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Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries

hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorJEWGINSKI, Michal
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRANIER, Thierry
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLANGLOIS D'ESTAINTOT, Beatrice
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorFISCHER DUROLA, Lucile
hal.structure.identifierAcides Nucléiques : Régulations Naturelle et Artificielle [ARNA]
dc.contributor.authorMACKERETH, Cameron D.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHUC, Ivan
dc.date.accessioned2020-07-09T14:16:49Z
dc.date.available2020-07-09T14:16:49Z
dc.date.issued2017-03
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10310
dc.description.abstractEnThe promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA2-23 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization.
dc.title.enSelf-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries
dc.typeArticle de revue
dc.identifier.doi10.1021/jacs.7b00184
dc.subject.halChimie/Matériaux
bordeaux.journalJournal of the American Chemical Society
bordeaux.page2928-2931
bordeaux.volume139
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue8
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.date=2017-03&rft.volume=139&rft.issue=8&rft.spage=2928-2931&rft.epage=2928-2931&rft.au=JEWGINSKI,%20Michal&GRANIER,%20Thierry&LANGLOIS%20D'ESTAINTOT,%20Beatrice&FISCHER%20DUROLA,%20Lucile&MACKERETH,%20Cameron%20D.&rft.genre=article


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