Journal
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
Volume 54, Issue -, Pages 255-263Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.ejmech.2012.05.007
Keywords
Human serum albumin; Amodiaquin; Fluorescence; Binding; Molecular modeling
Categories
Funding
- Shiraz University Research Council
Ask authors/readers for more resources
The interaction of amodiaquine (AQ) with human serum albumin (HSA) has been studied by fluorescence spectroscopy. Based on the sign and magnitude of the enthalpy and entropy changes (Delta H-0 = -43.27 kJ mol(-1) and as Delta S-0 = -50.03 J mol(-1) K-1), hydrogen bond and van der Waals forces were suggested as the main interacting forces. Moreover, the efficiency of energy transfer and distance between HSA and acceptor AQ was calculated. Finally, the binding of AQ to HSA was modeled by molecular docking and molecular dynamic simulation methods. Excellent agreement was found between the experimental and theoretical results. Both experimental results and modeling methods suggested that AQ binds mainly to the sub-domain IIA of HSA. (c) 2012 Elsevier Masson SAS. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available