Structural studies on Hgr3 orphan receptor ligand prolactin-releasing peptide

Journal of Medicinal Chemistry

Volumn 45, Issue 25, 2002, Pages 5483-5491

  D'Ursi, Anna Maria ^a   Albrizio, Stefania ^b   Di Fenza, Armida ^a   Crescenzi, Orlando ^b   Carotenuto, Alfonso ^a   Picone, Delia ^b   Novellino, Ettore ^b   Rovero, Paolo ^a  

^a UNIVERSITY OF SALERNO   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

DODECYL SULFATE SODIUM; NEUROPEPTIDE Y RECEPTOR; PROLACTIN RELEASING FACTOR; RECEPTOR; RECEPTOR HGR3; UNCLASSIFIED DRUG; WATER;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; DRUG ACTIVITY; DRUG SYNTHESIS; MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

EID: 0037028052     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm020975p     Document Type: Article

References (57)

1. Stadel, J. M.; Wilson, S.; Bergsma, D. J. Orphan G-protein-coupled receptors, a neglected opportunity for pioneer drug discovery. TIPS 1997, 18, 430-437.
2. Wilson, S.; Bergsma, D. J.; Chambers, J. K.; Muir, A. I.; Fantom, K. G. M.; Ellis, C.; Murdock, P. R.; Herrity, N. C.; Stadel, J. M. Orphan G-protein-coupled receptors, the next generation of drug targets? Br. J. Pharmacol. 1998, 125, 1387-1392.
3. Hamm, H. E. The Many Faces of G Protein Signali. J. Biol. Chem. 1998, 273, 669-672.
4. Civelli, O.; Reinscheid, R. K.; Nothacker, H. P. Orphan receptors, novel neuropeptides and reverse phamaceutical research. Brain Res. 1999, 848, 63-65.
5. Hinuma, S.; Habata, Y.; Fujii, R.; Kawamata, Y.; Hosoya, M.; Fukusumi, S.; Kitada, C.; Masuo, Y.; Asano, T.; Matsumoto, H.; Sekiguchi, M.; Kurokawa, T.; Nishimura, O.; Onda, H.; Fujino, M. A prolactin-releasing peptide in the brain. Nature 1998, 393, 272-302.
6. Hinuma, S.; Onda, H.; Fujino, M. The quest for novel bioactive peptides utilizing orphan seven-transmembrane-domain receptors. J. Mol. Med. 1999, 77, 495-504.
7. Marchese, A.; Heiber, M.; Nguyen, T.; Heng, H. H.; Saldivia, V. R.; Cheng, R.; Murphy, P. M.; Tsui, L. C.; Shi, X.; Gregor, P. Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors. Genomics 1995, 29 (2), 335-344.
8. Welch, S. K.; O'Hara, B. F.; Kilduff, T. S.; Heller, H. C. Sequence and tissue distribution of a candidate G-coupled receptor cloned from rat hypothalamus. Biochem. Biophys. Res. Commun. 1995, 209 (2), 606-613.
9. Roland, B. L.; Sutton, S. W.; Wilson, S. J.; Luo, L.; Pyati, J.; Huvar, R.; Erlander, M. G.; Lovenberg, T. W. Anatomical distribution of prolactin-releasing peptide and its receptor suggests additional functions in the central nervous system and periphery. Endocrinology 1999, 140, 5736-5745.
10. Ibata, Y.; Iijima, N.; Kataoka, Y.; Kakihara, K.; Tanaka, M.; Hosoya, M.; Hinuma, S. Morphological survey of prolactin-releasing peptide and its receptor with special reference to their functional roles in the brain. Neurosci. Res. 2000, 38 (3), 223-230.
11. Matsumoto, H.; Maruyama, M.; Noguchi, J.; Horikoshi, Y.; Fujiwara, K.; Kitada, C.; Hinuma, S.; Onda, H.; Nishimura, O.; Inoue, K.; Fujino, M. Stimulation of corticotropin-releasing hormone-mediated adrenocorticotropin secretion by central administration of prolactin-releasing peptide in rats. Neurosci. Lett. 2000, 285 (3), 234-238.
12. Seal, L. J.; Small, C. J.; Kim, M. S.; Stanley, S. A.; Taheri, S.; Ghatei, M. A.; Bloom, S. R. Prolactin releasing peptide (PrRP) stimulates luteinizing hormone (LH) and follicle stimulating hormone (FSH) via a hypothalamic mechanism in male rats. Endocrinology 2000, 141, 1909-1912.
