REDDY, Post Sai; D'ESTAINTOT, Beatrice Langlois; GRANIER, Thierry; MACKERETH, Cameron D.; FISCHER DUROLA, Lucile; HUC, Ivan

doi:10.1002/chem.201902942

Metadatos

Mostrar el registro completo del ítem

Licencia de uso del documento

REDDY, Post Sai
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

D'ESTAINTOT, Beatrice Langlois
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

GRANIER, Thierry

Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

Idioma

Article de revue

Este ítem está publicado en

Chemistry-a European Journal. 2019, vol. 25, p. 11042-11047

Resumen en inglés

The development of large synthetic ligands could be useful to target the sizeable surface areas involved in protein-protein interactions. Herein, we present long helical aromatic oligoamide foldamers bearing proteinogenic side chains that cover up to 450 angstrom(2) of the human carbonic anhydrase II (HCA) surface. The foldamers are composed of aminoquinolinecarboxylic acids bearing proteinogenic side chains and of more flexible aminomethyl-pyridinecarboxylic acids that enhance helix handedness dynamics. Crystal structures of HCA-foldamer complexes were obtained with a 9- and a 14-mer both showing extensive protein-foldamer hydrophobic contacts. In addition, foldamer-foldamer interactions seem to be prevalent in the crystal packing, leading to the peculiar formation of an HCA superhelix wound around a rod of stacked foldamers. Solution studies confirm the positioning of the foldamer at the protein surface as well as a dimerization of the complexes.< Leer menos

Palabras clave en inglés

aromatic oligoamides

foldamers

protein surface recognition

structure elucidation

X-ray crystallography

Metadatos

Compartir este ítem

Licencia de uso del documento

Structure Elucidation of Helical Aromatic Foldamer-Protein Complexes with Large Contact Surface Areas

Idioma

Este ítem está publicado en

Resumen en inglés

Palabras clave en inglés

URI

DOI

Centros de investigación