1283116-72-2

Upstream product

• 100-46-9 benzylamine 
• 66866-44-2 Boc-Leu-O-COO-isoBu 
• 60-18-4 L-tyrosine 
• 856794-72-4 2-bromo-4-nitrobenzoyl chloride 
• 16426-64-5 2-bromo-4-nitrobenzoic acid 
• 42406-77-9 L-tyrosine benzyl ester 
• 619-65-8 4-cyanobenzoic Acid 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 1283116-60-8 N-benzyl-2-bromo-4-((S)-2-((S)-2-(4-cyanobenzamido)-3-(4-hydroxyphenyl)propanamido)-4-methylpentanamido)-benzamide 
• 150255-96-2 (3‐cyanophenyl)boronic acid 
• 1283116-58-4 (S)-2-(4-cyanobenzamido)-3-(4-hydroxyphenyl)propanoic acid 
• 1283116-57-3 (S)-benzyl 2-(4-cyanobenzamido)-3-(4-hydroxyphenyl)-propanoate 
• 1283116-55-1 (S)-4-(2-amino-4-methylpentanamido)-N-benzyl-2-bromobenzamide 
• 1283116-53-9 4-amino-N-benzyl-2-bromobenzamide 

Downstream Products

• 1283116-42-6 4-((S)-3-(((S)-1-((6-(benzylcarbamoyl)-3'-cyano-[1,1'-biphenyl]-3-yl)amino)-4-methyl-1-oxopentan-2-yl)amino)-2-(4-cyanobenzamido)-3-oxopropyl)phenyl dihydrogenphosphate 
• 1283116-90-4 4-((S)-3-(((S)-1-((6-(benzylcarbamoyl)-3'-cyano-[1,1'-biphenyl]-3-yl)amino)-4-methyl-1-oxopentan-2-yl)amino)-2-(4-cyanobenzamido)-3-oxopropyl)phenyl N,N,N',N'-tetramethylphosphordiamidate 

Relevant academic research and scientific papers

Design, synthesis and in vitro characterization of novel hybrid peptidomimetic inhibitors of STAT3 protein

Aberrant activation of oncogenic signal transducer and activator of transcription 3 (STAT3) protein signaling pathways has been extensively implicated in human cancers. Given STAT3's prominent dysregulatory role in malignant transformation and tumorigenesis, there has been a significant effort to discover STAT3-specific inhibitors as chemical probes for defining the aberrant STAT3-mediated molecular events that support the malignant phenotype. To identify novel, STAT3-selective inhibitors suitable for interrogating STAT3 signaling in tumor cells, we explored the design of hybrid molecules by conjugating a known STAT3 inhibitory peptidomimetic, ISS610 to the high-affinity STAT3-binding peptide motif derived from the ILR/gp-130. Several hybrid molecules were examined in in vitro biophysical and biochemical studies for inhibitory potency against STAT3. Lead inhibitor 14aa was shown to strongly bind to STAT3 (KD = 900 nM), disrupt STAT3:phosphopeptide complexes (Ki = 5 μM) and suppress STAT3 activity in in vitro DNA binding activity/electrophoretic mobility shift assay (EMSA). Moreover, lead STAT3 inhibitor 14aa induced a time-dependent inhibition of constitutive STAT3 activation in v-Src transformed mouse fibroblasts (NIH3T3/v-Src), with 80% suppression of constitutively-active STAT3 at 6 h following treatment of NIH3T3/v-Src. However, STAT3 activity recovered at 24 h after treatment of cells, suggesting potential degradation of the compound. Results further showed a suppression of aberrant STAT3 activity in NIH3T3/v-Src by the treatment with compound 14aa-OH, which is the non-pTyr version of compound 14aa. The effect of compounds 14aa and 14aa-OH are accompanied by a moderate loss of cell viability.