UREkA Sarl

Pessac, France

UREkA Sarl

Pessac, France
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French National Center for Scientific Research and UREKA Sarl | Date: 2017-03-08

The present description provides compositions and methods for producing therapeutic oligomeric compounds. In another aspect the description provides methods for administering the oligomeric compounds for the treatment and prevention of disease in a mammal. In particular, the disclosure relates to medicaments comprising various novel oligomeric compounds and pharmaceutically acceptable salts thereof. The compounds of the disclosure may optionally be administered with at least one of a pharmaceutically acceptable excipient, additional pharmacologically active agent or a combination thereof.

Collie G.W.,University of Bordeaux Segalen | Bailly R.,French National Center for Scientific Research | Pulka-Ziach K.,University of Bordeaux Segalen | Lombardo C.M.,University of Bordeaux Segalen | And 6 more authors.
Journal of the American Chemical Society | Year: 2017

Artificial synthetic molecules able to adopt well-defined stable secondary structures comparable to those found in nature (“foldamers”) have considerable potential for use in a range of applications such as biomaterials, biorecognition, nanomachines and as therapeutic agents. The development of foldamers with the ability to bind and encapsulate “guest” molecules is of particular interest; as such an ability is a key step toward the development of artificial sensors, receptors and drug-delivery vectors. Although significant progress has been reported within this context, foldamer capsules reported thus far are largely restricted to organic solvent systems, and it is likely that the move to aqueous conditions will prove challenging. Toward this end, we report here structural studies into the ability of a recently reported water-soluble self-assembled foldamer helix bundle to encapsulate simple guest molecules within an internal cavity. Seven high-resolution aqueous crystal structures are reported, accompanied by molecular dynamics and high-field NMR solution data, showing for the first time that encapsulation of guests by a complex self-assembled foldamer in aqueous conditions is possible. The findings also provide ample insight for the future functional development of this system. © 2017 American Chemical Society.

Collie G.W.,University of Bordeaux Segalen | Pulka-Ziach K.,French National Center for Scientific Research | Lombardo C.M.,University of Bordeaux Segalen | Fremaux J.,French Institute of Health and Medical Research | And 7 more authors.
Nature Chemistry | Year: 2015

The design and construction of biomimetic self-Assembling systems is a challenging yet potentially highly rewarding endeavour that contributes to the development of new biomaterials, catalysts, drug-delivery systems and tools for the manipulation of biological processes. Significant progress has been achieved by engineering self-Assembling DNA-, protein-And peptide-based building units. However, the design of entirely new, completely non-natural folded architectures that resemble biopolymers ( € foldamers €) and have the ability to self-Assemble into atomically precise nanostructures in aqueous conditions has proved exceptionally challenging. Here we report the modular design, formation and structural elucidation at the atomic level of a series of diverse quaternary arrangements formed by the self-Assembly of short amphiphilic α-helicomimetic foldamers that bear proteinaceous side chains. We show that the final quaternary assembly can be controlled at the sequence level, which permits the programmed formation of either discrete helical bundles that contain isolated cavities or pH-responsive water-filled channels with controllable pore diameters. © 2015 Macmillan Publishers Limited. All rights reserved.

Fremaux J.,University of Bordeaux Segalen | Fremaux J.,UREkA Sarl | Kauffmann B.,University of Bordeaux Segalen | Guichard G.,University of Bordeaux Segalen
Journal of Organic Chemistry | Year: 2014

The synthesis and conformational analysis of aliphatic oligoureas containing multiple adjacent N-alkylated units derived from proline (i.e., Prou) are reported. The insertion of trisubstituted ureas in the main chain of N,N′-linked oligourea foldamers locally impairs the characteristic three centered-hydrogen bonding pattern associated with the formation of 2.5-helical structures. Three series of oligomers have been studied: one series in which the Prou repeat is flanked on both sides by canonical urea residues (e.g., oligomers 2-6), one series with canonical residues on either side of the Prou repeat (oligomers 12 and 23), and one series consisting exclusively of Prou residues (oligomers 25 and 26). Spectroscopic (NMR and electronic circular dichroism) and X-ray diffraction studies reveal that the 2.5-helix formed by oligomers of N,N′-disubstituted ureas is robust enough to accommodate short oligopyrrolidine segments (Prou)n (n < 7) that alone display no intrinsic folding propensity. © 2014 American Chemical Society.

Fremaux J.,University of Bordeaux Segalen | Fremaux J.,French National Center for Scientific Research | Fremaux J.,UREkA Sarl | Mauran L.,University of Bordeaux Segalen | And 12 more authors.
Angewandte Chemie - International Edition | Year: 2015

Short α-peptides with less than 10 residues generally display a low propensity to nucleate stable helical conformations. While various strategies to stabilize peptide helices have been previously reported, the ability of non-peptide helical foldamers to stabilize α-helices when fused to short α-peptide segments has not been investigated. Towards this end, structural investigations into a series of chimeric oligomers obtained by joining aliphatic oligoureas to the C- or N-termini of α-peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an α-helical conformation in the fused peptide segment. The remarkable compatibility of α-peptides with oligoureas described here, along with the simplicity of the approach, highlights the potential of interfacing natural and non-peptide backbones as a means to further control the behavior of α-peptides. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Mauran L.,University of Bordeaux Segalen | Mauran L.,French National Center for Scientific Research | Mauran L.,UREkA Sarl | Kauffmann B.,University of Bordeaux Segalen | And 6 more authors.
Comptes Rendus Chimie | Year: 2016

Template-based stabilization of α-peptide helices with short accessory non-peptide helical foldamers fused either at the N- or C-terminus or at both ends of the peptide segment has been investigated by NMR spectroscopy in polar solvents and by X-ray diffraction. In this work, we focused on aliphatic N,N′-linked oligoureas that form predictable and well-defined helical structures akin to α-helices. Our results indicate that urea oligomers have the ability to enforce a peptide segment to adopt a well-defined α-helical structure and may suggest a general approach to stabilize short helical peptide epitopes for the development of modulators of protein-protein interactions. © 2015 Académie des sciences.

French National Center for Scientific Research and Ureka Sarl | Date: 2016-06-22

The present description provides oligourea catalysts, a polar helical oligomeric strands, and methods for catalyzing reactions with polar helical oligomeric strands and oligourea catalysts. In particular, the invention relates to a polar helical oligomeric strand of at least 4 residues selected from the formula (I) and which can be used as a catalyst.

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