Investigation on interaction of prulifloxacin with pepsin: A spectroscopic analysis

Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy

Volumn 75, Issue 3, 2010, Pages 1024-1029

  Huang, Yabei ^a,b   Yan, Jie ^b   Liu, Benzhi ^a   Yu, Zhang ^a   Gao, Xiaoyan ^a   Tang, Yingcai ^a   Zi, Yanqin ^a  

^a HUAIBEI NORMAL UNIVERSITY   (China)

^b Huaibei Occupational Disease Prevention and Cure Hospital   (China)

Author keywords

Fluorescence quenching; Pepsin; Prulifloxacin; Stern Volmer equation; The F rster's resonance energy transfer theory

Indexed keywords

BINDING DISTANCE; BINDING PARAMETER; BINDING PROCESS; BIOLOGICAL SIGNIFICANCE; CLINICAL MEDICINE; FLUORESCENCE QUENCHING; FLUORESCENCE QUENCHING METHOD; IN-VITRO; INTRINSIC FLUORESCENCE; NEGATIVE VALUES; PHYSIOLOGICAL CONDITION; PRULIFLOXACIN; RESONANCE ENERGY TRANSFER; SPECTROSCOPIC METHOD; SPONTANEOUS PROCESS; STATIC QUENCHING; STERN-VOLMER EQUATION;

BIOLOGICAL MATERIALS; ENERGY TRANSFER; FLUORESCENCE; QUENCHING; RESONANCE; SPECTROSCOPIC ANALYSIS;

BINDING ENERGY;

1,3 DIOXOLANE DERIVATIVE; ANTIINFECTIVE AGENT; PEPSIN A; PIPERAZINE DERIVATIVE; PRULIFLOXACIN; QUINOLONE DERIVATIVE;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENERGY TRANSFER; HUMAN; METABOLISM; METHODOLOGY; PHYSIOLOGY; PROTEIN BINDING; SPECTROFLUOROMETRY; THERMODYNAMICS;

ANIMALS; ANTI-BACTERIAL AGENTS; BINDING SITES; DIOXOLANES; ENERGY TRANSFER; FLUOROQUINOLONES; HUMANS; MOLECULAR STRUCTURE; PEPSIN A; PIPERAZINES; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 76349097564     PISSN: 13861425     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.saa.2009.12.044     Document Type: Article

References (36)

