title: Interactions between m-phenylenediamine and bovine serum albumin measured by spectroscopy.
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.
authors.affiliation: State Key Laboratory of Pollution Control and Resource Reuse, School of the Environment, Nanjing University, Nanjing, China.
authors.forename: Jian-qiu
authors.initials: JQ
authors.lastname: Chen
authors.forename: Zhi-jun
authors.initials: ZJ
authors.lastname: Hu
authors.forename: Nan-xi
authors.initials: NX
authors.lastname: Wang
authors.forename: Rong
authors.initials: R
authors.lastname: Ji
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D010655:Phenylenediamines / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
chemical_list: D010655:Phenylenediamines; D012710:Serum Albumin, Bovine; C008381:3-phenylenediamine