Anatomy of an Oligourea Six-Helix Bundle
dc.relation.isnodouble | 9dfcc4de-caa7-40ef-b463-804e187beb78 | * |
dc.contributor.author | LOMBARDO, Caterina M. | |
dc.contributor.author | COLLIE, Gavin W. | |
dc.contributor.author | PULKA-ZIACH, Karolina | |
dc.contributor.author | ROSU, Frederic | |
dc.contributor.author | GABELICA, Valérie | |
dc.contributor.author | MACKERETH, Cameron D. | |
dc.contributor.author | GUICHARD, Gilles
IDREF: 084339268 | |
dc.date.accessioned | 2020-09-03T07:56:12Z | |
dc.date.available | 2020-09-03T07:56:12Z | |
dc.date.issued | 2016 | |
dc.identifier.issn | 0002-7863 | |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/10844 | |
dc.description.abstractEn | Non-natural synthetic oligomers that adopt well-defined secondary structures (i.e., foldamers) represent appealing components for the fabrication of bioinspired self assembled architectures at the nanometer scale. Recently, peptidomimetic N,N'-linked oligourea helices have been designed de novo with the ability to fold into discrete helix bundles in aqueous conditions. In order to gain better insight into the determinants of oligourea helix bundle formation, we have investigated the sequence-to-structure relationship of an 11-mer oligourea previously shown to assemble into a six-helix bundle. Using circular dichroism, NMR spectroscopy, native mass-spectrometry and X-ray crystallography, we studied how bundle formation was affected by systematic replacement of the hydrophobic surface of the oligourea helix with either polar or different hydrophobic side chains. The molecular information gathered here has revealed several key requirements for foldamer bundle formation in aqueous conditions, and provides valuable insight toward the development of foldamer quaternary assemblies with improved (bio)physical properties and divergent topologies. | |
dc.language.iso | en | |
dc.title.en | Anatomy of an Oligourea Six-Helix Bundle | |
dc.type | Article de revue | |
dc.subject.hal | Chimie/Matériaux | |
bordeaux.journal | Journal of the American Chemical Society | |
bordeaux.page | 10522-10530 | |
bordeaux.volume | 138 | |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | * |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248) | |
bordeaux.issue | 33 | |
bordeaux.institution | Université de Bordeaux | |
bordeaux.institution | Bordeaux INP | |
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