166597-76-8

Upstream product

• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 874-60-2 4-methyl-benzoyl chloride 
• 663923-72-6 (S)-methyl 4-methyl-2-(4-methylbenzamido)pentanoate 

Downstream Products

• 663923-78-2 1-(tert-butyloxycarbonylamino)-3-[N-(4-methylbenzoyl)-L-leucyl-L-prolyl-amino]propane 
• 663923-76-0 N-(4-methylbenzoyl)-L-leucyl-L-proline 
• 663923-74-8 N-(4-methylbenzoyl)-L-leucyl-L-proline methyl ester 

Relevant academic research and scientific papers

Synthesis and Structure-Activity Relationships of Arylsulfonamides as AIMP2-DX2 Inhibitors for the Development of a Novel Anticancer Therapy

AIMP2-DX2, a splicing variant of AIMP2, is up-regulated in lung cancer, possesses oncogenic activity, and results in tumorigenesis. Specifically inhibiting the interaction between AIMP2-DX2 and HSP70 to suppress AIMP2-DX2-dependent cancers with small molecules is considered a promising avenue for cancer therapeutics. Optimization of hit BC-DXI-04 (IC50 = 40.1 μM) provided new potent sulfonamide based AIMP2-DX2 inhibitors. Among these, BC-DXI-843 showed improved inhibition against AIMP2-DX2 (IC50 = 0.92 μM) with more than 100-fold selectivity over AIMP2 in a luciferase assay. Several binding assays indicated that this compound effectively induces cancer cell apoptosis by specifically interrupting the interaction between DX2 and HSP70, which leads to the degradation of DX2 via Siah1-mediated ubiquitination. More importantly, BC-DXI-843 demonstrated in vivo efficacy in a tumor xenograft mouse model (H460 cells) at a dosage of 50 mg/kg, suggesting it as a promising lead for development of novel therapeutics targeting AIMP2-DX2 in lung cancer.

New cyanopeptide-derived low molecular weight inhibitors of trypsin-like serine proteases

This paper deals with the design, syntheses, and inhibition tests of new low molecular weight thrombin inhibitors utilizing cyanopeptides, the secondary metabolites of cyanobacteria with interesting biological activities, as new lead structures. Starting with aeruginosin 98-B (1) as a lead structure, we have developed and synthesised new, selective acting inhibitors of serine proteases (RA-1005 and RA-1009), which are suitable targets for further structure-activity studies.