Characterization of drug-plasma protein interactions using surface plasmon resonance
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چکیده
Binding to plasma proteins is a key parameter in evaluating candidate compounds during the lead optimization and early ADME phases of the drug development process. Biacore’s surface plasmon resonance (SPR) technology is ideally suited for the analysis of multiple aspects of drug-plasma protein interactions. BiacoreS51 was used to analyze a panel of low molecular weight drug compounds for binding to human plasma proteins, using a two-stage assay strategy. Compounds were first ranked in terms of protein binding using a rapid, single-concentration assay. High affinity binders were then selected for a more comprehensive assay, in which compounds were analyzed over a range of concentrations and from which equilibrium constants were calculated. The results demonstrate that high-affinity plasma protein binders can be efficiently discriminated by SPR-derived affinity analyses and that these data can be simply converted to %-bound values that are simulated for defined plasma proteins.
منابع مشابه
Characterization of drug-plasma protein interactions using surface plasmon resonance
Binding to plasma proteins is a key parameter in evaluating candidate compounds during the lead optimization and early ADME phases of the drug development process. Surface plasmon resonance (SPR) technology is ideally suited for the analysis of multiple aspects of drug-plasma protein interactions. Here we describe how a BiacoreTM SPR based system was used to analyze a panel of low molecular wei...
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تاریخ انتشار 2002