Title : ( A novel view on interaction between human serum albumin and three different drugs as binary system by fluorescence spectroscopy )
Authors: M. Pirouzi , H. Salari , Ahmad Asoodeh , J. Chamani ,
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Abstract
Human serum albumin (HAS) was the most abundant protein in human plasma and has significant physiological function. The interaction betwwen estradiol, cyclophosphamide and aspirin with HAS was studied by fluorescence spectroscopy in this work. The results indicated that intrinsic fluorescence of HAS was strongly quenched by the three drugs. The Stern-Volmer quenching constant, Ksv was estimated and determined the binding affinity three drugs estradiol, cyclophosphamide and aspirin to human serum albumin. The Ksv values showed that the binding affinity of cyclophodphamide was more than estradiol and aspirin.
Keywords
, Human Serum albumin, Estradiol, Cyclophosphamide, Aspirin, Fluorescence spectroscopy.
@inproceedings{paperid:1029724,
author = {M. Pirouzi and H. Salari and Asoodeh, Ahmad and J. Chamani},
title = {A novel view on interaction between human serum albumin and three different drugs as binary system by fluorescence spectroscopy},
booktitle = {The First National Green Chemistry Congress Kerman, Iran, 14-15 December, 2011},
year = {2011},
location = {کرمان, IRAN},
keywords = {Human Serum albumin; Estradiol; Cyclophosphamide; Aspirin; Fluorescence spectroscopy.},
}
%0 Conference Proceedings
%T A novel view on interaction between human serum albumin and three different drugs as binary system by fluorescence spectroscopy
%A M. Pirouzi
%A H. Salari
%A Asoodeh, Ahmad
%A J. Chamani
%J The First National Green Chemistry Congress Kerman, Iran, 14-15 December, 2011
%D 2011
