albumin - publications

Predict more albumin - ligand interactions now!


1. Luminescence. 2012 Apr 18. doi: 10.1002/bio.2369. [Epub ahead of print]

Interactions between m-phenylenediamine and bovine serum albumin measured by
spectroscopy.

Chen JQ, Hu ZJ, Wang NX, Ji R.

State Key Laboratory of Pollution Control and Resource Reuse, School of the
Environment, Nanjing University, Nanjing, 210093, China; Department of
Environmental Science and Department of Analytical Chemistry, China
Pharmaceutical University, Nanjing, 210009, China.

This study explored interactions between m-phenylenediamine (MPD) and bovine
serum albumin (BSA) by spectrophotometry. The Stern-Volmer equation and UV-vis
spectra examination at different temperatures and pH were used to explore
different quenching mechanisms. Under simulated physiological conditions, the
binding distance between MPD and BSA was 5.18 nm with a ratio of 1:1. The
quenching effect of MPD on BSA intrinsic fluorescence depended strongly on pH,
and maximum quenching was observed at alkaline pH. Moreover, the thermodynamic
parameters of the MPD-BSA system showed that the predominant acting force between
MPD and BSA was a hydrophobic force. The impact of MPD on the conformation of BSA
and the effects of co-ions on binding interactions were also examined. Copyright
© 2012 John Wiley & Sons, Ltd.

Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 22511621 [PubMed - as supplied by publisher]