Title:Binding of a bcl-2 Family Inhibitor to Bovine Serum Albumin: Fluorescence Quenching and Molecular Docking Study
Volume: 19
Issue: 9
Author(s): Rui Zhao, Yonghua Xie, Ying Tan, Chunyan Tan and Yuyang Jiang
Affiliation:
Keywords:
Binding site, BSA, fluorescence quenching, molecular docking, stern-volmer equation
Abstract: Both fluorescence spectroscopic and molecular docking methods were used to investigate the interaction between
bovine serum albumin (BSA) and a known Bcl-xl/Bcl-2 inhibitor HA 14-1. Based on the spectral overlap between
the emission of BSA and absorption of HA 14-1, Forster energy transfer was proposed to be the possible quenching
mechanism. The Stern-Volmer constants are 2.49 x 104, 2.04x 104 and 0.90 x 104 M-1 at 293, 303 and 318 K, respectively,
indicating that a static quenching process dominates. Thermodynamic parameters were further obtained. The derived
negative Δ H (-27.51 kJ mol-1) and Δ S (-11.11 J mol-1K-1) values suggest hydrogen bond interaction and van der Waals
force are the main binding force. The docking study was performed on BSA model. According to the docking score and
the number of hydrogen bonds, the potential binding site for HA 14-1 is proposed to be the site IIA, also known as drug
site 1.