Interaction of an anticancer drug, gefitinib with human serum albumin: insights from fluorescence spectroscopy and computational modeling analysis

RSC Advances ◽  
2016 ◽  
Vol 6 (94) ◽  
pp. 91756-91767 ◽  
Author(s):  
Md. Zahirul Kabir ◽  
Wei-Ven Tee ◽  
Saharuddin B. Mohamad ◽  
Zazali Alias ◽  
Saad Tayyab
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Computational Modeling ◽  
Human Serum ◽  
Binding Site ◽  
Anticancer Drug ◽  
Modeling Analysis ◽  
Binding Orientation

Binding orientation of the GEF in the binding site III, located in subdomain IB of HSA.

Interactions of polyglycerol dendrimers with human serum albumin: insights from fluorescence spectroscopy and computational modeling analysis

2019 ◽  
Vol 30 (17) ◽  
pp. 1575-1590 ◽  
Author(s):  
Pedro Palhari Santos ◽  
Alexandro da Silva Nunes ◽  
Alfredo Antonio Alencar Exposito de Queiroz ◽  
Alvaro Antonio Alencar de Queiroz
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Computational Modeling ◽  
Human Serum ◽  
Modeling Analysis ◽  
Polyglycerol Dendrimers

scholarly journals Interaction between Alizarin and Human Serum Albumin by Fluorescence Spectroscopy

2011 ◽  
Vol 27 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Feng GE ◽  
Lixiang JIANG ◽  
Diqiu LIU ◽  
Chaoyin CHEN
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum

FLUORESCENCE CHANGE OF HUMAN SERUM ALBUMIN INDUCED BY METHYL VIOLET

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 261-264
Author(s):  
M.A. Shahinyan ◽  
N.H. Petrosyan ◽  
A.P. Antonyan
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Change ◽  
Fluorescence Intensity ◽  
Methyl Violet ◽  
Spectroscopy Method ◽  
Intensity Maximum ◽  
Fluorescence Change

The interaction of methyl violet (MV) with human serum albumin (HSA) has been studied, using the fluorescence spectroscopy method. It was shown that MV chnages the own fluorescence of HSA. It was also shown that MV does not induce any conformational change in the structure of HSA, since there is no change of the wavelength of HSA fluorescence intensity maximum. MV binds to HSA, near to fluorescing tryptophan, which in the hydrophilic environment, and changes the own fluorescence of the protein.

scholarly journals Indomethacin Increases Quercetin Affinity for Human Serum Albumin: A Combined Experimental and Computational Study and Its Broader Implications

2020 ◽  
Vol 21 (16) ◽  
pp. 5740
Author(s):  
Hrvoje Rimac ◽  
Tana Tandarić ◽  
Robert Vianello ◽  
Mirza Bojić
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Quantum Chemical ◽  
Computational Study ◽  
The Body ◽  
Active Concentration ◽  
Insight Into

Human serum albumin (HSA) is the most abundant carrier protein in the human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of the HSA-indomethacin-quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. The results show that the indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten the xenobiotics’ half-life in the body, depending on the desired outcomes.

Sign in / Sign up

Export Citation Format

Share Document