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Elucidation of the Teixobactin Pharmacophore.
Yang, Hyunjun; Chen, Kevin H; Nowick, James S.
Afiliación
  • Yang H; Department of Chemistry, University of California, Irvine , Irvine, California 92697-2025, United States.
  • Chen KH; Department of Chemistry, University of California, Irvine , Irvine, California 92697-2025, United States.
  • Nowick JS; Department of Chemistry, University of California, Irvine , Irvine, California 92697-2025, United States.
ACS Chem Biol ; 11(7): 1823-6, 2016 07 15.
Article en En | MEDLINE | ID: mdl-27232661
This paper elucidates the teixobactin pharmacophore by comparing the arginine analogue of teixobactin Arg10-teixobactin to seven homologues with varying structure and stereochemistry. The roles of the guanidinium group at position 10, the stereochemistry of the macrolactone ring, and the "tail" comprising residues 1-5 are investigated. The guanidinium group is not necessary for activity; Lys10-teixobactin is more active than Arg10-teixobactin against Gram-positive bacteria in minimum inhibitory concentration (MIC) assays. The relative stereochemistry of the macrolactone ring is important. Diastereomer l-Thr8,Arg10-teixobactin is inactive, and diastereomer d-allo-Ile11,Arg10-teixobactin is less active. The macrolactone ring is critical; seco-Arg10-teixobactin is inactive. The absolute stereochemistry is not important; the enantiomer ent-Arg10-teixobactin is comparable in activity. The hydrophobic N-terminal tail is important. Truncation of residues 1-5 results in loss of activity, and replacement of residues 1-5 with a dodecanoyl group partially restores activity. These findings pave the way for developing simpler homologues of teixobactin with enhanced pharmacological properties.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Depsipéptidos / Antibacterianos Idioma: En Revista: ACS Chem Biol Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Depsipéptidos / Antibacterianos Idioma: En Revista: ACS Chem Biol Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos