple ss-turns conformation is supported by both NMR and CD data for the peptide with Xxx = D-Ala. In the peptide with Xxx = Gly CD and NMR data suggest that both 310 helical and multiple turns conformations are simultaneously populated. The results suggest that incorporation of D-amino acids and Aib residues into all L-sequences may prove useful in generating sequences containing multiple turns.

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Product name:BOC-LEU-GLY-OH

Cas No:32991-17-6

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