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Name | In Vitro Interaction of Verapamil Hydrochloride with Zinc Sulphate (Anhydrous) and Its Influence on Protein Binding of Verapamil Hydrochloride |
Description | Research article:- Ummeh Khair Kulsum1, Niaz Uddin Mahmud2, Tapas Kanti Dey3, Talha Bin Emran3, and JoysreeDas3*.
1Department of Pharmacy, University of Science and Technology Chittagong, Bangladesh 2Department of Computer Science and Engineering, 3Department of Pharmacy, BGC Trust University Bangladesh.
Abstract: - Aim: This study was aimed to evaluate the influences of interaction of Verapamil Hydrochloride with Zinc Sulphate on protein binding of drug in physiological pH and temperature. Materials and methods: The interaction between Verapamil Hydrochloride and Zinc Sulphate (anhydrous) has been studied in an aqueous system at a fixed temperature (37±0.5)0C and under pH 7.4 and 2.4 by a variety of physical method, to detect and confirm the nature of complexation of this drug with Zinc sulfate (anhydrous). The methods include- inspection of spectral behavior, Job’s method of continuous variation and Ardon’s straight line plots by spectrophotometer. The protein binding experiments of the free drugs as well as the combined systems were studied by equilibrium dialysis method. Results: From spectrophotometric study, it has been found that Verapamil Hydrochloride form 1:1 complex with Zinc Sulphate (anhydrous). Spectral studies helps to detect the initial complexation between drug and metal. Job’s plot at 7.4 and 2.4 provides same type of information. The Ardon’s spectrophotometric method confirmed the 1:1 complexation and the value of stability constants was calculated using Ardon’s plot. The Scatchard plots were prepared to reveal the number of binding sites and the affinity for protein binding. It has been found that interaction of the drug with Zinc Sulphate (anhydrous) results into increasing the affinity and increasing the protein binding of Verapamil Hydrochloride. Conclusion: The results show that Zinc sulphate (anhydrous) increases the percentage of protein binding of Verapamil hydrochloride at saturation zone. Key words:- Ardon’s method, Equilibrium dialysis, Protein binding, Scatchard plot, Verapamil Hydrochloride, Zinc Sulphate (anhydrous). References:- 1.Bertram G. Katzung. Basic amnd Clinical Pharmacology. 7th Edition. Appleton & Lange. (1997) 165. 2.Kragh-Hanse U. Molecular aspects of ligand binding to serum albumin. Pharmacia Review 1981; 33: 17-53. 3.Jusko WJ. In the effects of disease states on Drug Pharmacokinetics. (L.Z. Benet, ed.), 1976; P. 99, American Pharmaceutical Association. 4.Wilkinson GR. Molecular aspects of ligand binding. Drug Metal Rev 1983; 14: 427. 5.Peters T. Advances in protein chemistry. Jr. Serum Albumin 1985; 37: 161-245. 6.He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature 1992; 358: 209-15. 7.Kragh-Hansen U. Structure and ligand binding properties of human serum albumin. Dansish Medical bulletin 1990; 37: 57-79. 8.Donald E. Cadwallader. Biopharmaceutics and Drug Interactions. 3 Sub Edition. Raven Pr. (1983) 107-143. 9.Vogel AI. Textbook of Quantitative Inorganic Analysis. 4th Edition. Longman (1978). 10.Ardon M.. Oxidation of ethanol by ceric perchlorate. Oxidation of ethanol by ceric perchlorate (1957). 11.Singlass E. Protein binding of drugs, 2nd edition. F. Hoffman La Roche & Co. Ltd., Basle, Switzerland. (1987) 17-32. 12.Geisow MJ, Beaven GH. Large fragments of human serum albumin. Biochem J 1977; 161: 619-25. 13.Goldstein A, Aronow L, Kalman SM. Principle of drug action-the basis of pharmacology, 2nd edition, John wily and sons, New York. (1974) 47-52. 14.Scatchard G. The attractions of proteins for small molecules and ions. Ann NY Acad Sci 1949; 660-73. 15.Hossain MA, Momen AZMR. Protein binding of theophylline in presence of cobalt. J Bangladesh Chem Soc 1994; 7 (1): 93-103. 16.Hansten PD, Horn JR. Drug interactions clinical significance of drug-drug interactions, 6th edition, Philadelphia. (1989) 22-23.
Copyright © 2013 Das Joysree et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
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