N'est plus au Laboratoire.
CALMES Monique
Fonction : directeur de recherche
Thème de Recherche: Synthèses Stéréosélectives & Acides Aminés Modifiés (responsable de)
monique.calmes
univ-montp2.fr
0467144994
Bureau: 0, Bât: 17 - Site : UM campus triolet
Domaines de Recherche: - Chimie/Cristallographie
- Chimie/Chimie organique
- Chimie
- Chimie/ou physique
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Dernieres productions scientifiques :
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Synthesis of Enantiopure 1,2-Diaminobicyclo[2.2.2]octane Derivatives, C 1 -Symmetric Chiral 1,2-Diamines with a Rigid Bicyclic Backbone
Auteur(s): Milbeo P., Moulat L., Didierjean Claude, Aubert Emmanuel, Martinez J., Calmes M.
(Article) Publié:
European Journal Of Organic Chemistry, vol. 82 p.3144 - 3151 (2017)
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N-Pyrrolidine-based alpha/beta-peptides incorporating ABOC, a constrained bicyclic beta-amino acid, for asymmetric aldol reaction catalysis
Auteur(s): Milbeo P., Maurent Kelly, Moulat L., Lebrun A., Didierjean Claude, Aubert Emmanuel, Martinez J., Calmes M.
(Article) Publié:
Tetrahedron / Tetrahedron [London]; Tetrahedron Suppl; Tetrahedron (London), vol. 72 p.1706-1715 (2016)
Ref HAL: hal-01532027_v1
DOI: 10.1016/j.tet.2016.02.027
Résumé: A series of N-pyrrolidine-based alpha,beta-peptide catalysts incorporating a constrained 2-aminobicyclo[2.2.2] octane carboxylic acid (ABOC) residue were synthesized and evaluated in the asymmetric aldol reaction from acetone and some p-substituted benzaldehydes. Their catalytic properties were shown to be highly dependent on the amino acid sequences and on the absolute configuration of the ABOC residue that played a determinant role. Among the peptides tested, the heterochiral tripeptide H-Pro-(R)-ABOC-Asp-OCH3 13, that adopts a turn conformation in the solid state, proved to be the most efficient catalyst affording beta-hydroxy ketones in high yields and good enantioselectivities (up to 87%).
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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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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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Synthesis and analgesic effects of novel 2-tryptophan hexapeptide analogs
Auteur(s): Bocheva Adriana, Nocheva Hristina, Pavlov N., Todorov P., Calmes M., Martinez J., Naydenova Emilia
(Article) Publié:
Amino Acids, vol. 45 p.983-988 (2013)
Ref HAL: hal-00969128_v1
DOI: 10.1007/s00726-013-1555-4
Résumé: Aiming to develop more potent analgesic substances a new series of hexapeptides containing b2-tryptophan analogues was synthesized. The Trp in position 4 and 5, respectively in Ac-Arg-Phe-Met-Trp-Met-Lys-NH2 (opioid receptor antagonist) and Ac-Arg-Tyr-Tyr-Arg-Trp-Lys- NH2 (highly potent and selective NOP-receptor agonist) was substituted by the (S)-2-(1-methyl-1H-indol-3-yl)propionic residue or the (S)-2-(5-methoxy-1H-indol-3-yl)propionic residue. The analgesic effect of the four newly synthesized compounds has been evaluated in male Wistar rats by PPand HP tests and compared to the native templates. Further estimation of the mechanisms of action of each compound was achieved using specific antagonists--naloxone for opioid and JTC801 for the NOP receptor. Replacement of Trp with b2-tryptophan analogues in 4th position (Ac-Arg-Phe-Met-Trp-Met-Lys-NH2) led to increased and longer lasting analgesic effect. The results obtained permit us to assume that both opioid and NOP receptors take part in the newly synthesized compounds analgesic effects.
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