IN-VITRO STUDIES OF THE EFFECT OF ARSENIC ON THE BINDING OF METRONIDAZOLE AT THE BINDING SITES OF BOVINE SERUM ALBUMIN

S.J.  Uddin; R.  Rouf; P.K.  Sen; M.A.  Alam; M.M.  Sarder; J.A.  Shilpi; S.K.  Sadhu

doi:10.53808/KUS.2005.6.1and2.0408-L

Authors

S.J. Uddin Pharmacy Discipline, Khulna University, Khulna, Bangladesh
R. Rouf Pharmacy Discipline, Life Science School, Khulna University, Khulna 9208, Bangladesh
P.K. Sen Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh
M.A. Alam Pharmacy Discipline, Life Science School, Khulna University, Khulna 9208, Bangladesh
M.M. Sarder Pharmacy Discipline, Life Science School, Khulna University, Khulna 9208, Bangladesh
J.A. Shilpi Pharmacy Discipline, Life Science School, Khulna University, Khulna 9208, Bangladesh
S.K. Sadhu Pharmacy Discipline, Life Science School, Khulna University, Khulna 9208, Bangladesh

DOI:

https://doi.org/10.53808/KUS.2005.6.1and2.0408-L

Keywords:

Equilibrium dialysis, metronidazole, arsenic, arsenic-metronidazole interaction

Abstract

The effect of arsenic on the binding of metronidazole (an anti-amoebic agent) to bovine serum albumin (BSA) was studied by equilibrium dialysis (ED) method in order to justify the nature of binding capability of the drug and arsenic to BSA. There was decrease in metronidazole concentration due to addition of arsenic. But the free metronidazole concentration was increased with increasing the metronidazole concentration when only the BSA was present. The result obtained when no arsenic was added the free concentration of metronidazole was 41% whereas this release was only 7% when arsenic was added with an increasing concentration from 0.5x10^-5 to 10x10^-5M. But the free concentration of metronidazole was 36% to 71% when only metronidazole was added to BSA from 0.5x10^-5 M to12x10^-5M. This result suggests that in presence of arsenic, metronidazole shows a greater binding to BSA and results in a decreased serum drug concentration. It could be suggested that in the presence of arsenic, metronidazole may form complex with arsenic, arsenic may increases the binding affinity to its sites or may form complex to BSA and metronidazole.

Downloads

Download data is not yet available.

References

Brown, J.R. 1977a. Serum albumin, Amino acid sequence. In: Albumin Structure Function and Uses. Pergamon Press, Oxford, pp. 27-51.

Brown, J.R. 1976. Structural origins of mammalian albumin. Feb. Proc., 35: 591.

Feshke, K.J.; Schlafer, U.; Wollert, U. and Muller, W.E. 1979. A highly reactive tyrosine residue as part of the indole and benzodiazepine binding site of human serum albumin. Biochem. Biophys. Acta., 577:346-359.

Hansen, K.U. 1981. Effect of aliphatic fatty acid on the binding of phenol red to human serum alnbumin. Journal of Biochemistry, 195: 603-613.

Jiunn, H.L.; David, M.; Cochetto, E.; Daniel, E. and Duggam, F. 1987. Protein binding: as a primary determinant of the clinical pharmacokinetic properties of non-steroidal anti-inflmmatory drugs. Clinical Pharmacokinetic, 12: 402-432.

Koch-Wester, J. Sellers, E.M. 1976. Binding of drugs to serum albumin. N. Engl. J. Med., 294: 311.

Kragh-Hansen, U. 1981. Molecular aspects of ligand binding to serum albumin. Pharmacology Review, 34: 7-51.

Meloun, B.; Moravec, L. and Kostka, V. 1975. Complete amino acid sequence of human serum albumin. FEBS Letters, 58: 134-137.

Nahar, Z.; Rhaman, M.H. and Hasnat, A. 1997. Interaction of nifedipine with BSA: effect of metals. Bangladesh Journal of Physiology and Pharmacology, 13(1): 18-20.

Rahman, M.H. 1993. Characterization of high affinity binding sites of non-steroidal anti-inflamatory with respect to site specific probes on human serum albumin. Ph.D. Thesis, Kumamoto University, Japan, pp. 2-8.

Signals, E. 1987b. Determination of protein binding and its characteristics. In: Protein Binding of Drug, 2nd edn. Chapter 1, pp. 25–31.

Signals, E. 1987a. Protein Binding of Drug, 2nd edn. Chapter 1, pp. 20-22.