DRUGPROFILBIND
"Chemogenomic profiling of drug-protein binding by shape, enthalpy/entropy and interaction kinetics"
| Coordinatore | PHILIPPS UNIVERSITAET MARBURG
Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie. |
| Nazionalità Coordinatore | Germany [DE] |
| Totale costo | 1˙754˙615 € |
| EC contributo | 1˙754˙615 € |
| Programma | FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
| Code Call | ERC-2010-AdG_20100317 |
| Funding Scheme | ERC-AG |
| Anno di inizio | 2011 |
| Periodo (anno-mese-giorno) | 2011-05-01 - 2016-04-30 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
PHILIPPS UNIVERSITAET MARBURG
Organization address
address: Biegenstrasse 10 contact info |
DE (MARBURG) | hostInstitution | 1˙754˙615.20 |
| 2 |
PHILIPPS UNIVERSITAET MARBURG
Organization address
address: Biegenstrasse 10 contact info |
DE (MARBURG) | hostInstitution | 1˙754˙615.20 |
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Obiettivo del progetto (Objective)
'Once a new drug target is discovered, screening techniques are applied to detect prospective hits. However, which hit should be taken to the next level of development? This decision is most crucial as it entails huge financial commitments of the subsequent drug optimization. In consequence drugs are only developed against diseases that promise short-term profit. Chemogenomic profiling allows to compile parameters characterizing binding of drug candidates that achieve optimal interference with protein function. Membrane proteins demand different properties than viral ones. Either high isoform selectivity, promiscuous family-wide binding or efficient resistance tolerance is desired. This calls for very different ligand binding characteristics, requiring either enthalpy-/entropy-driven binding, rigid shape complementarity or pronounced residual mobility at the binding site. Interaction kinetics determine on/off-rates and the time a drug spends with its target. Their correct adjustment is essential for drug efficacy. At present chemogenomic binding parameters are rarely available and their correlation with the required target properties is hardly understood. We want to compile a knowledge base from congeneric protein-ligand series to correlate structural, thermodynamic, interaction-kinetic and dynamic behaviour to predict the qualities a lead must meet to optimally address a target. Our studies involve crystal structure analyses, microcalorimetry, molecular dynamics simulations, site-directed mutagenesis and interaction kinetics. This provides a comprehensive picture to productively change our current understanding of drug-protein binding to move from a current trial-and-error to a more efficient rational approach. It provides the opportunity to also consider orphan drugs and address neglected diseases.'