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Structural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers

dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCUSSOL, Leonie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMAURAN-AMBROSINO, Laura
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBURATTO, Jeremie
dc.contributor.authorBELORUSOVA, Anna Y.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorNEUVILLE, Maxime
dc.contributor.authorOSZ, Judit
hal.structure.identifierAcides Nucléiques : Régulations Naturelle et Artificielle [ARNA]
dc.contributor.authorFRIBOURG, Sebastien
dc.contributor.authorFREMAUX, Juliette
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDOLAIN, Christel
dc.contributor.authorGOUDREAU, Sebastien R.
dc.contributor.authorROCHEL, Natacha
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
dc.date.accessioned2021-07-08T14:07:27Z
dc.date.available2021-07-08T14:07:27Z
dc.date.issued2021
dc.identifier.issn1433-7851en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/106475
dc.description.abstractEnEfficient optimization of a peptide lead into a drug candidate frequently needs further transformation to augment properties such as bioavailability. Among the different options, foldamers, which are sequence-based oligomers with precise folded conformation, have emerged as a promising technology. We introduce oligourea foldamers to reduce the peptide character of inhibitors of protein-protein interactions (PPI). However, the precise design of such mimics is currently limited by the lack of structural information on how these foldamers adapt to protein surfaces. We report a collection of X-ray structures of peptide-oligourea hybrids in complex with ubiquitin ligase MDM2 and vitamin D receptor and show how such hybrid oligomers can be designed to bind with high affinity to protein targets. This work should enable the generation of more effective foldamer-based disruptors of PPIs in the context of peptide lead optimization.
dc.language.isoENen_US
dc.subject.enPeptidomimetics
dc.subject.enFoldamers
dc.subject.enProtein-protein interactions
dc.subject.enHelical structures
dc.subject.enStructure-activity relationships
dc.title.enStructural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers
dc.typeArticle de revueen_US
dc.identifier.doi10.1002/anie.202008992en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalAngewandte Chemie-International Editionen_US
bordeaux.page2296-2303en_US
bordeaux.volume60en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue5en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03039251
hal.exportfalse
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Angewandte%20Chemie-International%20Edition&rft.date=2021&rft.volume=60&rft.issue=5&rft.spage=2296-2303&rft.epage=2296-2303&rft.eissn=1433-7851&rft.issn=1433-7851&rft.au=CUSSOL,%20Leonie&MAURAN-AMBROSINO,%20Laura&BURATTO,%20Jeremie&BELORUSOVA,%20Anna%20Y.&NEUVILLE,%20Maxime&rft.genre=article


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