Article details
Journal
Biotechnology and Food Science
Volume 76 Number 1
Volume 76 Number 1
Year
2012
Title
Binding of harmane to human and bovine serum albumin: fluorescence and phosphorescence study
Authors
Krystian Gałęcki,1* Biljana Despotović,2 Céline Galloway,3
Angelos-Gerasimos Ioannidis,4 Tahereh Janani5, Yuki Nakamura,6
Grace Oluyinka7
1 Institute of General Food Chemistry, Lodz University of Technology,
90-924 Lodz, Poland
2 University of Sarajevo, 71000, Sarajevo, Bosnia and Hercegowina
3 University of Newcastle Upon Tyne, NE1 7RU, Newcastle Upon Tyne, England
4 Agricultural University of Athens, 11855, Athens, Greece
5 Norwegian University of Science and Technology, 7491, Trondheim, Norway
6 Kyushu University, 8120053, Fukuoka, Japan
7 University of Greenwich, SE10 9LS, London, England
*kgalecki87@gmail.com
Pages: 3 - 12
Abstract
The binding of harmane with human serum albumin (HSA) and bovine serum albumin (BSA) were studied by fluorescence and phosphorescence spectroscopic methods. Quenching of fluorescence of serum albumins by harmane was found to be a static quenching process. The equilibrium constant (K) of complex formation was found to be equal to (5.16±0.28)x104 M-1 and (4.32±0.30)x104 M-1 for HSA and BSA, respectively. It was found that the interactions of harmane with HSA and BSA were also in the excited triplet state. The determined bimolecular
constant or triplet state quenching (kqT)of the proteins studied by harmane was (1.15± 0.10)x107 M-1 s-1 and (2.88±0.22)x107 M-1 s-1 for HSA and BSA, respectively. Based on the similar value of K and kqT for HSA and BSA, a
possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa.
possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa.
Keywords
human and bovine serum albumin, harmane, fluorescence,
phosphorescence