586396-32-9

Upstream product

• 586396-30-7 (2S,4R)-4-[(R)-2-(Acetylamino-methylsulfanyl)-1-(methoxycarbonylmethyl-carbamoyl)-ethylcarbamoyl]-pyrrolidine-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 586396-27-2 trans-N-(benzyloxycarbonyl)-4-carboxy-L-proline methyl ester 
• 130830-70-5 N-(benzyloxycarbonyl)-trans-4-carboxy-L-proline dimethyl ester 

Downstream Products

• 586396-34-1 C₃₈H₄₄N₆O₁₆S₂ 

Relevant academic research and scientific papers

Proline-glutamate chimeras in isopeptides. Synthesis and biological evaluation of conformationally restricted glutathione analogues

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.