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Séminaire Chimie IBMM

Constrained amino acids in peptide and peptidomimetic design

Prof. Ém Dirk Tourwé (Organic Chemistry Department, Vrije Universiteit Brussel, Belgium)

publié le

Le Lundi 20 Juin 2016 à 11h
UM Faculté de Pharmacie, amphithéâtre C

Side chain topography of amino acids that are part of a peptide’s pharmacophore represents a crucial structural feature in peptide and peptidomimetic design. Constraining the side chain dihedral angles (χ angles) limits the number of low energy conformations and allows to obtain more potent, receptor subtype selective and enzymatically stable peptide ligands. We will describe this strategy for aromatic amino acids such a Phe, Tyr, Trp and His. The side chains of these residues are incorporated in or mimicked by amino-arylazepinones. A selection of synthetic pathways starting from amino acids that were used by our group to obtain the desired conformationally constrained 4-amino-2-benzazepinones (Aba), the corresponding amino-indolo- and amino-triazoloazepinones (Aia and Ata, respectively) will be discussed. The selected biological applications illustrating the potential of this approach for the development of novel peptide-based pharmacological probes and drug candidates involves somatostatin, angiotensin IV, neurotensin, opioids and hybrid opioid/substance P peptides.

Contact local IBMM : Dr. Florine Cavelier, DR CNRS (DAPP)


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