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Interactions between m ‐phenylenediamine and bovine serum albumin measured by spectroscopy
Author(s) -
Chen Jianqiu,
Hu Zhijun,
Wang Nanxi,
Ji Rong
Publication year - 2012
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2369
Subject(s) - bovine serum albumin , chemistry , quenching (fluorescence) , analytical chemistry (journal) , spectrophotometry , fluorescence , spectroscopy , fluorescence spectroscopy , hydrophobic effect , chromatography , biochemistry , physics , quantum mechanics
ABSTRACT 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.