Study of bradykinin conformation in the presence of model membrane by Nuclear Magnetic Resonance and molecular modelling

Biochimica et Biophysica Acta - Biomembranes

Volumn 1788, Issue 3, 2009, Pages 708-716

  Bonechi, Claudia ^a   Ristori, Sandra ^b   Martini, Giacomo ^b   Martini, Silvia ^a   Rossi, Claudio ^a  

^a UNIVERSITY OF SIENA   (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Bradykinin; DOPC DOPE; Monolamellar liposome; NMR

Indexed keywords

BRADYKININ; G PROTEIN COUPLED RECEPTOR; LIPOSOME;

ARTICLE; ARTIFICIAL MEMBRANE; CONFORMATIONAL TRANSITION; LIPID BILAYER; MEMBRANE MODEL; MOLECULAR MODEL; MONTE CARLO METHOD; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

BRADYKININ; COMPUTER SIMULATION; LIPOSOMES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLETHANOLAMINES; PROTEIN CONFORMATION;

EID: 60549096725     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.12.019     Document Type: Article

References (55)

1. Farmer S.G., and Burch R.M. In: Burch R.M. (Ed). In Bradykinin Antagonists, Basic and Clinical Research (1991), Marcel Dekker, New York 1-31
2. Moreau M.E., Garbacki N., Molinaro G., Brown N.J., Marceau F., and Adam A. The kallikrein-kinin system: current and future pharmacological targets. J. Pharmacol. Sci. 99 1 (2005) 6-38
3. Carbonell L.F., Carretero O.A., Stewart J.M., and Scicli A.G. Effect of a kinin antagonist on the acute antihypertensive activity of enalaprilat in severe hypertension. Hypertension 11 (1988) 239-243
4. Ragoli D., and Barabe J. Pharmacology of bradykinin and related kinins. Pharmacol. Rev. 32 (1980) 1-46
5. Dray A., and Perkins M. Bradykinin and inflammatory pain. Trends Neurosci. 16 (1993) 99-104
6. Kyle D.J., and Burch R.M. A survey of bradykinin receptors and their antagonists. Curr. Opin. Invest. Drugs 2 1 (1993) 5-20
7. Miskolzie M., Gera L., Stewart J.M., and Kotovych G. Correlation of secondary structures of bradykinin B1 receptor antagonists with their activity. J. Biomol. Struct. Dyn. 19 (2002) 585-593
8. Desai P., Coutinho E., and Srivastava S. Conformational diversity of T-kinin in DMSO, water and HFA. Eur. J. Med. Chem. 37 (2002) 135-146
9. Jensen J., Soto A.M., and Colon J.M. Structure-activity relationships of trout bradykinin ([Arg0,Trp5,Leu8]-bradykinin). Peptides 21 (2000) 1793-1798
10. Cai X., and Dass C. Conformational analysis of proteins and peptides. Current Organic Chemistry 7 18 (2003) 1841-1854 (14)
11. Kyle D.J., A Martin J., Farmer S.G., and Burch R.M. Design and conformational analysis of several highly potent bradykinin receptor antagonists. J. Med. Chem. 34 (1991) 1230-1233
12. Sawutz D.G., Salvino J.M., Seoane P.R., Douty B.D., Houck W.T., Bobko M.A., Doleman M.S., Dolle R.E., and Wolfe H.R. Synthesis, characterization, and conformational analysis of the D/L-Tic7 stereoisomers of bradykinin receptor antagonist DArg0[Hyp3,Thi5,D-Tic7,Oic8]bradykinin. Biochemistry 33 9 (1994) 2373-2379
13. Ottleben H., Haasemann M., Ramachandran R., Görlach M., Müller-Esterl W., and Brown L.R. An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of the bradykinin B2 receptor. Eur. J. Biochem. 244 (1997) 471-478
14. Kotovych G., Cann J.R., Stewart J.M., and Yamamoto H. NMR and CD conformational studies of bradykinin and its agonists and antagonists: application to receptor binding. Biochem. Cell Biol. 76 2-3 (1998) 257-266
