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dc.rights.licenseopenen_US
dc.contributor.authorTALLET, Lorene
dc.contributor.authorFRISCH, Emilie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBORNERIE, Megane
dc.contributor.authorMEDEMBLIK, Claire
dc.contributor.authorFRISCH, Benoit
dc.contributor.authorLAVALLE, Philippe
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
IDREF: 084339268
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDOUAT, Celine
dc.contributor.authorKICHLER, Antoine
dc.date.accessioned2024-09-19T08:14:48Z
dc.date.available2024-09-19T08:14:48Z
dc.date.issued2022-03-07
dc.identifier.issn1420-3049en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/201674
dc.description.abstractEnThere is an urgent need to develop new therapeutic strategies to fight the emergence of multidrug resistant bacteria. Many antimicrobial peptides (AMPs) have been identified and characterized, but clinical translation has been limited partly due to their structural instability and degradability in physiological environments. The use of unnatural backbones leading to foldamers can generate peptidomimetics with improved properties and conformational stability. We recently reported the successful design of urea-based eukaryotic cell-penetrating foldamers (CPFs). Since cell-penetrating peptides and AMPs generally share many common features, we prepared new sequences derived from CPFs by varying the distribution of histidine- and arginine-type residues at the surface of the oligourea helix, and evaluated their activity on both Gram-positive and Gram-negative bacteria as well as on fungi. In addition, we prepared and tested new amphiphilic block cofoldamers consisting of an oligourea and a peptide segment whereby polar and charged residues are located in the peptide segment and more hydrophobic residues in the oligourea segment. Several foldamer sequences were found to display potent antibacterial activities even in the presence of 50% serum. Importantly, we show that these urea-based foldamers also possess promising antifungal properties.
dc.language.isoENen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subject.enAmphiphilic cationic foldamers
dc.subject.enAntibacterial activity
dc.subject.enAntifungal properties
dc.subject.enOligourea-peptide hybrids
dc.subject.enOligoureas
dc.title.enDesign of Oligourea-Based Foldamers with Antibacterial and Antifungal Activities
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/molecules27051749en_US
dc.subject.halChimie/Matériauxen_US
dc.identifier.pubmed35268850en_US
bordeaux.journalMoleculesen_US
bordeaux.volume27en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue5en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDMinistère de l'Enseignement supérieur, de la Recherche et de l'Innovationen_US
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
dc.rights.ccCC BY-NC-NDen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Molecules&rft.date=2022-03-07&rft.volume=27&rft.issue=5&rft.eissn=1420-3049&rft.issn=1420-3049&rft.au=TALLET,%20Lorene&FRISCH,%20Emilie&BORNERIE,%20Megane&MEDEMBLIK,%20Claire&FRISCH,%20Benoit&rft.genre=article


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