scholarly journals Stoichiometry and Binding Site Analysis of Ligand-Human Serum Albumin Complex by Photoaffinity Labeling and Mass Spectrometry

2005 ◽  
Vol 53 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Katsuyoshi MASUDA ◽  
Kohichi KAWAHARA ◽  
Akihiko KUNIYASU ◽  
Masaji ISHIGURO ◽  
Hitoshi NAKAYAMA
Keyword(s):  
Mass Spectrometry ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Photoaffinity Labeling ◽  
Site Analysis

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.

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.

The binding affinity of amino acid–protein: hydroxyproline binding site I on human serum albumin

2012 ◽  
Vol 10 (41) ◽  
pp. 8314 ◽  
Author(s):  
Ximin Zhou ◽  
Wenjuan Lü ◽  
Li Su ◽  
Yalei Dong ◽  
Qianfeng Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Affinity ◽  
Acid Protein ◽  
Amino Acid Protein
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