Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2009 | 7 | 1 | 96-104
Tytuł artykułu

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Treść / Zawartość
Warianty tytułu
Języki publikacji
The mechanism of interaction of hypoglycemic drugs, glimepiride and glipizide with human serum albumin (HSA) has been studied using fluorescence spectroscopy. The results are discussed in terms of the binding parameters, thermodynamics of the binding process, nature of forces involved in the interaction, identification of drug binding site on serum albumin and the fluorescence quenching mechanism involved. The association constants were of the order of 105 and glipizide was found to have much higher affinity for HSA than glimepiride at all temperatures. Thermodynamic parameters for the binding suggested that hydrophobic interactions are primarily involved in the binding of these drugs to HSA. However, glimepiride and glipizide appear to cause temperature-dependent conformational changes in the albumin molecule and, therefore, the nature of interaction varied with temperature. Glimepiride and glipizide bind to both site I and site II on HSA, but the primary interaction occurs at site II. The binding region in site II is different for the two drugs. Stern-Volmer analysis of quenching data indicated that tryptophan residues of HSA are not fully accessible to the drugs and a predominantly dynamic quenching mechanism is involved in the binding. Results can provide useful insight into prediction of competitive displacement of these drugs by other co-administered drugs and excipients, resulting in serious fluctuations of the blood glucose levels in diabetic patients. [...]
Słowa kluczowe

Opis fizyczny
  • Department of Chemistry, Panjab University, Chandigarh, 160014, India,
  • Department of Chemistry, Panjab University, Chandigarh, 160014, India
  • [1] U. Kragh-Hansen, V.T.G. Chuang, M. Otagiri, Biol. Pharm. Bull. 25, 695 (2002)[Crossref]
  • [2] C. Bertucci, E. Domenici, Curr. Med. Chem. 9, 1463 (2002)
  • [3] U. Kragh-Hansen, Pharmacol. Rev. 33, 17 (1981)
  • [4] P. Hsu, J.K.H. Ma, L.A. Luzzi, J. Pharm. Sci. 63, 570 (1974)[Crossref]
  • [5] T. Izumi, Biopharm. Drug Disp. 18, 241 (1997)<241::AID-BDD17>3.0.CO;2-O[Crossref]
  • [6] H. Gao, L.D. Lei, J.Q. Liu, Q. Kong, X.G. Chen, Z.D. Hu, J. Photochem. Photobiol. A: Chem. 167, 213 (2004)[Crossref]
  • [7] N. Zhou, Y. Liang, P. Wang, J. Mol. Struc. 872, 190 (2008)[Crossref]
  • [8] A. Sulkowska, M. Maciazek-Jurczyk, B. Bojko, J. Rownicka, I. Zubik-Skupien, E. Temba, D. Pentak, W.W. Sulkowski, J. Mol. Struc. 881, 97 (2008)[Crossref]
  • [9] M.H. Rahman, T. Maruyama, T. Okada, K. Yamasaki, M. Otagiri, Biochem Pharmacol 46, 1721 (1993)[Crossref]
  • [10] G. Weber, L.B. Young, J Biol. Chem. 239, 1415 (1964)
  • [11] T. Maruyama, M. Otagiri, S.G. Schulman, Int. J. Pharm. 59, 137 (1990)[Crossref]
  • [12] L.D. Ward, Methods Enzymol. 117, 400 (1985)[Crossref]
  • [13] B.K. Martin, Nature 207, 274 (1965)[Crossref]
  • [14] S. Jamzad, R. Fassihi, AAPS PharmSciTech. 7, E17 (2006)[Crossref]
  • [15] J. Kang, Y. Liu, M. Xie, S. Li, M. Jiang, Y. Wang, Biochim. Biophys. Acta 1674, 205 (2004)
  • [16] B. Kljnert, L. Stainislawska, M. Bryszewska, B. Palecz, Biochim. Biophys. Acta 1648, 115 (2003)
  • [17] W. Zhong, Y. Wang, J. Yu, Y. Liang, K. Ni, S. Tu, J. Pharm. Sci. 93, 1039 (2004)[Crossref]
  • [18] H. Zia, J.C. Price, J. Pharm. Sci. 64, 1177 (1975)[Crossref]
  • [19] E.J. Lien, P.H. Wang, J. Pharm. Sci. 69, 648 (1980)[Crossref]
  • [20] D. Silva, C.M. Cortez, R.W. Louro, Spectrochimica Acta Part A 60, 1215 (2004)[Crossref]
  • [21] Y.H. Pang, L.L. Yang, S.M. Shuang, C. Dong, M. Thompson, J. Photochem. Photobiol. B: Biology 80, 139 (2005)[Crossref]
  • [22] W. He, Y. Li, C. Xue, Z. Hu, X. Chen, F. Sheng, Bioorg. Med. Chem. 13, 1837 (2005)[Crossref]
  • [23] P.D. Ross, S. Subramanian, Biochemistry 20, 3096 (1981)[Crossref]
  • [24] A. Sulkowska, B. Bojko, J. Rownicka, W.W. Sulkowski, J. Mol. Struc. 792, 249 (2006)[Crossref]
  • [25] H.W. Jun, P.C. Ruenitz, J. Pharm. Sci. 67, 861 (1978)[Crossref]
  • [26] A.E.A. Thumser, A.G. Buckland, D.C. Wilton, J. Lipid Res. 39, 1033 (1998)
  • [27] G. Sudlow, D. Birkett, D. Wade, Mol. Pharmacol. 11, 824 (1975)
  • [28] B. Nerli, D. Romanini, G. Pico, Chemico-Biological Interact. 104, 179 (1997)[Crossref]
  • [29] S. Sugio, A. Kashima, S. Mochizuki, M. Noda, K. Kobayashi, Protein Eng. 12, 439 (1999)[Crossref]
  • [30] X.M. He, D.C. Carter, Nature 358, 209 (1992)[Crossref]
  • [31] M.R. Eftink, C.A. Ghiron, Anal. Biochem. 114, 199 (1981)[Crossref]
  • [32] P. Midoux, P. Wahl, J. Auchet, M. Monsigny, Biochim. Biophys. Acta 801, 16 (1984)
Typ dokumentu
Identyfikator YADDA
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.