Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Laura Mauran"'
Autor:
Juliette Fremaux, Claire Venin, Laura Mauran, Robert H. Zimmer, Gilles Guichard, Sébastien R. Goudreau
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
The peptide hormone GLP-1 has the potential to be a remedy for diabetes type II, yet is unstable. Here, the authors synthesized α-peptide-oligourea hybrid analogues of GLP-1 some of which showing significantly prolonged activity in vivo.
Externí odkaz:
https://doaj.org/article/7e2c09e5f5e9452e9f698d011ed0817b
Autor:
Maxime Neuville, Sébastien R. Goudreau, Juliette Fremaux, Laura Mauran-Ambrosino, Sébastien Fribourg, Anna Y. Belorusova, Christel Dolain, Judit Osz, Natacha Rochel, Gilles Guichard, Léonie Cussol, Jérémie Buratto
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202008992⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202008992⟩
Efficient optimization of a peptide lead into a drug candidate frequently needs further transformation to augment properties such as bioavailability. Among the different options, foldamers, which are sequence-based oligomers with precise folded confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cadec756596d26e4291809b6b810b3a
http://hdl.handle.net/20.500.12278/106475
http://hdl.handle.net/20.500.12278/106475
Autor:
Claire Venin, Robert H. Zimmer, Ben Jones, Laura Mauran, Stavroula Bitsi, Alejandra Tomas, Didier Rognan, Florian Koensgen, Gilles Guichard, Sébastien R. Goudreau, Maria Lucey, Juliette Fremaux
Publikováno v:
Chemical Science
Chemical Science, The Royal Society of Chemistry, 2019, 10 (42), pp.9872-9879. ⟨10.1039/c9sc02079a⟩
Chemical Science, The Royal Society of Chemistry, 2019, 10 (42), pp.9872-9879. ⟨10.1039/C9SC02079A⟩
Chemical Science, The Royal Society of Chemistry, 2019, 10 (42), pp.9872-9879. ⟨10.1039/c9sc02079a⟩
Chemical Science, The Royal Society of Chemistry, 2019, 10 (42), pp.9872-9879. ⟨10.1039/C9SC02079A⟩
International audience; The high demand of the pharmaceutical industry for new modalities to address the diversification of biological targets with large surfaces of interaction led us to investigate the replacement of alpha-amino acid residues with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa0810e201c5d94816890ca7af7126b
http://hdl.handle.net/20.500.12278/7639
http://hdl.handle.net/20.500.12278/7639
Publikováno v:
ChemPlusChem. 85:2210-2210
Autor:
Gilles Guichard, Caterina Lombardo, Cameron D. Mackereth, Frédéric Rosu, Olivier Lambert, Laura Mauran, Juliette Fremaux, Marion Decossas, Valérie Gabelica, Gavin W. Collie, Karolina Pulka-Ziach
Publikováno v:
Nature Chemistry. 7:871-878
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c90378624c49709e84e634ee99d144ff
http://hdl.handle.net/20.500.12278/10840
http://hdl.handle.net/20.500.12278/10840
Autor:
Gilles Guichard, Brice Kauffmann, Benoit Odaert, Laura Mauran, Juliette Fremaux, Karolina Pulka-Ziach
Publikováno v:
Angewandte Chemie (International ed. in English). 54(34)
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 foldamer