15. Denys L., Bothner-By A.A., and Fisher G. Conformational diversity of bradykinin in aqueous solution. Biochemistry 21 (1982) 6531-6536
16. Chatterjee C., and Mukhopadhyay C. Conformational alteration of bradykinin in presence of GM1 micelle. Biochem. and Biophys Res. Communications 315 4 (2004) 866-871
17. Prosser R.S., Evanics F., Litevski J.L., and Sameer Al-Abdul-Wahid M. Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins. Biochemistry 45 28 (2006) 8453-8465
18. Cann J.R., Vatter A., Vavrek R.J., and Stewart J.M. Interaction of bradykinin with sodium dodecyl sulfate and certain acidic lipids. Peptides 7 (1986) 1121-1130
19. Pellegrini M., Mammi S., Peggion E., and Mierke D.F. Threonine6-bradykinin: structural characterization in the presence of micelles by nuclear magnetic resonance and distance geometry. J. Med. Chem. 40 (1997) 92-98
20. Hakomari S.I. Structure & function of sphingoglycolipids in transmembrane signaling and cell-cell interaction. Biochem. Soc. Trans. 21 (1993) 583-585
21. Strosberg A.D., and Nahmias C. G-protein-coupled receptor signalling through protein networks. Biochem. Soc. Trans. 35 (2007) 23-27
22. Moroder L., Romano R., Guba W., Mierke D.F., Kessler H., Delporte C., Winand J., and Christophe J. New evidence for a membrane bound pathway in hormone receptor binding. Biochemistry 32 (1993) 13551-13559
23. Schwyzer R. Peptide-membrane interactions and a new principle in quantitative structure-activity relationships. Biopolymers 31 (1991) 785-792
24. Ulrich A.S. Biophysical aspects of using liposomes as delivery vehicles. Biosci. Rep. 22 2 (2002) 129-150
25. Lohner K., Sevcsik E., and Pabst G. Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions. Advances in Planar Lipid Bilayers and Liposome 6 (2008) 103-137
26. Tamm L.K., and Binyong L. NMR of membrane proteins in solution. Prog. Nucl. Magn. Reson. Spectrosc. 48 4 (2006) 201-210
27. Borgias B.A., and James T.L. Two-dimensional nuclear Overhauser effect: complete relaxation matrix analysis. Methods Enzymol. 176 (1989) 169-183
28. Wang C., Yao J., Yu Y., Shao X., Cui Y., Liu H., Lai L., and Wang R. Structure-activity study of endomorphin-2 analogs with C-terminal modifications by NMR spectroscopy and molecular modelling. Bioorg. & Med. Chemistry 16 12 (2008) 6415-6422
29. Scott W.R.P., Baek S.B., Jung D., Hancock R.E.W., and Straus S.K. NMR structural studies of the antibiotic lipopeptide daptomycin in DHPC micelles. Biochim. Biophys. Acta 1768 (2008) 3116-3126
30. Wakamatsu K., Takeda A., Tachi T., and Matsuzaki K. Dimer structure of magainin 2 bound to phospholipid vesicles. Biopolymers 64 (2002) 314-327
31. Halskau Ø., Frøystein N.Å., Muga A., and Martínez A. The membrane bound conformation of a-lactalbumin studied by NMR-monitored 1H exchange. J. Mol. Biol. 321 (2002) 99-110
32. Garcia-Fuentes M., Torres D., Martin-Pastor M., and Alonso M.J. Application of NMR spectroscopy to the characterization of PEG-stabilized lipid nanoparticles. Langmuir 20 (2004) 8839-8845
33. Turchiello R.F., Juliano L., Ito A.S., and Lamy-Freund M.T. How bradykinin alters the lipid membrane structure: a spin label comparative study with bradykinin fragments and other cations. Biopolymers 54 (2000) 211-221
