Abstract
Second derivative spectrophotometry was applied to determine the binding constant (K) between codeine phosphate (COD) and bovine serum albumin (BSA) at simulated physiological conditions (37.00 °C and pH = 7.4). The second derivative spectra of COD in buffer solutions containing various amounts of BSA showed derivative isosbestic points. The residual background signals derived from incomplete suppression of BSA signals can be entirely eliminated in the second derivative spectra indicating that BSA has spectrophotometrically one kind of binding site for COD. The fractions of COD bound to BSA were calculated from the derivative intensity differences (ΔD values) of COD before and after the addition of BSA. Scatchard plot calculation suggested that the binding of COD to BSA can be explained by a partition-like non-specific binding model. The binding constant (K) was calculated from ΔD values according to the non-specific binding model by a nonlinear least-squares method. K values were almost constant for all of the COD concentrations studied with good reproducibility. The fractions predicted by the K values were in good agreement with the observed values. The results indicate the usefulness of the derivative method in drug–albumin binding studies without the need for prior separation procedures which may disturb the equilibrium states of the samples solutions.
Similar content being viewed by others
References
Lowenstein, M.: Codeine. In: Advanced Treatment of Opiate Dependency. Anesthesia Assisted Medical Opiate Detoxification, Inc. (1997). Available via DIALAOG http://www.opiates.com/codeine/
Carter, D.C., Ho, J.X.: Structure of serum albumin. Adv. Protein Chem. 45, 153–198 (1994)
Abuin, E., Calderón, C., Lissi, E.: Interaction of alkylpyridinium chlorides with human serum albumin studied by fluorescence techniques. J. Photochem. Photobiol. A Chem. 195, 295–300 (2008)
Li, Y., He, W.Y., Liu, H.X., Yao, X.J., Hu, Z.D.: Daidzein interaction with human serum albumin studied using optical spectroscopy and molecular modeling methods. J. Mol. Struct. 831, 144–150 (2007)
Ulrich, K.H., Victor, T.G.C., Otagiri, M.: Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol. Pharm. Bull. 25, 695–704 (2002)
Sugio, S., Kashima, A., Mochizuki, S., Noda, M., Kobayashi, K.: Crystal structure of human serum albumin at 25 Å resolution. Protein Eng. 12, 439–446 (1999)
Curry, S., Mandelkow, H., Brick, P., Franks, N.: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827–835 (1998)
Ferrer, M.L., Duchowicz, R., Carrasco, B., García de la Torre, J., Acuña, A.U.: The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophys. J. 80, 2422–2430 (2001)
He, X.M., Carter, D.C.: Atomic structure and chemistry of human serum albumin. Nature 358, 209–215 (1992)
Kragh-Hansen, U.: Molecular aspects of ligand binding to serum albumin. Pharmacol. Rev. 33, 17–53 (1981)
Peters, T. Jr.: Ligand binding by albumin. In: Peters, T. Jr. (ed.) All About Albumin, pp. 76–132. Academic Press, New York (1996)
Borgå, O., Borgå, B.: Serum protein binding of nonsteroidal anti-inflammatory drugs: a comparative study. J. Pharm. Biopharm. 25, 63–77 (1997)
Rieutord, A., Bourget, P., Torche, G., Zazzo, J.F.: In vitro study of the protein binding of fusidic acid: a contribution to the comprehension of its pharmacokinetic behavior. Int. J. Pharm. 119, 57–64 (1995)
Ashoka, S., Seetharamappa, J., Kandagal, P.B., Shaikh, S.M.T.: Investigation of the interaction between trazodone hydrochloride and bovine serum albumin. J. Lumin. 121, 179–186 (2006)
Zia, H., Price, J.C.: Binding study of sulfonylureas and phenothiazines to bovine serum albumin using difference spectrophotometry. J. Pharm. Sci. 64, 1177–1181 (1975)
