AMBLARD Muriel
Fonction : Directeur de recherche
Thème de Recherche: Chimie des Acides Aminés, Peptides, Hétérocycles, Chimie Sup (responsable de)
muriel.amblard
umontpellier.fr
0448792182
Bureau: N3H02, Etg: 3 - Site : Pôle Chimie Balard Recherche
Domaines de Recherche: - Chimie/Matériaux
- Chimie/ou physique
- Chimie/Cristallographie
- Chimie/Chimie organique
- Chimie/Polymères
- Chimie
- Sciences du Vivant/Biologie cellulaire
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Dernieres productions scientifiques :
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Site-specific grafting on titanium surfaces with hybrid temporin antibacterial peptides
Auteur(s): Masurier N., Tissot Jean-Baptiste, Boukhriss Douae, Jebors S., Pinese C., Verdie P., Amblard M., Mehdi Ahmad, Martinez J., Humblot Vincent, Subra G.
(Article) Publié:
Journal Of Materials Chemistry B, vol. 6 p.1782 - 1790 (2018)
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12/14/14-Helix Formation in 2:1 alpha/beta-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints
Auteur(s): Legrand B., Andre C., Moulat L., Didierjean Claude, Hermet Patrick, Bantignies Jean-Louis, Martinez J., Amblard M., Calmes M.
(Article) Publié:
Chemistry - A European Journal, vol. 22 p.11986-11990 (2016)
Ref HAL: hal-01368422_v1
DOI: 10.1002/chem.201602746
Résumé: The highly constrained b-amino acid ABOC induces different types of helices in b urea and 1:1 a/b amide oligomers. The latter can adopt 11/9- and 18/16-helical folds depending on the chain length in solution. Short peptides alternating proteinogenic a-amino acids and ABOC in a 2:1 a/b repeat pattern adopted an unprecedented and stable 12/14/14-helix. The structure was established through extensive NMR, molecular dynamics, and IR studies. While the 1:1 a-AA/ABOC helices diverged from the canonical a-helix, the helix formed by the 9-mer 2:1 a/b-peptide allowed the projection of the a-aminoacid side chains in a spatial arrangement according to the a-helix. Such a finding constitutes an important step toward the conception of functional tools that use the ABOC residue as a potent helix inducer for biological applications.
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Selective homodimerization of unprotected peptides using hybrid hydroxydimethylsilane derivatives
Auteur(s): Echalier C., Kalistratova A., Ciccione J., Lebrun A., Legrand B., Naydenova Emilia, Gagne D., Fehrentz J.-A., Marie J., Amblard M., Mehdi Ahmad, Martinez J., Subra G.
(Article) Publié:
Rsc Advances, vol. p. (2016)
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Crystal structure of Boc-(S)-ABOC-(S)-Ala-(S)ABOC-(S)-Phe-OBn chloroform monosolvate
Auteur(s): Wenger Emmanuel, Moulat L., Legrand B., Amblard M., Calmes M., Didierjean Claude
(Article) Publié:
Acta Crystallographica. Section E, Crystallographic Communications, vol. 71 p.1193+ (2015)
Ref HAL: hal-01521800_v1
DOI: 10.1107/S2056989015016941
Résumé: In the title compound, phenyl (S)-2-[(S)-(1-\2-[(S)-(1-\[(tert-butoxy)carbonyl]amino\bicycloĂ [2.2.2]octan-2-yl)formamido]propanamido\bicyclo[2.2.2]octan-2-yl)for mamido]-3-phenylpropanoate chloroform monosolvate, C42H56N4O7-CHCl3, the alpha,beta-hybrid peptide contains two non-proteinogenic amino acid residues of (S)-1-aminobicyclo[2.2.2]octane-2-carboxylic acid [(S)-ABOC], two amino acid residues of (S)-2-aminopropanoic acid [(S)-Ala] and (S)-2-amino-3-phenylpropanoic acid [(S)-Phe], and protecting groups of tert-butoxycarbonyl (Boc) and benzyl ester (OBn). The tetramer folds into a right-handed mixed 11/9 helix stabilized by intramolecular i, i +3 and i, i-1 C=O center dot center dot center dot H-N hydrogen bonds. In the crystal, the oligomers are linked by N-H center dot center dot center dot O=C hydrogen bonds into chains along the a-axis direction. The chloroform solvent molecules are intercalated between the folded chains via C-H center dot center dot center dot O=C interactions.
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Unprecedented Chain-Length-Dependent Conformational Conversion Between 11/9 and 18/16 Helix in α/β-Hybrid Peptides.
Auteur(s): Amblard M.
(Article) Publié:
Angewandte Chemie International Edition, vol. 53 p.13131–13135 (2014)
Ref HAL: hal-01095670_v1
DOI: 10.1002/anie.201407329
Résumé: α,β-Hybrid oligomers of varying lengths with alternating proteogenic α-amino acid and the rigid β2,3,3-trisubstituted bicyclic amino acid ABOC residues were studied using both X-ray crystal and NMR solution structures. While only an 11/9 helix was obtained in the solid state regardless of the length of the oligomers, conformational polymorphism as a chain-length-dependent phenomenon was observed in solution. Consistent with DFT calculations, we established that short oligomers adopted an 11/9 helix, whereas an 18/16 helix was favored for longer oligomers in solution. A rapid interconversion between the 11/9 helix and the 18/16 helix occurred for oligomers of intermediate length.
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