QSAR Modeling of Human Serum Protein Binding with Several Modeling Techniques Utilizing Structure−Information Representation

2006 ◽  
Vol 49 (24) ◽  
pp. 7169-7181 ◽  
Author(s):  
Joseph R. Votano ◽  
Marc Parham ◽  
L. Mark Hall ◽  
Lowell H. Hall ◽  
Lemont B. Kier ◽  
...  
2013 ◽  
Vol 42 (33) ◽  
pp. 11841 ◽  
Author(s):  
Gisela Gonçalves ◽  
Isabel Tomaz ◽  
Isabel Correia ◽  
Luís F. Veiros ◽  
M. Margarida C. A. Castro ◽  
...  

2015 ◽  
Vol 59 (11) ◽  
pp. 7121-7123 ◽  
Author(s):  
Henrietta Abodakpi ◽  
Jie Gohlke ◽  
Kai-Tai Chang ◽  
Diana S.-L. Chow ◽  
Vincent H. Tam

ABSTRACTTo enhance our understanding of the pharmacological properties of polymyxin B, serum protein binding for polymyxin B1, B2, and B3 and for isoleucine-polymyxin B1 was evaluated. Using equilibrium dialysis and ultrafiltration, comparable protein binding was found in all 4 components of polymyxin B (92% to 99%). Protein binding in human serum was further assessed using a functional assay, the results of which were in general agreement with previous findings (approximately 90%).


2010 ◽  
Vol 54 (8) ◽  
pp. 3481-3483 ◽  
Author(s):  
Francis F. Arhin ◽  
Adam Belley ◽  
Geoffrey McKay ◽  
Sylvain Beaulieu ◽  
Ingrid Sarmiento ◽  
...  

ABSTRACT Biophysical methods to study the binding of oritavancin, a lipoglycopeptide, to serum protein are confounded by nonspecific drug adsorption to labware surfaces. We assessed oritavancin binding to serum from mouse, rat, dog, and human by a microbiological growth-based method under conditions that allow near-quantitative drug recovery. Protein binding was similar across species, ranging from 81.9% in human serum to 87.1% in dog serum. These estimates support the translation of oritavancin exposure from nonclinical studies to humans.


2021 ◽  
pp. 174751982199306
Author(s):  
Ya Gan ◽  
Ning Bai ◽  
Xitong Li ◽  
Shuiting Gao ◽  
Ruiyong Wang

The interactions between radicicol and four proteins (catalase, trypsin, pepsin, and human serum protein) are investigated by spectroscopic techniques and molecular docking. A static quenching process is confirmed. The binding constant value between radicicol and human serum protein is the largest among the four proteins. Results reveal changes in the micro-environment of the protein by the addition of radicicol. It is found that radicicol shows an inhibitory effect on the activity of proteins (catalase, trypsin, and pepsin). Molecular docking results are consistent with the thermodynamic experimental results. This work provides clues to the elucidation of the mechanisms of the interactions between radicicol and proteins.


1984 ◽  
Vol 61 (2) ◽  
pp. 127-133 ◽  
Author(s):  
Dennis E. Coyle ◽  
Donald D. Denson ◽  
Gary A. Thompson ◽  
Jane A. Myers ◽  
G. Richard Arthur ◽  
...  

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