Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry

There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.

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Detalles Bibliográficos
Autores principales: Justin M. Di Trani, Stephane De Cesco, Rebecca O’Leary, Jessica Plescia, Claudia Jorge do Nascimento, Nicolas Moitessier, Anthony K. Mittermaier
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/695ef23f7e8d4d87a44cc9ad450d7ebc
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Descripción
Sumario:There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.