13. Lawrence, C. B.; Celsi, F.; Brennand, J.; Luckman, S. M. Alternative role for prolactin-releasing peptide in the regulation of food intake. Nat. Neurosci. 2000, 7, 645-646.
14. Ellacott, K. L.; Lawrence, C. B.; Rothwell, N. J.; Luckman, S. M. PRL-releasing peptide interacts with leptin to reduce food intake and body weight. Endocrinology 2002, 143 (2), 368-374.
15. Lin, S. H.; Arai, A. C.; Wang, Z.; Nothacker, H. P.; Civelli, O. The carboxyl terminus of the prolactin-releasing peptide receptor interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor clustering. Mol. Pharmacol. 2001, 60, 916-924.
16. Grundemar, L.; Sheikh, S. P.; Wahlestedt, C. In Biology of Neuropeptide Y and Related Peptides; Colmers, W. F., Wahlestedt, C., Eds.; Humana Press: Totowa, NJ, 1993; pp 197-239.
17. Inui, A. Neuropeptide Y feeding receptors: Are multiple subtypes involved? Trends Pharmacol. Sci. 1999, 20, 43-46.
18. Darbon, H.; Bernassau, J. M.; Deleuze, C.; Chenu, J.; Roussel, A.; Cambillau, C. Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics. Eur. J. Biochem. 1992, 209 (2), 765-771.
19. Khiat, A.; Labelle, M.; Boulanger, Y. Three-dimensional structure of the Y1 receptor agonist [Leu31, Pro34]NPY as determinated by NMR and molecular modeling. J. Pept. Res. 1998, 51 (4), 317-322.
20. Allen, J.; Novotny, J.; Martin, J.; Heinrich, G. Molecular structure of mammalian neuropeptide Y: Analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 2532-2536.
21. Monks, S. A.; Karagianis, G.; Howlett, G. J.; Norton, R. S. Solution structure of human neuropeptide Y. J. Biomol. NMR 1996, 8, 379-390.
22. Bader, R.; Bettio, A.; Beck-Sickinger, A. G.; Zerbe, O. Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection. J. Mol. Biol. 2001, 305, 307-329.
23. Douzou, P.; Petsko, G. A. Proteins at work: "Stop-Action" pictures at subzero temperatures. Adv. Protein Chem. 1984, 36, 245-361.
24. Fink, A. L. Protein folding in cryosolvents at subzero temperatures. Methods Enzymol. 1986, 131, 173-187.
25. Amodeo, P.; Motta, A.; Picone, D.; Saviano, G.; Tancredi, T.; Temussi, P. A. Viscosity as a conformational sieve. NOE of linear peptides in cryoprotective mixtures. J. Magn. Reson. 1991, 95, 201-207.
26. Hamada, D.; Kuroda, Y.; Tanaka, T.; Goto, Y. High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. J. Mol. Biol. 1995, 254, 737-746.
27. Shiraki, K.; Nishikawa, K.; Goto, Y. Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: Implication for non-hierarchical protein folding. J. Mol. Biol. 1995, 254, 180-194.
28. Sonnichsen, F. D.; Van Eyk, J. E.; Hodges, R. S.; Sykes, B. D. Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide. Biochemistry 1992, 31, 8790-8798.
29. Rajan, R.; Awasthi, S. K.; Bhattachajya, S.; Balaram, P. Teflon-coated peptides: Hexafluoroacetone trihydrate as a structure stabilizer for peptides. Biopolymers 1997, 42, 125-128.
30. Saviano, G.; Crescenzi, O.; Picone, D.; Temussi, P. A.; Tancredi, T. Solution structure of human β-endorphin in helicogenic solvents: A NMR study. J. Pept. Sci. 1999, 5, 410-422.
31. Romano, R.; Dufresne, M.; Prost, M. C.; Bali, J. P.; Bayerl, T. M.; Moroder, L. Peptide hormone-membrane interactions. Intervesicular transfer of lipophilic gastrin derivative to artificial membranes and their bioactivities. Biochim. Biophys. Acta 1993, 1145, 235-242.
32. Moroder, L.; Romano, R.; Guba, W.; Mierke, D. F.; Kessler, H.; Delporte, C.; Winand, J.; Christophe, J. New evidence for a membrane bound pathway in hormone receptor binding. Biochemistry 1993, 32, 13551-13559.
