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

• Published in: Luminescence (Chichester, England) Vol. 28; no. 2; pp. 226 - 231
• Main Authors: Chen, Jian-qiu, Hu, Zhi-jun, Wang, Nan-xi, Ji, Rong
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.03.2013; Wiley Subscription Services, Inc
• Subjects: Animals; Binding; Binding Sites; bovine serum albumin; Cattle; fluorescence spectrophotometry; interaction; m-Phenylenediamine; Phenylenediamines - chemistry; Protein Binding; Protein Conformation; quenching mechanisms; Serum Albumin, Bovine - chemistry; Spectrophotometry, Ultraviolet; Thermodynamics
• ISSN: 1522-7235; 1522-7243
• DOI: 10.1002/bio.2369

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.