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Targeting clinically-relevant metallo-ß-lactamases: from high-throughput docking to broad-spectrum inhibitors.
Brindisi, Margherita; Brogi, Simone; Giovani, Simone; Gemma, Sandra; Lamponi, Stefania; De Luca, Filomena; Novellino, Ettore; Campiani, Giuseppe; Docquier, Jean-Denis; Butini, Stefania.
Afiliação
  • Brindisi M; a European Research Centre for Drug Discovery and Development (NatSynDrugs), University of Siena , Siena , Italy.
  • Brogi S; b Department of Biotechnology , Chemistry and Pharmacy, University of Siena , Siena , Italy.
  • Giovani S; a European Research Centre for Drug Discovery and Development (NatSynDrugs), University of Siena , Siena , Italy.
  • Gemma S; b Department of Biotechnology , Chemistry and Pharmacy, University of Siena , Siena , Italy.
  • Lamponi S; a European Research Centre for Drug Discovery and Development (NatSynDrugs), University of Siena , Siena , Italy.
  • De Luca F; b Department of Biotechnology , Chemistry and Pharmacy, University of Siena , Siena , Italy.
  • Novellino E; a European Research Centre for Drug Discovery and Development (NatSynDrugs), University of Siena , Siena , Italy.
  • Campiani G; b Department of Biotechnology , Chemistry and Pharmacy, University of Siena , Siena , Italy.
  • Docquier JD; a European Research Centre for Drug Discovery and Development (NatSynDrugs), University of Siena , Siena , Italy.
  • Butini S; b Department of Biotechnology , Chemistry and Pharmacy, University of Siena , Siena , Italy.
J Enzyme Inhib Med Chem ; 31(sup1): 98-109, 2016.
Article em En | MEDLINE | ID: mdl-27121013
ABSTRACT
Metallo-ß-lactamases (MBLs) represent one of the most important and widespread mechanisms of resistance to ß-lactam antibiotics (including the life-saving carbapenems), against which no clinically useful inhibitors are currently available. We report herein a structure-based high-throughput docking (HTD) campaign on three clinically-relevant acquired MBLs (IMP-1, NDM-1 and VIM-2). The initial hit NF1810 (1) was optimized providing the broad-spectrum inhibitor 3i, which is able to potentiate the in vitro activity of cefoxitin on a VIM-2-producing E. coli strain.
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Ensaios de Triagem em Larga Escala / Simulação de Acoplamento Molecular / Inibidores de beta-Lactamases / Antibacterianos Limite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Itália
Buscar no Google
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PubMed Links

Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Ensaios de Triagem em Larga Escala / Simulação de Acoplamento Molecular / Inibidores de beta-Lactamases / Antibacterianos Limite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Itália