albumin - publications

Predict more albumin - ligand interactions now!


1. Protein Pept Lett. 2012 Apr 9. [Epub ahead of print]

Binding of a bcl-2 family inhibitor to bovine serum albumin: fluorescence
quenching and molecular docking study.

Zhao R, Xie Y, Tan Y, Tan C, Jiang Y.

Key Laboratory of Chemical Biology, Guangdong Province, Graduate School at
Shenzhen, Tsinghua University, Shenzhen 518055 P. R. China.
jiangyy@sz.tsinghua.edu.cn.

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, Förster energy transfer was proposed
to be the possible quenching mechanism. The Stern-Volmer constants are 2.49 ×
104, 2.04× 104 and 0.90 × 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 ΔH (-27.51 kJ mol-1) and ΔS (-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.

PMID: 22486616 [PubMed - as supplied by publisher]