Person:
Martín-Fontecha Corrales, María Del Mar

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First Name
María Del Mar
Last Name
Martín-Fontecha Corrales
URI
https://hdl.handle.net/20.500.14352/79945
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Óptica y Optometría
Department
Química Orgánica
Area
Química Orgánica
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Author: Araujo Bazán, Lidia × Subject: 615.28 ×

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    Targeting the FtsZ Allosteric Binding Site with a Novel Fluorescence Polarization Screen, Cytological and Structural Approaches for Antibacterial Discovery
    (Journal of Medicinal Chemistry, 2021) Huecas, Sonia; Araujo Bazán, Lidia; Ruiz, Federico M.; Ruiz Ávila, Laura, Laura B.; Martínez, R. Fernando; Escobar Peña, Ana Andrea; Artola, Marta; Vázquez Villa, María Del Henar; Martín-Fontecha Corrales, María Del Mar; Fernández Tornero, Carlos; López Rodríguez, María Luz; Andreu, José M.
    Bacterial resistance to antibiotics makes previously manageable infections again disabling and lethal, highlighting the need for new antibacterial strategies. In this regard, inhibition of the bacterial division process by targeting key protein FtsZ has been recognized as an attractive approach for discovering new antibiotics. Binding of small molecules to the cleft between the N-terminal guanosine triphosphate (GTP)-binding and the C-terminal subdomains allosterically impairs the FtsZ function, eventually inhibiting bacterial division. Nonetheless, the lack of appropriate chemical tools to develop a binding screen against this site has hampered the discovery of FtsZ antibacterial inhibitors. Herein, we describe the first competitive binding assay to identify FtsZ allosteric ligands interacting with the interdomain cleft, based on the use of specific high-affinity fluorescent probes. This novel assay, together with phenotypic profiling and X-ray crystallographic insights, enables the identification and characterization of FtsZ inhibitors of bacterial division aiming at the discovery of more effective antibacterials.