Artículo
Speeding-up the Determination of Protein-Ligand Affinities by STD NMR: The Reduced Data Set STD NMR Approach (rd-STD NMR)
Autor/es | Rocha, Gabriel
Ramírez Cárdenas, Jonathan Padilla Pérez, María del Carmen ![]() ![]() ![]() ![]() ![]() ![]() Walpole, Samuel Nepravishta, Ridvan García Moreno, M. Isabel ![]() ![]() ![]() ![]() ![]() ![]() Sánchez Fernández, Elena Matilde ![]() ![]() ![]() ![]() ![]() ![]() Ortiz Mellet, Carmen ![]() ![]() ![]() ![]() ![]() ![]() ![]() Angulo, Jesús Muñoz García, Juan Carlos |
Departamento | Universidad de Sevilla. Departamento de Química orgánica |
Fecha de publicación | 2024-01-02 |
Fecha de depósito | 2024-06-24 |
Publicado en |
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Resumen | STD NMR spectroscopy is a powerful ligand-observed NMR tool for screening and characterizing the interactions of small molecules and low molecular weight fragments with a given macromolecule, identifying the main intermolecular ... STD NMR spectroscopy is a powerful ligand-observed NMR tool for screening and characterizing the interactions of small molecules and low molecular weight fragments with a given macromolecule, identifying the main intermolecular contacts in the bound state. It is also a powerful analytical technique for the accurate determination of protein–ligand dissociation constants (KD) of medium-to-weak affinity, of interest in the pharmaceutical industry. However, accurate KD determination and epitope mapping requires a long series of experiments at increasing saturation times to carry out a full analysis using the so-called STD NMR build-up curve approach and apply the “initial slopes approximation”. Here, we have developed a new protocol to bypass this important limitation, which allows us to obtain initial slopes by using just two saturation times and, hence, to very quickly determine precise protein–ligand dissociation constants by STD NMR. |
Agencias financiadoras | Ministerio de Ciencia e Innovación (MICIN). España Agencia Estatal de Investigación. España European Commission (EC). Fondo Europeo de Desarrollo Regional (FEDER) Universidad de Sevilla |
Identificador del proyecto | PID2019- 109395GB-I00
![]() PID2022-142879NB-I00 ![]() PID2019-105858RB-I00 ![]() PID2022-141034OB-C21 ![]() USE VII PPIT ![]() |
Cita | Rocha, G., Ramírez Cárdenas, J., Padilla Pérez, M.d.C., Walpole, S., Nepravishta, R., García Moreno, M.I.,...,Muñoz García, J.C. (2024). Speeding-up the Determination of Protein-Ligand Affinities by STD NMR: The Reduced Data Set STD NMR Approach (rd-STD NMR). Analytical Chemistry, 96 (2), 615-619. https://doi.org/10.1021/acs.analchem.3c03980. |
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rocha-et-al-2024.pdf | 1.886Mb | ![]() | Ver/ | |