Author/Authors :
Mario Paglialunga Paradisi، نويسنده , , Adriano Mollica، نويسنده , , Ivana Cacciatore، نويسنده , , Antonio Di Stefano، نويسنده , , Francesco Pinnen، نويسنده , , Anna Maria Caccuri، نويسنده , , Giorgio Ricci، نويسنده , , Silvestro Dupré، نويسنده , , Alessandra Spirito، نويسنده , , Gino Lucente، نويسنده ,
Abstract :
The two novel diastereoisomeric glutathione analogues 1 and 2 have been designed and synthesized by replacing the native γ-glutamylic moiety with the conformational rigid skeleton of cis- or trans-4-carboxy-l-proline residue. Both analogues have been obtained by following the solution phase peptide chemistry methodologies and final reduction of the corresponding disulfide forms 13 and 14. The two analogues 1 and 2 have been tested towards γ-glutamyltranspeptidase (γ-GT) and human glutathione S-transferase (hGST P1-1). Both analogues 1 and 2 are completely resistant to enzymatic degradation by γ-GT. The S-transferase utilizes the analogue 2 as a good substrate while is unable to bind the analogue 1.
