The Investigation of the Interaction between Lomefloxacin and Human Serume Albumin by Specteroscopic Methods

Subject Areas : Journal of Chemical Health Risks

F. S. Goldouzian ¹ , Z. S. Goldouzian ² , M. Momen Heravi ³ , J. Khanchamani ⁴

1 - Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran
2 - Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran
3 - Department of Chemistry, Mashhad Branch, Islamic Azad University, Mashhad, Iran
4 - Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran

Received: 2012-03-10 Accepted : 2018-10-29 Published : 2012-03-10

Keywords: Human serum albumin, Lomefloxacin, Fluorescence spectroscopy, Fluorophore, Fluoroquinolone,

Abstract :

Mechanism of the binding of lomefloxacin (LMF) with human serum albumin has been studied at physiological pH (7.4) using fluorescence spectroscopic technique. LMF is a third-generation fluoroquinolone antibiotic that exhibits striking potency against a broad spectrum of Gram-negative and Gram-positive bacteria through inhibition of DNA gyrase. Lomefloxacin is a drug that is excreted in urine and has very variable systemic absorption. Human serum albumin (HSA) is the most important and abundant constituent of blood plasma and serves as a protein storage component. Recently, the three-dimensional structure of HSA was determined through X-ray crystallographic measurement. Fluorescence studies showed that (LMF) has an ability to quench the intrinsic fluorescence of HSA through a static quenching  procedure  according to the Stern–Volmer equation .LMF showed two types of binding sites, the first having a very high affinity (1/72 ×107M-1) and a secondary binding site with an affinity two orders lower than the primary site. The number of binding sites for complex: HSA-LMF at 280 nm was calculated 1and0.5. The microenvironment of tryptophan and tyrosin residues and more hydrophobic of fluorophores microenvironment were changed and disturbed by the blue shift in maximum wavelength and decreased in fluorescence intensity in the presence of lomefloxacin revealed  decreased polarity of the fluorophores. The binding site for LMF is in a hydrophobic pocket in the sub-domain II A of HSA.

References:

1. American Society of Microbiology, Washington,
2. DC, USA, 1993:1-11.
3. Dufour C. and O. Dangles, 2005. Flavonoid-serum
4. albumin complexation: determination of
5. binding complexation: determination of binding
6. constants and binding sites by fluorescence
7. spectroscopy," Biochim. Biophys. Acta 1721,
8. -173.
9. Quan J., F. Jin, T. Sun and X. Zhou, 2007. "Multispectroscopic
10. study on interaction of bovine
11. serum albumin with lomefloxacin ââ‚‌“ copper (II)
12. Complex" International Journal of Biological
13. Macromolecules, 40, 299-304.
14. Tang J., N. Lian, X. He and G. Zhang, 2008.
15. "Investigation of the interaction between
16. sophoricoside and human serum albumin by
17. optical spectroscopy and molecular modeling
18. methods, "J. Mol. Struct. 889 , 408-41.
19. Xie M. X., M. Long and Y. liu, 2006.
20. Characterization of the interaction between
21. human serum albumin and morinââ‚‌œ Biochim.
22. Biophys. Acta.1760, 1184-1191
23. Yue Y., Y. Zhang, J. Qin and X. Chen, 2008.
24. "Study of the interaction between esculetin and
25. human serum albumin by multi-spectroscopic
26. method and molecular modeling," J. Mol.
27. Struct. 888, 25-32.
28. Zhang G., Q. Que, J. Pan and J. Guo, 2008. "Study
29. of the interaction between icariin and human
30. serum albumin by fluorescence spectroscopy,"
31. J. Mol. Struct., 881, 132-138