1. Aszmann O.C. The life and work of Theodore Schwann. J. Reconstr. Microsurg. 16 (2000) 291-296
2. Zhu D.N., Wu B.W., and Fan X.L. Physiology. 7th ed. (2008), People's Medical Publishing House Press, Beijing pp. 180-181
3. Kitahara F., Kobayashi K., Sato T., Kojima Y., Araki T., and Fujino M.A. Accuracy of screening for gastric cancer using serum pepsinogen concentrations. Gut 44 (1999) 693-697
4. Oishi Y., Kiyohara Y., Kubo M., Tanaka K., Tanizaki Y., Ninomiya T., Doi Y., Shikata K., Yonemoto K., Shirota T., Matsumoto T., and Iida M. The serum pepsinogen test as a predictor of gastric cancer: the Hisayama study. Am. J. Epidemiol. 163 (2006) 629-637
5. Ricci C., Vakil N., Rugge M., Gatta L., Perna F., Osborn J.F., Russo V.M., Tampieri A., Bernabucci V., Miglioli M., and Vaira D. Serological markers for gastric atrophy in asymptomatic patients infected with Helicobacter pylori. Am. J. Gastroenterol. 99 (2004) 1910-1915
6. Antonov V.K., Ginodman L.M., Kapitannikov Y.V., Barshevskaya T.N., Gurova A.G., and Rumsh L.D. Mechanism of pepsin catalysis: general base catalysis by the active-site carboxylate ion. FEBS Lett. 88 (1978) 87-90
7. Campos L.A., and Sancho J. The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH. FEBS Lett. 538 (2003) 89-95
8. Fass R.J. In vitro activity of ciprofloxacin (Bay o 9867). Antimicrob. Agents. Chemother. 24 (1983) 568-574
9. Wolfson J.S., and Hooper D.C. Fluoroquinolone antimicrobial agents. Clin. Microbiol. Rev. 2 (1989) 378-424
10. Gould I.M., and Milne K. In-vitro pharmacodynamic studies of piperacillin/tazobactam with gentamicin and ciprofloxacin. J. Antimicrob. Chemother. 39 (1997) 53-61
11. Woodcock J.M., Andrews J.M., Boswell F.J., Brenwald N.P., and Wise R. In vitro activity of BAY 12-8039, a new fluoroquinolone. Antimicrob Agents Chemother. 41 (1997) 101-106
12. Imada T., Miyazaki S., Nishida M., Yamaguchi K., and Goto S. In vitro and in vivo antibacterial activities of a new quinolone, OPC-17116. Antimicrob. Agents Chemother. 36 (1992) 573-579
13. Matera M.G. Pharmacologic characteristics of prulifloxacin. Pulmon. Pharmacol. Ther. 19 (2006) 20-29
14. Yoshida Y., and Mitsuhashi S. Antibacterial activity of NM394, the active form of prodrug NM441, a new quinolone. Antimicrob. Agents Chemother. 37 (1993) 793-800
15. Keam J.K., and Perry C.M. Prulifloxacin. Drugs 64 (2004) 2221-2234
16. Wen J., Zhu Z.Y., Hong Z.Y., Wu Y.W., Fei Y., Lin M., Fan G.R., and Wu Y.T. Determination of the active metabolite of prulifloxacin in human plasma by HPLC with fluorescence detection. Chromatographia 66 (2007) 37-41
17. Quayle O.R. The parachors of organic compounds. An interpretation and catalogue. Chem. Rev. 53 (1953) 439-589
18. Lakowicz J.R. Principles of Fluorescence Spectroscopy (1983), Plenum Press, New York Chapter 10, pp. 303-339
19. Eftink M.R., and Ghiron C.A. Fluorescence quenching of indole and model michelle systems. J. Phys. Chem. 80 (1976) 486-493
20. Zhao H.W., Ge M., Zhang Z.X., Wang W.F., and Wu G.Z. Spectroscopic studies on the interaction between riboflavin and albumins. Spectrochim. Acta Part A 65 (2006) 811-817
21. Tang J.H., Qi S.D., and Chen X.G. Spectroscopic studies of the interaction of anti-coagulant rodenticide diphacinone with human serum albumin. J. Mol. Struct. 779 (2005) 87-95
22. Lakowicz J.R., and Weber G. Quenching of fluorescence by oxygen, probe for structural fluctuations in macromolecules. Biochemistry 12 (1973) 4161-4170
23. Ware W.R. Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem. 66 (1962) 455-458
24. Papadopoulou A., Green R.J., and Frazier R.J. Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J. Agric. Food Chem. 53 (2005) 158-163
25. Tian J.N., Liu J.Q., He W.Y., Hu Z.D., Yao X.J., and Cheng X.G. Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules 5 (2004) 1956-1961
26. Feng X.Z., Lin Z., Yang L.J., Wang C., and Bai C.L. Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 47 (1998) 1223-1229
27. Jiang M., Xie M.X., Liu Y., Li X.Y., and Chen X. Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin. J. Mol. Struct. 692 (2004) 71-80
28. Kandagal P.B., Ashoka S., Seetharamappa J., Shaikh S.M.T., Jadegoud Y., and Ijare O.B. Study of the interaction of an anticancer drug with human and bovine serum albumin: spectroscopic approach. J. Pharm. Biomed. Anal. 41 (2006) 393-399
29. Wei Y.L., Li J.Q., Dong C., Shuang S., Liu D.S., and Huie C.W. Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy. Talanta 70 (2006) 377-382
30. Ross P.D., and Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981) 3096-3102
31. Chen G.Z., Huang X.Z., Xu J.G., Zheng Z.X., and Wang Z.B. The Methods of Fluorescence Analysis. 2nd ed. (1990), Science in China Press, Beijing (in Chinese) p. 503
32. Förster T. In: Sinaoglu O. (Ed). Modern Quantum Chemistry vol. 3 (1965), Academic Press, New York
33. Cristobal G., Dos R., and Pierre D.J.M. Fluorescence resonance energy transfer spectroscopy is a reliable "Ruler" for measuring structural changes in proteins: dispelling the problem of the unknown orientation factor. J. Struct. Biol. 115 (1995) 175-185
34. Saha D.C., Ray K., and Misra T.N. Energy transfer in triton-X 100 micelles: a fluorescence study. Spectrochim. Acta Part A 56 (2000) 797-801
35. Bertucci C., and Domenici E. Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance. Curr. Med. Chem. 9 (2002) 1463-1481
36. Valeur B., and Brochon J.C. New Trends in Fluorescence Spectroscopy. 6th ed. (1999), Springer Press, Berlin