Tailoring the Physicochemical Properties of Antimicrobial Peptides onto a Thiazole-Based γ-Peptide Foldamer.

Autor:	Bonnel C; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France., Legrand B; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France., Simon M; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France., Clavié M; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France., Masnou A; Laboratoire HydroSciences Montpellier, UMR 5569, CNRS, UM, IRD, Département d'Hygiène Hospitalière-CHU Montpellier, 34095 Montpellier, France., Jumas-Bilak E; Laboratoire HydroSciences Montpellier, UMR 5569, CNRS, UM, IRD, Département d'Hygiène Hospitalière-CHU Montpellier, 34095 Montpellier, France., Kang YK; Department of Chemistry, Chungbuk National University, Cheongju, Chungbuk 28644, Republic of Korea., Licznar-Fajardo P; Laboratoire HydroSciences Montpellier, UMR 5569, CNRS, UM, IRD, Département d'Hygiène Hospitalière-CHU Montpellier, 34095 Montpellier, France., Maillard LT; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France., Masurier N; Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, UM, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France.
Jazyk:	angličtina
Zdroj:	Journal of medicinal chemistry [J Med Chem] 2020 Sep 10; Vol. 63 (17), pp. 9168-9180. Date of Electronic Publication: 2020 Aug 31.
DOI:	10.1021/acs.jmedchem.0c00077
Abstrakt:	Antimicrobial peptides (AMPs) are amphipathic molecules displaying broad-spectrum bactericidal activity, providing opportunities to develop a new generation of antibiotics. However, their use is limited either by poor metabolic stability or by high hemolytic activity. We herein addressed the potential of thiazole-based γ-peptide oligomers named ATCs as tunable scaffolds to design polycationic AMP mimetics. Knowing the side chain distribution along the backbone, we rationally designed facially amphiphilic sequences with bactericidal effect in the micromolar range. Since no hemolytic activity was detected up to 100 μM, this class of compounds has shown the potential for therapeutic development.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu