Nmr and molecular dynamics studies of tachykinins: Conformation of substance p fragment 4-11

Journal of Biomolecular Structure and Dynamics

Volumn 16, Issue 3, 1998, Pages 747-755

  Coutinho, Evans ^a   Kamath, Shantaram ^a   Saran, Anil ^b   Srivastava, Sudha ^b  

^a BOMBAY COLLEGE OF PHARMACY   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

SUBSTANCE P; TACHYKININ;

ARTICLE; CALCULATION; CARBOXY TERMINAL SEQUENCE; INFLAMMATORY CELL; LIPID MEMBRANE; MAMMAL; MOLECULAR DYNAMICS; NERVE CELL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION;

EID: 0032452770     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.1998.10508286     Document Type: Article

References (35)

1. Dutta, AS. 1990. “ in “Tachykinin Receptors” in ”. In Comprehensive Medicinal Chemistry Edited by:Hansch, C., Sammes, PG, and Taylor, JB. Vol. 3, 1001Pergamon Press.
2. 6
3. Convert, O., Ploux, O., Lavielle, S., Cotrait, M., and Chassaing, G., 1988. Analysis of tachykinin-binding interactions using NMR and energy calculation data of potent cyclic analogues of Substance P. Biochem. Biophys. Ada., 954:287–302.
4. Convert, O., Duplaa, H., Lavielle, S., and Chassaing, G., 1991. Influence of the replacement of amino acid by its D-enantiomer in the sequence of Substance P. 2. Conformational analysis by NMR and energy calculations. Neuropeptides, 19:259–270.
5. Grdadolmik, SG, Mierke, DF, Zeltser, KG, I, Gilon, C., and Kessler, H., 1994. Comparison of conforma tion of active and nonactive cyclic analogs of substance P as a tool to elucidate features of bioac tive conformation:NMR and molecular dynamics in DMSO and water. J. Med. Chem., 37:2145–2152.
6. 1984. Peptides, 5:85–89. Hall ME and Stewart JM. Modulation of isolation-induced fighting by Nand C-terminal analogs of substance P; evidence for multiple recognition sites
7. Kulakowski, EC, Lampson, WA, Schaffer, SW, and Lovenberg, W. 1983. Action of Substance P on the working heart. Biochem. Pharmacol., 32:1097–1100.
8. 1979. Brain Res., 166:273–283. Zieglgausberger W and Tulloch IF, Effects of Substance P on neurons in the dorsal horn of the spinal cord of cat
9. Damonneville, M., Monte, D., Auriantt, C., and Capron, A., 1990. The neuropeptide substance P stimulates the effector functions of platelets. Clin. Exp. Immunol., 81:346–351.
10. Sumner, SC, Gallagher, KS, Davis, DG, Covell, DG, Jemigan, RL, and Ferretti, JA. 1990. Conformational analysis of the tachykinins in solution:Substance P and physalemin. J. Biomol. Struct. Dyn., 8:687–707.
11. Shukla, DR, and Mahajan, S., 1991. A magnetic resonance investigation of solution conformation of sub slance Pand its N-terminal fragment. Proleins,:85–95.
12. Chassaing, G., Convert, O., and Lavielle, S., 1986. Preferred conformation of substance P in solution. Eur. J. Biochem., 154:77–86.
13. Mehlis, B., Boehm, S., Becker, M., and Bienert, M., 1975. CD and IR studies of substance P. and carboxyterminal analogs. Biochem. Biophys. Res. Commun., 66:1447–1453.
14. Mehlis, B., Rueger, M., Becker, M., Bienert, N., Niedlich, H., and Oehme, P., 1980. CD studies of substance P and its C-terminal sequences. CD spectra in aqueous solutions and effects on hydrogen ion concentration. Int. J. Pepi. Prolein Res., 15:20–28.
15. Nikiforovich, GV, Balodis, I. Yu, and Cipens, G., 1981. Conformational function relations for substance P. Bioorg. Khim., 7:645–654.
16. Manavalan, P., and Momany, FA. 1982. Conformational energy calculations on substance P. Int. J. Pepi. Protein Res., 20:351–365.
17. th
18. Schwyzer, P., Eme, D., and Rolka, K., Membrance structure of substance P. Helv. Chim. Acta., 691789–1797.
19. Miyazawa, T., 1984. Active conformation of peptides analysed by molecular spectroscopy. Kagaku Kyoiku., 32:18–21.
20. Rolka, K., Eme, D., and Schwyzer, R., 1986. Membrane structure of substance P. II. Secondary structure of substance P., [9-Leu]S ub P. and shorter segments in 2,2,2-trifluroethanol, methanol and lipo somes studied by CD. Helv. Chim. Acta., 69:1798–1806.
21. Williams, RW, and Weaver, JL. 1990. Secondary structure of substance P bound liposomes in organic solvents and in solution from Raman and CD spectroscopy. J. Biol. Chem., 265:2505–2523.
22. Eme, D., Rolka, K., and Schwyzer, R., 1986. Membrane structure of substance P III. Secondary structure of substance P in 2,2,2-trifluoroethanol, methanol and on flat lipid membranes studied by IR spectroscopy. Helv. Chim. Acta, 69:1807–1816.
23. Hall, ME, and Stewart, JJ. Peptides, 4763–766.
24. 13C-NMR study of substance P fragment Arg-Pro-Lys-Pro
25. Kawaki, H., Otter, A., Beierbeck, H., Kotovych, G., and Stewart, JM. 1986. The conformational analysis of substance P analogs using highfield NMR techniques. J. BiomoI. Struct. Dyn., 3:795–803.
26. Szollosy, A., Otter, A., Stewart, JM, and Kotovych, G., 1986. An NMR study of the conformations of Nterminal substance P. fragments and antagonists. J. Biomol. Struct. Dyn., 4:501–519.
27. 7-11.). Ind. J. Biochem. Biophys., 34:435–448.
28. 2. Biochem. Biophys. Res. Commun., 109:1123–1128.
29. Saran, A., Srivastava, S., Coutinho, E., and Kamath, S., 1998. A Comparison of the conformation of a Eledoisin Related Peptide and the C-terminal pentapeptide of substance P by NMR and MD simulations. Physiol. Chem. Phy. Med. NMR, 29
30. Piantini, U., Sorenson, OW, and Ernst, RR. 1982. Multiple quantum filters for elucidating NMR cou pling networks. J. Am. Chem., 104:6800
31. Braunschweiler, L., and Ernst, RR. 1983. J. Magn. Reson., 53:521
32. Kumar, A., Ernst, RR, and Wüthrich, K., 1980. A two dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun., 95:1–6.
33. Bax, A., and Davis, DG. 1985. J. Magn. Reson., 63:207
34. Dauber Osguthorpe, P., Roberts, VA, Osguthorpe, DJ, Wolff, J., Genest, M., and Hagler, AT. 1988. Structure and energetics of ligand binding to proteins:E. coli dihydrofolate reductase-Trimethoprim, a drug receptor system. Proteins Struct. Function Genet., 4:31–47.
35. Bach, AC, II, Eyermann, CY, Gross, JD, Bower, MJ, Haflow, RL, Weber, PC, and Degrado, WF. 1994. Structural studies of a family of high affinity ligands for GPIIb/IIIa. J. Am. Chem. Soc., 116:3207–3209.