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Cyclic Analogues of Proline-Rich Protein Fragments : Part II : Conformational Studies Using NMR Spectroscopy and Theoretical Conformational Analysis

Rodziewicz S., Wirkus-Romanowska I., Ciurak M., Miecznikowska H., Kupryszewski G., Czaplewski C., Liwo A., Rolka K.

Polish Journal of Chemistry

1999

Vol. 73, nr 10

1697-1710

These peptides were designed based on the immunoregulatory activity of linear peptides obtained after chymotrypsin digestion of PRP. Despite the fact that the structures of both analogues cannot be interpreted in terms of a single conformation, the superposition of the most populated conformations of the cyclic peptides studied revealed a similar geometry for the Tyr-Val-pro-Leu-Phe-Pro fragment (RMSD=1.6 A) in both peptides and therefore might be considered to be responsible for the biological activity.

Conformational studies of tachykinin peptides using NMR spectroscopy

Rodziewicz S., Xiao-Fei Qi., Rolka K.

TASK Quarterly : scientific bulletin of Academic Computer Centre in Gdansk

1998

Vol. 2, No 1

47-53

Conformational analysis of two tachykinin family peptides: Scyliorhinin I (ScyI) and Scyliorhinin II (ScyII) was carried out by 1D- and 2D-NMR (DQF-COSY, TOCSY, HMQC, HMBC, NOESY and ROESY) and molecular dynamics calculation methods in water and DMSO. Scyliorhinin I is an equipotent agonist of NK-1 and NK-2 tachykinin receptors and Scyliorhinin II is a selective agonist of the NK-3 tachykinin receptor. In DMSO, two groups of conformations (major and minor) were obtained for both peptides based on the experimental data. The conformations proposed for ScyI represent a folded structure, which show certain similarities to the structures reported for other NK-1 and NK-2 tachykinin agonists. In water ScyII displays a flexible, extended structure, whereas in DMSO the structure is more compact and in the fragment from the centre to the C-terminus several beta -turns may be present.