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Séminaire Chimie ED459

Conformationally preorganized peptidomimetics : controlling shape and function with azepinone scaffolds

Prof Steven Ballet (Department of Chemistry, Vrije Universiteit Brussel, Belgium)

publié le , mis à jour le

Le Jeudi 18 décembre 2014 à 14h
UM1 Faculté de Pharmacie, amphithéâtre D

Classic disadvantages of peptides as therapeutic agents include poor metabolic stability due to proteolytic degradation, rapid excretion through liver and kidneys, limited bioavailability, etc. These inherent properties of peptides are caused by a high conformational freedom and reduced membrane permeability. To counter these limitations, and to enhance receptor selectivity and metabolic stability, constrained amino acids can be employed. The benzazepinone scaffold 1 (Aba) mimics natural amino acids, such as Phe and Tyr. By limiting their χ1 space, the biologically active conformation is fixed. Similarly, indolo-azepinone 2 (Aia) provides a constrained Trp template and triazolo-diazepinone 3 (Ata) a constrained His template.

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Scheme 1

The introduction of 1 to 3 into biologically active peptides and its use as a privileged template will be discussed. Moreover, the biological evaluation of azepinone-containing peptides, the synthetic routes to obtain substituted benzo-, triazole- and indolo-azepinones and the influence of ring substitution on the conformation and β-turn mimicry of azepinone peptidomimetics will be presented.

Contact local IBMM : Dr. Florine Cavelier D.R. CNRS, Prof. Gilles Subra (DAPP)


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