Variation in the binding affinity of warfarin and phenprocoumon to human serum albumin in relation to surgery

1993 ◽  
Vol 44 (2) ◽  
pp. 157-162 ◽  
Author(s):  
H. Vorum ◽  
H. R. I. J�rgensen ◽  
R. Brodersen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity

A fluorescent probe for butyrylcholinesterase activity in human serum based on a fluorophore with specific binding affinity for human serum albumin

2019 ◽  
Vol 55 (97) ◽  
pp. 14574-14577 ◽  
Author(s):  
Soyeon Yoo ◽  
Min Su Han
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescent Probe ◽  
Binding Affinity ◽  
Specific Binding ◽  
Turn On ◽  
High Binding ◽  
Butyrylcholinesterase Activity ◽  
High Binding Affinity

We report a novel turn-on sensing probe for the detection of butyrylcholinesterase activity in human serum using a fluorophore with high binding affinity for 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

scholarly journals Development and Validation Molecular Docking Analysis of Human serum albumin (HSA)

2021 ◽  
Author(s):  
IVAN VITO FERRARI ◽  
Paolo Patrizio
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Water Soluble ◽  
Inhibition Constant ◽  
Ligand Efficiency ◽  
Protein Preparation ◽  
Docking Analysis

Background: HAS (Human Serum Albumin) is a highly water-soluble globular plasma protein, with a relative molecular weight (g/mol) of 67 KDa, consisting of 585 amino acid residues. In this study, we have investigated the interaction of the crystal structures complexed in human serum albumin at resolutions of 2.8 to 2.0: Camptothecin, 9-amino-camptothecin, Etoposide, Teniposide, Bicalutamide and Idarubicin, using a bioinformatic approach, estimated by Pyrx Virtual Screen Tool and AMDock ( AMDock, Assisted Molecular Docking). We have analyzed a validated protocol, studying several parameters, as Binding Affinity, RMSD value, Ligand Efficiency, and Inhibition constant (Ki value). Methods: Human Serum Albumin protein preparation was characterized with several programs, as Chimera, MGLTools 1.5.6, Swiss PDB Viewer Software to perform docking analysis by Autodock Vina estimated with Pyrx Software. Results: In this work, we found crystalized camptothecin, 9-amino-camptothecin and teniposide, gave excellent results for Binding Affinity, (kcal/mol), RMSD value (A ), inhibition constant Ki value (nM): -Binding Affinity of 9-amino-camptothecin (ca.-10 kcal/mol), camptothecin ( -9 kcal/mol) and teniposide ( -11 kcal/mol, -RMSD Value of 9 -amino-camptothecin (ca.1.8 A ), camptothecin (ca.2.2 A ) and teniposide (ca. 3.6 A), - Ki Value: 9 -amino-camptothecin (ca 59 nM), camptothecin ( ca 183 nM) and teniposide ( ca 9 nM), -Ligand efficiency: of 9 -amino-camptothecin(ca -0.35 kcal/mol) , camptothecin (ca -0.34 kcal/mol) and teniposide (ca -0.24 kcal/mol Conclusions: We explored the best three crystallized ligand in Human Serum Albumin. Moreover, we have observed a complete overlap, during the re-docking analysis phase, estimated by chimera Software. Therefore we have concluded that ID PDB Crystal 4L8U human serum albumin-Crystallised 9 -amino Camptothecin; ID PDB Crystal 4L9K human serum albumin- Crystallised Camptothecin and ID PDB Crystal 4L9Q human serum albumin-Crystallised teniposide be used as a possible as a reference template protein to be compared with the target protein, by Docking molecular analysis.

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