Zia, H., Price, J.C.: Binding study of tetracyclines to human serum albumin using difference spectrophotometry. J. Pharm. Sci. 65, 226–230 (1976)
Rojas, F.S., Ojeda, C.B., Pavon, J.M.C.: Derivative ultraviolet–visible region absorption spectrophotometry and its analytical applications. Talanta 35, 753–761 (1988)
Kitamura, K., Imayoshi, N., Goto, T., Shiro, H., Mano, T., Nakai, Y.: Second derivative spectrophotometric determination of partition coefficients of chlorpromazine and promazine between lecithin bilayer vesicles and water. Anal. Chim. Acta 304, 101–106 (1995)
Takegami, S., Kitamura, K., Takahashi, K., Kitade, T.: Partition of N-monodemethylated phenothiazine drugs to phosphatidylcholine bilayer vesicles studied by second-derivative spectrophotometry. Pharm. Sci. 91, 1568–1572 (2002)
Omran, A.A., Kitamura, K., Takegami, S., El-Sayed, A.Y., Abdel-Mottaleb, M.: Determination of partition coefficients of diazepam and flurazepam between phosphatidylcholine bilayer vesicles and water by second derivative spectrophotometric method. J. Pharm. Biomed. Anal. 25, 319–324 (2001)
Omran, A.A., Kitamura, K., Takegaami, S., El-Sayed, A.Y., Mohamed, M.H., Abdel-Mottaleb, M.: Effect of phosphatidylserine content on the partition coefficients of diazepam and flurazepam between phosphatidylcholine–phosphatidylserine bilayer of small unilamellar vesicles and water studied by second derivative spectrophotometry. Chem. Pharm. Bull. 50, 312–315 (2002)
Kitamura, K., Imayoshi, N.: Second-derivative spectrophotometric determination of the binding constant between chlorpromazine and β-cyclodextrin in aqueous solutions. Anal. Sci. 8, 497–501 (1992)
Kitamura, K., Goto, T., Kitade, T.: Second derivative spectrophotometric determination of partition coefficients of phenothiazine derivatives between human erythrocyte ghost membranes and water. Talanta 46, 1433–1438 (1998)
Kitamura, K., Mano, H., Shimamoto, Y., Tadokoro, Y., Tsuruta, K., Kitagawa, S.: Second-derivative spectrophotometric study on the interactions of chlorpromazine and triflupromazine with bovine serum albumin. Fresenius J. Anal. Chem. 358, 509–513 (1997)
Kitamura, K., Omran, A.A., Nagata, C., Kamijima, Y., Tanaka, R., Takegami, S., Kitade, T.: Effects of inorganic ions on the binding of triflupromazine and chlorpromazine to bovine serum albumin studied by spectrometric methods. Chem. Pharm. Bull. 54, 972–976 (2006)
Omran, A.A., El-Sayed, A.Y., Shehata, A.M.: Binding of benzodiazepine drugs to bovine serum albumin: a second derivative spectrophotometric study. Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 83, 362–367 (2011)
Connors, K.A.: Optical absorption spectroscopy. In: Connors, K.A. (ed.) Binding Constants, pp. 141–149. Wiley, New York (1987)
Klotz, I.M.: Protein interactions with small molecules. Acc. Chem. Res. 7, 162–168 (1974)
Scatchard, G.: The interaction of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51, 660–667 (1949)
Taira, Z., Terada, H.: Specific and non-specific ligand binding to serum albumin. Biochem. Pharmacol. 34, 1999–2005 (1985)
Varshney, A., Sen, P., Ahmad, E., Rehan, M., Subbarao, N., Khan, R.H.: Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 22, 77–87 (2010)
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Omran, A., El-Sayed, AA. & Shehata, A. Second Derivative Spectrophotometric Determination of the Binding Constant Between Codeine Phosphate and Bovine Serum Albumin. J Solution Chem 41, 1412–1421 (2012). https://doi.org/10.1007/s10953-012-9869-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10953-012-9869-5