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

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.

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.

The binding of 3-(p-bromophenyl)-5-methyl-thiohydantoin with human serum albumin: Investigation by fluorescence spectroscopy and molecular model

2007 ◽  
Vol 127 (2) ◽  
pp. 409-415 ◽  
Author(s):  
Fengling Cui ◽  
Junli Wang ◽  
Yanrui Cui ◽  
Jianping Li ◽  
Xiaojun Yao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Model
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