Gel permeation chromatographic method for drug protein binding studies

Yıl 2017, Cilt: 21 Sayı: 4, 938 - 948, 01.12.2017

Manish Bhatıa Swapnil Jadhav Santosh Kumbhar

Öz

The estimation of individual plasma protein in free and bound

form with analytes has importance in pharmacokinetics

study. Albumins and globulins are most abundantly found in

plasma and plays crucial role in plasma protein binding. The

present communication deals with the development of gel

permeation chromatographic method for the estimation of

plasma protein binding studies for ketoprofen, tapentadol and

furaltadone. The method was developed using WATER system

with Ultrahydrogel column (7.8 x 300 mm i.d.), refractive index

detector (1.00 to 1.75 RIU) and Rheodyne injection valve fitted

with a 20μl sample loop using 0.1% sodium nitrate as a mobile

phase. The method was developed by studying binding above

drugs with most of plasma proteins. These complexes have

shown linearity in range of 100 to 300μg/ml of these drugs. The

developed method has been validated using USFDA guidelines.

The developed bioanalytical method is accurate, precise, and

selective and sensitive for quantification of plasma proteins

bound drugs. The further optimization of method using

other standard plasma proteins will explore its applicability

in pharmacokinetic and biopharmaceutical studies of most of

drugs.

Anahtar Kelimeler

Bovine serum albumin; gel permeation chromatography; plasma protein binding; human serum albumin.

Kaynakça

• 1. Goodman GA. The pharmacological basis of therapeutics, 9th edition. MacGrow Hill, New York. 1996. 2. Tajminr-Riahi HA. An overview of drug binding to human serum albumin: protein folding and unfolding. Scientia Iranica 2007; 14: 87-95. 3. Kratochwil NA, Walter H, Fransis M, Malfred K, Poul RJ. Predicting plasma protein binding of drugs: a new approach. Biochem Pharmacol 2002; 64: 1355-74. 4. Anastasios D. Applicability of the modified universal calibration of gel permeation chromatography on proteins. J Chromatogr 2006; 183–6. 5. Bernd T. Size-exclusion Chromatography of Polymers, Encyclopedia of Analytical Chemistry. Karl-Franzens- University, Graz, Austria. John Wiley & Sons Ltd. 2000, pp. 8008–8034. 6. David AH, Robert BF. Resolution of protein disulphideisomerase and glutathione-insulin transhydrogenase activities by covalent chromatography. Biochem J 1980; 191; 373-88. 7. Hideo H, Kayoko A, Ewamura J. Immunofluorescence determination of Ig G in cerebrospinal fluid following high performance liquid gel permeation chromatography. J Immunol Methods 1987; 98: 1-4. 8. Morris CJOR, Morris P. Molecular-Sieve chromatography and electrophoresis in polyacrylamide gels. Biochem J 1971; 124: 517-28. 9. Plet JM, Van den O, Cees PM, Breed JS, Herman JH. Detection of serum proteins by high-pressure gel-permeation chromatography with low-angle laser light scattering compared with analytical ultracentrifugation. Clin Chem 1986; 32: 363-7. 10. Kuzayev AI. Determining absolute molecular weights of styrene and ethylene oxide oligomers by gel permeation chromatography. Polymer Sci U.S.S.R. 1980; 22: 1260-7. 11. Shah RB, Yang Y, Khan MA, Faustino PJ. Molecular weight determination for colloidal iron by Taguchi optimized validated gel permeation chromatography. Int J Pharm 2008; 353: 21–7. 12. Van den Eijnden-van Raaij AJM, Koornneef I, van Oostwaard MJ, de Laat SW, van Zoelen EJJ. Cation-exchange highperformance liquid chromatography: separation of highly basic proteins using volatile acidic solvents. Anal Biochem 1987; 163: 263-9. 13. Winfried M, Rudiger S, Hubert S, Ullrich B, Werner G. Fast lipoprotein chromatography: New method of analysis for plasma lipoproteins. Clin Chem 1993; 39: 2276-81. 14. Fernández SO, Rodríguez JA, Padilla AP. Removal concentration and desalination of bovine serum albumin (BSA) with membrane technology. European Conference on Desalination and the Environment 1999; 126: 95-100. 15. Hiroyuki H, Motoaki A, Yasuyugi T. An endonuclease associated with bovine plasma albumin fraction’. J Biol Chem 1972; 247: 193-8. 16. Jacinto S, Johanna K, Joan GL. Differences between bovine and human serum albumins. Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects. Biochem 1971; 10: 4005–15. 17. Jaldappa S, Bhalchandra K. Mechanism of interaction of vincristine sulphate and rifampicin with Bovine serum albumin: A spectroscopic study. J Chem Sci 2005; 117: 649– 55. 18. Alpert J, Shukla AK. Precipitation of large, high abundance proteins from serum with organic solvents. ABRF. 2003; (2/3; Denver): Poster# P111-W. 19. Bardarov V, Shishenkov M, Bardarov K. Application of preparative size-exclusion chromatography (SEC) for separation/clean-up of platelets from blood plasma before their chemical investigation. J Univ Chem Technol Metallurgy 2012; 47: 97-102. 20. Teresa F, Roman K, Michal M. Estimation of buspirone- Bovine serum albumin binding by affinity capillary electrophoresis. Acta Pol Pharm–Drug Res 2001; 58: 319-23. 21. Pal PK, Ganesan M. Bioavailability and Bioequivalence in Pharmaceutical Technology, 1st ed. CBS Publishers and Distributors, New Delhi. 1999, pp 1–145. 22. U.S. Department of Health and Human Services Food and Drug Administration (USFDA). Guidance for Industry: Bioanalytical Method Validation. Rockville: Center for Drug Evaluation and Research, USFDA, May 2001.