Analytical Characterization of Chiral Drug−Protein Interactions:  Comparison between the Optical Biosensor (Surface Plasmon Resonance) Assay and the HPLC Perturbation Method

2006 ◽  
Vol 78 (5) ◽  
pp. 1682-1689 ◽  
Author(s):  
Robert Arnell ◽  
Natalia Ferraz ◽  
Torgny Fornstedt
Langmuir ◽  
2006 ◽  
Vol 22 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Taewook Kang ◽  
Surin Hong ◽  
Hyun Jin Kim ◽  
Jungwoo Moon ◽  
Seogil Oh ◽  
...  

2010 ◽  
Vol 114 (8) ◽  
pp. 3346-3353 ◽  
Author(s):  
Sabine Szunerits ◽  
Slimane Ghodbane ◽  
Joanna Niedziółka-Jönsson ◽  
Elisabeth Galopin ◽  
Frederik Klauser ◽  
...  

Bioanalysis ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 193-207 ◽  
Author(s):  
Jia Duo ◽  
JoAnne Bruno ◽  
Steven Piccoli ◽  
Binodh DeSilva ◽  
Yan J Zhang

2019 ◽  
Vol 27 (15) ◽  
pp. 21717
Author(s):  
Tsz Kit Yung ◽  
Ranran Zhang ◽  
Qiuling Zhao ◽  
Xia Wang ◽  
Wensheng Gao ◽  
...  

2009 ◽  
Vol 53 (4) ◽  
pp. 1528-1531 ◽  
Author(s):  
Françoise Banères-Roquet ◽  
Maxime Gualtieri ◽  
Philippe Villain-Guillot ◽  
Martine Pugnière ◽  
Jean-Paul Leonetti

ABSTRACT The pharmacologic effect of an antibiotic is directly related to its unbound concentration at the site of infection. Most commercial antibiotics have been selected in part for their low propensity to interact with serum proteins. These nonspecific interactions are classically evaluated by measuring the MIC in the presence of serum. As higher-throughput technologies tend to lose information, surface plasmon resonance (SPR) is emerging as an informative medium-throughput technology for hit validation. Here we show that SPR is a useful automatic tool for quantification of the interaction of model antibiotics with serum proteins and that it delivers precise real-time kinetic data on this critical parameter.


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