33. Schwyzer, R. In Natural Products and Biological Activities; Imura, H., Goto, T., Murachi, T., Nakajima, T., Eds.; Tokyo Press and Elsevier: Tokyo, 1986; pp 197-207.
34. Schwyzer, R. Peptide-membrane interactions and a new principle in quantitative structure-activity realtionships. Biopolymers 1991, 31, 785-792.
35. Sargent, D. F.; Schwyzer, R. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 5774-5778.
36. Schwyzer, R. Estimated conformation, orientation, and accumulation of dynorphin A-(1-13)-tridecapeptide on the surface of neutral lipid membranes. Biochemistry 1986, 25, 4281-4286.
37. Schwyzer, R. How do peptides interact with lipid membranes and how does this affect their biological activity? Braz. J. Med. Biol. Res. 1992, 25, 1077-1089.
38. Wüthrich, K. NMR of Proteins and Nucleic Acids; John Wiley & Sons: New York, 1986.
39. Piantini, U.; Soerensen, O. W.; Ernst, R. R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 1982, 104, 6800-6801.
40. Bax, A.; Davis, D. G. Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985, 65, 355-360.
41. Jeener, J.; Meyer, B. H.; Bachman, P.; Ernst, R. R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 1979, 71, 4546-4553.
42. Bartels, C.; Xia, T.; Billeter, M.; Guentert, P.; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 1995, 6, 1-10.
43. Wishart, D. S.; Sykes, B. D.; Richards, F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 1991, 222, 311-333.
44. Wishart, D. S.; Sykes, B. D.; Richards, F. M. The chemical shift index. A fast and simple method for the assignment of protein secondary structure trough NMR spectroscopy. Biochemistry 1992, 31, 1647-1651.
45. Dyson, H. J.; Rance, M.; Houghten, R. A.; Wright, P. E.; Lerner, R. A. Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J. Mol. Biol. 1988, 201, 201-217.
46. Guntert, P.; Mumenthaler, C.; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 1997, 273, 283-298.
47. Weiner, S. J.; Kollman, P. A.; Case, D. A.; Singh, U. C.; Chio, C.; Alagona, G.; Profeta, S.; Weiner, P. J. Am. Chem. Soc. 1984, 106, 765.
48. Case, D. A.; Pearlman, D. A.; Caldwell, J. W.; Cheatham, T. E., III; Ross, W. S.; Simmerling, C. L.; Darden, T. A.; Merz, K. M.; Stanton, R. V.; Cheng, A. L.; Vincent, J. J.; Crowley, M.; Ferguson, D. M.; Radmer, R. J.; Seibel, G. L.; Singh, U. C.; Weiner, P. K.; Kollman, P. A. AMBER 5; University of California, San Francisco: San Francisco, CA, 1997.
49. Eilers, M.; Shekar, S. C.; Shieh, T.; Smith, S. O.; Fleming, P. J. Internal packing of helical membrane proteins. Proc. Natl. Acad. Sci. 2000, 97, 5796-5801.
50. 1H NMR. Biochemistry 1997, 36 (26), 8153-8163.
51. Lindberg, M.; Jarvet, J.; Langel, U.; Graslund, A. Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry 2001, 40 (10), 3141-3149.
52. Thompson, J. D.; Higgins, D. G.; Gibson, T. J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22, 4673-4680.
53. Cabrele, C.; Beck-Sickinger, A. G. Molecular characterization of the ligand-receptor interaction of the neuropeptide Y family. J. Pept. Sci. 2000, 6 (3), 97-122.
54. Gill, S. C.; von Hippel, P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182 (2), 319-326.
55. Greenfield, N.; Fasman, G. D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8, 4108-4116.
56. Lauterwein, J.; Bosch, C.; Brown, L. R.; Wuthrich, K.; Physiochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim. Biophys. Acta 1979, 556, 244-264.
57. MSI Molecular Symulations, 965 Scranton Road, San Diego, CA 92121-3752.