586396-26-1Relevant articles and documents
Proline-glutamate chimeras in isopeptides. Synthesis and biological evaluation of conformationally restricted glutathione analogues
Paradisi, Mario Paglialunga,Mollica, Adriano,Cacciatore, Ivana,Di Stefano, Antonio,Pinnen, Francesco,Caccuri, Anna Maria,Ricci, Giorgio,Dupre, Silvestro,Spirito, Alessandra,Lucente, Gino
, p. 1677 - 1683 (2003)
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.
Pyrrolidine compounds
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Page/Page column 6, (2010/11/26)
A compound of the following formula: wherein R1, R2, R3, R4, R5, R6, R7, R8, T, X, Y, and Z are as defined herein. Also disclosed is a method for inhibiting dipeptidyl