Isosteric exchange of the acylsulfonamide moiety in Abbott’s Bcl-X(L) protein interaction antagonis

June 29th, 2008 | by admin |

Isosteric exchange of the acylsulfonamide moiety in Abbott\’s Bcl-X(L) protein interaction antagonist.

A multi-component reaction strategy was used for the fast and efficient synthesis of amide isosteres of known Bcl-2 inhibitors capable of disrupting protein-protein interactions. Ugi reaction and a subsequent nucleophilic aromatic substitution reaction provide a versatile path to libraries of compounds similar to Abbott\’s acylsulfonamides. Modeling arguments are used to explain the inferior activity of the amide as opposed to the sulfonamide series.

Dömling A, Antuch W, Beck B, Schauer-Vukašinović V.

Department of Pharmaceutical Sciences, University of Pittsburgh, PA 15261, USA; Department of Chemistry, University of Pittsburgh, PA 15261, USA; Morphochem AG, Gmunderstrasse 37–37a, 81379 München, Germany.

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