scholarly journals Physiological concentrations of albumin favor drug binding

2015 ◽  
Vol 17 (35) ◽  
pp. 22678-22685 ◽  
Author(s):  
D. Tatlidil ◽  
M. Ucuncu ◽  
Y. Akdogan

We exploit the direct measurements of spin labeled drugs to study drug binding to/release from protein using EPR spectroscopy.

2016 ◽  
Vol 18 (32) ◽  
pp. 22531-22539 ◽  
Author(s):  
Y. Akdogan ◽  
M. Emrullahoglu ◽  
D. Tatlidil ◽  
M. Ucuncu ◽  
G. Cakan-Akdogan

EPR spectroscopy is a very promising technique to understand the details of drug binding and competitive drug binding to proteins.


2001 ◽  
Vol 29 (1) ◽  
pp. 5-18 ◽  
Author(s):  
Omoefe O. Abugo ◽  
Chavali Balagopalakrishna ◽  
Joseph M. Rifkind ◽  
Alan S. Rudolph ◽  
John R. Hess ◽  
...  

2003 ◽  
Vol 56 (9) ◽  
pp. 855 ◽  
Author(s):  
William S. Price

Characterizing the binding of ligands to macromolecular receptors in solution is important to many areas of chemistry, biology, and nanobiotechnology, but perhaps most notably to drug development. NMR has proven to be particularly useful for such studies, but the systems studied have generally been restricted to model systems with dubious physiological relevance. This paper reviews the use of NMR diffusion measurements to study drug binding and two recent advances that enable measurements to be conducted in more sensitive higher-field NMR spectrometers in non-deuterated aqueous samples.


2021 ◽  
Vol 57 (14) ◽  
pp. 1814-1817
Author(s):  
Cécile Echalier ◽  
Anna Rutkowska ◽  
Ana Kojic ◽  
Douglas W. Thomson ◽  
Lee J. Edwards ◽  
...  

We provide a new tagging entity for click chemistry to perform improved drug binding assays in intact cells.


2005 ◽  
Vol 28 (3-4) ◽  
pp. 251-265 ◽  
Author(s):  
G. S. Shakurov ◽  
M. V. Vanyunin ◽  
B. Z. Malkin ◽  
B. Barbara ◽  
R. Yu. Abdulsabirov ◽  
...  

2018 ◽  
Author(s):  
Ying Yu Liang ◽  
Anderson Ramos ◽  
Henriette Laursen ◽  
Olga Surova ◽  
Johan Lengqvist ◽  
...  

Author(s):  
R. H. Liss

Piperacillip (PIP) is b-[D(-)-α-(4-ethy1-2,3-dioxo-l-piperzinylcar-bonylamino)-α-phenylacetamido]-penicillanate. The broad spectrum semisynthetic β-lactam antibiotic is believed to effect bactericidal activity through its affinity for penicillin-binding proteins (PBPs), enzymes on the bacterial cytoplasmic membrane that control elongation and septation during cell growth and division. The purpose of this study was to correlate penetration and binding of 14C-PIP in bacterial cells with drug-induced lethal changes assessed by microscopic, microbiologic and biochemical methods.The bacteria used were clinical isolates of Escherichia coli and Pseudomonas aeruginosa (Figure 1). Sensitivity to the drug was determined by serial tube dilution in Trypticase Soy Broth (BBL) at an inoculum of 104 organisms/ml; the minimum inhibitory concentration of piperacillin for both bacteria was 1 μg/ml. To assess drug binding to PBPs, the bacteria were incubated with 14C-PIP (5 μg/0.09 μCi/ml); controls, in drug-free medium.


2011 ◽  
Vol 45 (8) ◽  
pp. 21
Author(s):  
DAMIAN McNAMARA

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