Ciprofloxacin interactions with bacterial protein OmpF: Modelling of FRET from a multi-tryptophan protein trimer

Biochimica et Biophysica Acta - Biomembranes

Volumn 1768, Issue 11, 2007, Pages 2822-2830

  Fernandes, Fábio ^a   Neves, Patrícia ^b   Gameiro, Paula ^b   Loura, Luís M S ^c   Prieto, Manuel ^a  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^b Faculdade de Farmácia da Universidade do Porto   (Portugal)

^c UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

Fluorescence; Fluoroquinolones; Membrane model system; Membrane protein; Porin

Indexed keywords

CIPROFLOXACIN; OUTER MEMBRANE PROTEIN F; TRYPTOPHAN;

ARTICLE; BINDING SITE; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER; LIPID MEMBRANE; MATHEMATICAL MODEL; MEMBRANE MODEL; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANTI-INFECTIVE AGENTS; CIPROFLOXACIN; DIMYRISTOYLPHOSPHATIDYLCHOLINE; FLUORESCENCE RESONANCE ENERGY TRANSFER; LIPOSOMES; MODELS, THEORETICAL; PORINS; TRYPTOPHAN;

BACTERIA (MICROORGANISMS);

EID: 35848961035     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.07.016     Document Type: Article

References (27)

1. Chapman J.S., and Georgopapadakou N.H. Routes of quinolone permeation in Escherichia coli. Antimicrob. Agents Chemother. 32 (1988) 438-442
2. Pestova E., Millichap J.J., Noskin G.A., and Peterson L.R. Intracellular targets of moxifloxacin: a comparison with other fluoroquinolones. J. Antimicrob. Chemother. 45 (2000) 583-590
3. Mascaretti O.A. Bacteria versus Antibacterial Agents: An integrated approach (2003), ASM Press, Washington D.C.
4. Chevalier J., Malléa M., and Pagès J.-M. Comparative aspects of the diffusion of norfloxacin, cefepime and spermine through the F porin channel of Enterobacter cloacae. Biochem. J. 348 (2000) 223-227
5. Piddock L.J.V., Jin Y.-F., Ricci V., and Asuquo A.E. Quinolone accumulation by Pseudomonas aeruginosa, Staphylococcus aureus and Escherichia coli. J. Antimicrob. Chemother. 43 (1999) 61-70
6. Hirai K., Aoyama H., Irikura T., Iyobe S., and Mitsuhashi S. Differences in susceptibility to quinolones of outer membrane mutants of Salmonella typhimurium and Escherichia coli. Antimicrob. Agents Chemother. 29 (1986) 535-538
7. O'Keeffe A.H., East J.M., and Lee A.G. Selectivity in lipid binding to the bacterial outer membrane protein OmpF. Biophys. J. 79 (2000) 2066-2074
8. Gravito R.M., and Rosenbusch J.P. Isolation and crystallization of bacterial porin. Methods Enzymol. 125 (1986) 309-328
9. Rigaud J.-L., Pitard B., and Levy D. Reconstitution of membrane proteins into liposomes: application to energy transducing membrane proteins. Biochim. Biophys. Acta 123 (1995) 223-246
10. Rigaud J.-L., Paternostre M.T., and Bluzat A. Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin. Biochemistry 27 (1988) 2677-2688
11. Richard P., Rigaud J.-L., and Graber P. Reconstitution of CF0F1 into liposomes using a new reconstitution procedure. Eur. J. Biochem. 193 (1990) 921-930
12. 2+ATPase: mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. Biochim. Biophys. Acta 1107 (1992) 283-298
13. Paternostre M.T., Roux M., and Rigaud J.-L. Mechanisms of membrane protein insertion into liposomes during reconstruction procedures involving the use of detergents. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside and sodium cholate. Biochemistry 27 (1988) 2668-2677
14. Plançon L., Chami M., and Letellier L. Reconstitution of FhuA, an Escherichia coli outer membrane protein, into liposomes. J. Biol. Chem. 272 (1997) 16868-16872
15. Knol J., Sjollema K., and Poolman B. Detergent-mediated reconstitution of membrane proteins. Biochemistry 37 (1998) 16410-16415
16. Bangham A.D., Standish M.M., and Watkins J.C. Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 13 (1965) 238-252
17. Im W., and Roux B. Ions and counterions in a biological channel: a molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution. J. Mol. Biol. 319 (2002) 1177-1197
18. Nestorovich E.M., Danelon C., Winterhalter M., and Bezrukov S.M. Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9789-9794
19. Lakowicz J.R. Principles of fluorescence spectroscopy. Chapter 13. 3rd edition (2006), Springer Science, New York 443-475
20. Davenport L., Dale R.E., Bisby R.E., and Cundall R.B. Transverse location of the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene in model lipid bilayer membrane systems by resonance energy transfer. Biochemistry 24 (1985) 4097-4108
21. Martin D.W. Active unit of solubilized sarcoplasmic reticulum calcium adenosinetriphophatase: an active enzyme centrifugation analysis. Biochemistry 22 (1983) 2276-2282
22. Vazquez J.L., Montero M.T., Merino S., Domenech O., Berlanga M., Vinas M., and Hernandez-Borrel J. Location and nature of the surface membrane binding site of ciprofloxacin: a fluorescence study. Langmuir 17 (2001) 1009-1014
23. Nagle J.F., and Tristam-Nagle S. Structure of lipid bilayers. Biochim. Biophys. Acta 1469 (2000) 159-195
24. Cowan S.W., Garavito R.M., Jansonius J.N., Jenkins J.A., Karlsson R., Konig N., Pai E.F., Pauptit R.A., Rizkallah P.J., Rosenbusch J.P., Rummel G., and Schimer T. The structure of OmpF porin in a tetragonal crystal form. Structure 10 (1995) 1041-1050
25. Neves P., Berkane E., Gameiro P., Winterhalter M., and de Castro B. Interaction between quinolones antibiotics and bacterial outer membrane porin OmpF. Biophys. Chemist. 113 (2005) 123-128
26. Wolber P.K., and Hudson B.S. An analytical solution to the Förster energy transfer problem in two dimensions. Biophys. J. 28 (1979) 197-210
27. Capeta R.C., Poveda J.A., and Loura L.M.S. Non-uniform membrane probe distribution in resonance energy transfer. Application to protein-lipid selectivity. J. Fluoresc. 16 (2005) 161-172