Conformational studies of tachykinin peptides using NMR spectroscopy

• Autorzy: Rodziewicz S. , Xiao-Fei Qi. , Rolka K.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

conformational analysis; tachykinin peptides; NMR spectroscopy; Scyliorhinin II; molecular dynamics calculation methods; DMSO

• Wydawca: Politechnika Gdańska
• Czasopismo: TASK Quarterly : scientific bulletin of Academic Computer Centre in Gdansk
• Rocznik: 1998
• Tom: Vol. 2, No 1
• Strony: 47--53
• Opis fizyczny: Bibliogr. 10 poz., rys.

Twórcy

autor

Rodziewicz S.

• Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland

autor

Xiao-Fei Qi.

• Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland

autor

Rolka K.

• Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland

Bibliografia

• [1] Conlon J.l f, Deacon C.F., O'Toole L. andThim, L„ FEBS Lett., 200 (1986) 111
• [2] Buck S.H. and Krastenansky J.L., Eur. J. Pharmacol., 144 (1987) 109
• [3] Beaujouan J. C., SafTroy M., Petitct F., Torrens Y. and Glowinski J., Eur. J. Pharmacol., 151 (1988)353
• [4] Patacchini R., Quartara L., Rolka K., Zboihska J., Kupryszcwski G. and Maggi C. A., Eur. J. Pharmacol., 250(1993)311
• [5] Bystrov V. F., Progr. NMR Spcctrosc. 10,(1976)41
• [6] Parti A., BilleterM. and Wuthrich K.,J. Mol. Biol. 180,(1984)741
• [7] Wiitrich K. (Ed.) NMR of Proteins and Nucleic Acids,Wiley Intersciences, New York, 1986
• [8] Saviano, G., Temussi, P. A., Motta, A., Maggi, C. A. and Rovero, P, Biochemistry, 30, (1991)10175.
• [9] Saultis J., Mierke D. F., Dyk G.. Gilon C. and Kessler H., J. Am. Chcm. Soc. 114,(1992)4818
• [10] Tallon M.,Ron D., Halle D., Amodeo P„ Saviano G., Temussi P. A., SclingerZ.,Naider F., Chorev M., Biopolymers, 33, (1993) 915