Structure of a Complex Formed by a Protein and a Helical Aromatic Oligoamide Foldamer at 2.1 angstrom Resolution

In the search of molecules that could recognize sizeable areas of protein surfaces, a series of ten helical aromatic oligoamide foldamers was synthesized on solid phase. The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interco...

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Bibliographic Details
Published inAngewandte Chemie International Edition Vol. 53; no. 3; pp. 883 - 887
Main Authors Buratto, Jeremie, Colombo, Cinzia, Stupfel, Marine, Dawson, Simon J., Dolain, Christel, d'Estaintot, Beatrice Langlois, Fischer, Lucile, Granier, Thierry, Laguerre, Michel, Gallois, Bernard, Huc, Ivan
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 13.01.2014
Subjects
Chemistry
Chemistry, Multidisciplinary
Physical Sciences
Science & Technology
DESIGN
ANTAGONIST
RECOGNITION
HANDEDNESS
circular dichroism
solid-phase synthesis
foldamers
protein recognition
crystallography
CARBONIC-ANHYDRASE-II
AFFINITY
SURFACE
INHIBITORS
RNA APTAMER
BINDING
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Summary:In the search of molecules that could recognize sizeable areas of protein surfaces, a series of ten helical aromatic oligoamide foldamers was synthesized on solid phase. The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interconverting right-handed and left-handed helices. Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase II (HCA) ensured that they would be held in close proximity to the protein surface. Foldamer-protein interactions were screened by circular dichroism (CD). One foldamer displayed intense CD bands indicating that a preferred helix handedness is induced upon interacting with the protein surface. The crystal structure of the complex between this foldamer and HCA could be resolved at 2.1 angstrom resolution and revealed a number of unanticipated protein-foldamer, foldamer-foldamer, and protein-protein interactions.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201309160