scholarly journals In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Hideto Isogai ◽  
Noriaki Hirayama
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Mode ◽  
X Ray ◽  
Docking Simulations ◽  
X Ray Crystallography ◽  
Inflammatory Drugs ◽  
Multiple Template

Since binding of a drug molecule to human serum albumin (HSA) significantly affects the pharmacokinetics of the drug, it is highly desirable to predict the binding affinity of the drug. Profen drugs are a widely used class of nonsteroidal anti-inflammatory drugs and it has been reported that several members of the profen class specifically bind to one of the main binding sites named site II. The actual binding mode of only ibuprofen has been directly confirmed by X-ray crystallography. Therefore, it is of interest whether other profen drugs are site II binders. Docking simulations using multiple template structures of HSA from three crystal structures of complexes between drugs and HSA have demonstrated that most of the currently available profen drugs should be site II binders.

Cisplatin binding to human serum albumin: a structural study

2015 ◽  
Vol 51 (46) ◽  
pp. 9436-9439 ◽  
Author(s):  
Giarita Ferraro ◽  
Lara Massai ◽  
Luigi Messori ◽  
Antonello Merlino
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Crystal Structures ◽  
Structural Study ◽  
X Ray ◽  
X Ray Crystallography ◽  
First Time

The reaction between cisplatin and human serum albumin (HSA) was investigated by X-ray crystallography and crystal structures of the cisplatin/HSA adduct were eventually solved for the first time.

scholarly journals The Effect of Tigecycline on the Binding of Fluoroquinolones to Human Serum Albumin

2018 ◽  
Vol 19 (1) ◽  
pp. 17-25 ◽  
Author(s):  
Ratomir M. Jelic ◽  
Stefan D. Stojanovic ◽  
Jelena D. Beric ◽  
Jadranka Odovic
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Interaction Mechanism ◽  
Binding Constants ◽  
Binding Mode ◽  
Binding Ability ◽  
Free Plasma

AbstractThe co-administration of several drugs in multidrug therapy may alter the binding of each drug to human serum albumin (HSA) and, thus, their pharmacology effect. Therefore, in this study, the interaction mechanism between HSA and two fluoroquinolones (FQs), sparfloxacin (SPF) and levofloxacin (LVF), was investigated using fluorescence and absorption methods in the absence and presence of the competing drugtigecycline (TGC). The the UV-Vis and fluorescence spectroscopy results showed that the fluorescence quenching of HSA was a result of the formation of the HSA-SPF and HSA-LVF complexes. The fluorescence quenching of HSA-TGC revealed that tigecycline can regulate the binding sites, binding mode and binding affinity of fluoroquinolones. The binding constants (KA) and binding sites (n) of the interaction systems were calculated. The results confirmed that the KA values of the HSA-FQ system decreased in the presence of TGC, indicating that TGC can affect the binding ability of FQ for HSA. This interaction may increase the free plasma concentration of unbound FQ and enhance their pharmacology effect.

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

Zinc–human serum albumin association: testimony of two binding sites

Talanta ◽  
2004 ◽  
Vol 63 (2) ◽  
pp. 503-508 ◽  
Author(s):  
C. André ◽  
Y.C. Guillaume
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites

scholarly journals Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

2012 ◽  
Vol 18 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Orsolya Dömötör ◽  
Christian G. Hartinger ◽  
Anna K. Bytzek ◽  
Tamás Kiss ◽  
Bernhard K. Keppler ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites
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