Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking

Author:

Farnoush Faridbod^a   Mohammad Reza Ganjali^{b   ganjali@khayam.ut.ac.ir}   Bagher Larijani^b   Siavash Riahi^{c   a}   Ali Akbar Saboury^d   Morteza Hosseini^e   Parviz Norouzi^b  Christoph Pillip^b  

Journal:

Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

Issue Date:

2011

Abstract(summary):

Pioglitazone is a medicine of thiazolidinedione (TZD) class with hypoglycemic (antihyperglycemic, antidiabetic) action. Pioglitazone binding to human serum albumin (HSA) was investigated at different temperatures (290, 300 and 310 K) by fluorescence spectroscopic method. Molecular docking study was also carried out besides the experiments. Experimental results revealed that pioglitazone have an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The binding constant was determined using Stern–Volmer modified equation and energy transfer mechanisms of quenching were discussed. Thermodynamic parameters were also calculated according to enthalpy changes dependence on different temperatures. According to the theoretical and experimental results, hydrogen bonding was found to play a major role in the interaction of pioglitazone with HSA.

Page:

96-101