JEWGINSKI, Michal; FISCHER DUROLA, Lucile; COLOMBO, Cinzia; HUC, Ivan; MACKERETH, Cameron D.

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JEWGINSKI, Michal

FISCHER DUROLA, Lucile

COLOMBO, Cinzia

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Article de revue

Ce document a été publié dans

ChemBioChem. 2016, vol. 17, n° 8, p. 727-736

Résumé en anglais

The 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.< Réduire

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https://oskar-bordeaux.fr/handle/20.500.12278/10856

Unités de recherche

CBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248