Probing the structure of the warfarin-binding site on human serum albumin using site-directed mutagenesis

2002 ◽  
Vol 47 (2) ◽  
pp. 116-125 ◽  
Author(s):  
Charles E. Petersen ◽  
Chung-Eun Ha ◽  
Stephen Curry ◽  
Nadhipuram V. Bhagavan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Site-directed mutagenesis studies of human serum albumin define tryptophan at amino acid position 214 as the principal site for nitrosation

2002 ◽  
Vol 9 (1) ◽  
pp. 47-58 ◽  
Author(s):  
Krishna Harohalli ◽  
Charles E. Petersen ◽  
Chung-Eun Ha ◽  
Jimmy B. Feix ◽  
Nadhipuram V. Bhagavan
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Position ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals TOPOLOGY ANALYSIS OF DRUG BINDING SITES ON HUMAN SERUM ALBUMIN USING SITE-DIRECTED MUTAGENESIS

2000 ◽  
Vol 15 (supplement) ◽  
pp. 122-123
Author(s):  
Hiroshi WATANABE ◽  
Sumio TANASE ◽  
Keisuke NAKAJOU ◽  
Yasunori IWAO ◽  
Maki MITARAI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Topology Analysis ◽  
Drug Binding Sites

Chain Length-dependent Binding of Fatty Acid Anions to Human Serum Albumin Studied by Site-directed Mutagenesis

2006 ◽  
Vol 363 (3) ◽  
pp. 702-712 ◽  
Author(s):  
Ulrich Kragh-Hansen ◽  
Hiroshi Watanabe ◽  
Keisuke Nakajou ◽  
Yasunori Iwao ◽  
Masaki Otagiri
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chain Length ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

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.

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