34. Turchiello R.F., Lamy-Freund M.T., Hirata I.Y., Juliano L., and Ito A.S. Orthoaminobenzoic acid labeled bradykinins in interaction with lipid vesicles: fluorescence study. Biopolymers 65 (2002) 336-346
35. In: Yeagle P. (Ed). The Structure of Biological Membranes (2005), CRC Press, Boca Raton, Florida
36. Delaglio F., Grzesiek S., Vuister G., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
37. Still C. Macromodel, Columbia University Molecular Modelling System (1987)
38. Mohamadi F., Richards N.G.J., Guida W.C., Liskamp R., Lipton M., Caufield C., Chan G., Hendrickson T., and Still W.C. Macromodel-an integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J. Comput. Chem. 11 (1990) 440-467
39. Case A., Cheatham III T.E., Darden T., Gohlke H., Luo R., Merz Jr. K.M., Onufriev A., Simmerling C., Wang B., and Woods R. The Amber biomolecular simulation programs. J. Computat. Chem. 26 (2005) 1668-1688
40. Chang G., Guida W.C., and Still W.C. An internal-coordinate Monte Carlo method for searching conformational space. J. Am. Chem. Soc. 11 (1989) 4379-4386
41. Shenkin P.S., and Mcdonald D.Q. Cluster analysis of molecular conformations. J. Comput. Chem. 15 (1994) 899-916
42. Mirmira S.R., Durani S., Srivastava S., and Phadke R.S. Occurrence of β-bends in bradykinin dissolved in DMSO-d6. Magn. Res. Chem. 28 7 (1990) 587-593
43. London R.E., Stewart J.M., Cann J.R., and Matwiyoff N.A. 13C and proton nuclear magnetic resonance studies of bradykinin and selected peptide fragments. Biochemistry 17 (1978) 2270-2283
44. Chapman D., and Chen S. Thermal and NMR spectroscopic studies of lipids and membranes. Chem. Phys. Lipids 8 (1972) 318-326
45. Neumann J.M., Zachowski A., Tran-Dinh S., and Devaux P.F. High resolution proton magnetic resonance of sonicated phospholipids. Eur. Biophys. J. 11 (1985) 219-233
46. Levitt M.H. Spin Dynamics: Basics of Nuclear Magnetic Resonance (2001), John Wiley & Sons
47. Wüthrich K. NMR of proteins and Nucleic Acids (1986), John Wiley & Sons, New York
48. Maddox M.W., and Longo M.L. A Monte Carlo study of peptide insertion into lipid bilayers: equilibrium conformations and insertion mechanisms. Biophys. J. 82 (2002) 244-263
49. Still C. XCluster 1.2 (1995), Columbia University, New York
50. Lins L., Charloteaux B., Thomas A., and Brasseur R. Computational study of lipiddestabilizing protein fragments: towards a comprehensive view of tilted peptides. Proteins 44 (2001) 435-447
51. Metropolis N., Rosenbluth A.W., Rosenbluth M.N., Teller A.H., and Teller E.J. Equation of state calculations by fast computing machines. J. Chem. Phys. 21 (1953) 1087-1092
52. Bissantz C. Conformational changes of G-protein coupled receptors during their activation by agonist binding. J. Receptors and Signal Transduction 23 2 & 3 (2003) 123-153
53. Nakamura G.R., Reynolds M.E., Chen Y.M., and Starovasnik M.A. Stable "zeta" peptides that act as potent antagonists of the high-affinity IgE receptor. PNAS 99 3 (2002) 1303-1308
54. He X., Chow D., Martick M.M., and Garcia K.C. Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science 293 5535 (2001) 1657-1662
55. Marcotte I., Separovic F., Auger M., and Gagné S. A multidimensional 1H-NMR investigation of the conformation of Methionine-Enkephalin in fast-tumbling bicelles. Biophys. J. 86 (2004) 1587-1600