1037593-63-7

Upstream product

• 27894-50-4 methyl (2S)-2-amino-6-{[(benzyloxy)carbonyl]amino}hexanoate hydrochloride 
• 89-75-8 2,4-dichlorobenzoyl chloride 
• 501-53-1 benzyl chloroformate 
• 47115-81-1 Cu(lysinate)2 
• 42893-94-7 Cu(Nε-benzyloxy carbonyl-lysinate)2 
• 1155-64-2 N₆-[(benzyloxy)carbonyl]-L-lysine 
• 50-84-0 2,4 dichlorobenzoic acid 

Downstream Products

• 1037593-41-1 C₂₁H₂₂Cl₂N₂O₅ 
• 1037593-51-3 C₂₁H₂₃Cl₂N₃O₅ 

Relevant academic research and scientific papers

Novel aminopeptidase N inhibitors with improved antitumor activities

A series of aminopeptidase N (APN) inhibitors were designed and synthesized. Enzyme inhibitory, docking and antiproliferative studies were performed to evaluate the derived molecules. Molecule D15, with IC50 values of 10.9 μM, showed the best performance in the APN enzymatic inhibition assay. The binding pattern of molecule D9 and D15 in the active site of APN was predicted by docking studies. Hydrophobic and H-bond interactions were discovered to make key roles in the ligand-receptor bindings. Compared with the previous C7, several molecules such as D9, D14 and D15, exhibited significantly improved activities in inhibiting the growth of HL-60, ES-2, A549 and PLC cell lines.

Design, synthesis, and QSAR studies of novel lysine derives as amino-peptidase N/CD13 inhibitors

A series of novel l-lysine derivatives were designed, synthesized, and assayed for their inhibitory activities on amino-peptidase N (APN)/CD13 and matrix metalloproteinase-2 (MMP-2). The preliminary biological test showed that most of the compounds displayed a high inhibitory activity against MMP-2 and a low activity against APN except compound B6 which exhibited good potency (IC50 = 13.2 μM) similar with APN inhibitor Bestatin (IC50=15.5 μM), and could be used as lead compound in the future.