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Solution Observation of Dimerization and Helix Handedness Induction in a Human Carbonic Anhydrase-Helical Aromatic Amide Foldamer Complex

dc.contributor.authorJEWGINSKI, Michal
dc.contributor.authorFISCHER DUROLA, Lucile
dc.contributor.authorCOLOMBO, Cinzia
dc.contributor.authorHUC, Ivan
dc.contributor.authorMACKERETH, Cameron D.
dc.date.accessioned2020-09-03T07:56:15Z
dc.date.available2020-09-03T07:56:15Z
dc.date.issued2016
dc.identifier.issn1439-4227
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10856
dc.description.abstractEnThe design of synthetic foldamers to selectively bind proteins is currently hindered by the limited availability of molecular data to establish key features of recognition. Previous work has described dimerization of human carbonic anhydraseII (HCA) through self-association of a quinoline oligoamide helical foldamer attached to a tightly binding HCA ligand. A crystal structure of the complex provided atomic details to explain the observed induction of single foldamer helix handedness and revealed an unexpected foldamer-mediated dimerization. Here, we investigated the detailed behavior of the HCA-foldamer complex in solution by using NMR spectroscopy. We found that the ability to dimerize is buffer-dependent and uses partially distinct intermolecular contacts. The use of a foldamer variant incapable of self-association confirmed the ability to induce helix handedness separately from dimer formation and provided insight into the dynamics of enantiomeric selection.
dc.language.isoen
dc.title.enSolution Observation of Dimerization and Helix Handedness Induction in a Human Carbonic Anhydrase-Helical Aromatic Amide Foldamer Complex
dc.typeArticle de revue
dc.subject.halChimie/Matériaux
bordeaux.journalChemBioChem
bordeaux.page727-736
bordeaux.volume17
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=ChemBioChem&rft.date=2016&rft.volume=17&rft.issue=8&rft.spage=727-736&rft.epage=727-736&rft.eissn=1439-4227&rft.issn=1439-4227&rft.au=JEWGINSKI,%20Michal&FISCHER%20DUROLA,%20Lucile&COLOMBO,%20Cinzia&HUC,%20Ivan&MACKERETH,%20Cameron%20D.&rft.genre=article


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