16281-60-0Relevant academic research and scientific papers
Synthesis, spectroscopic evaluation, molecular modelling, thermal study and biological evaluation of manganese(II) complexes derived from bidentate N,O and N,S donor Schiff base ligands
Bargujar, Savita,Chandra, Sulekh,Chauhan, Reeta,Rajor, Hament K.,Bhardwaj, Jyoti
, (2018)
Manganese(II) complexes having the general composition Mn(L)2X2 (where L?=?3-bromoacetophenone semicarbazone, 3-bromoacetophenone thiosemicarbazone, 1-tetralone semicarbazone, 1-tetralone thiosemicarbazone, flavanone semicarbazone or
Small-molecule inhibitors of cathepsin L incorporating functionalized ring-fused molecular frameworks
Song, Jiangli,Jones, Lindsay M.,Chavarria, Gustavo E.,Charlton-Sevcik, Amanda K.,Jantz, Adam,Johansen, Audra,Bayeh, Liela,Soeung, Victoria,Snyder, Lindsey K.,Lade Jr., Shawn D.,Chaplin, David J.,Trawick, Mary Lynn,Pinney, Kevin G.
supporting information, p. 2801 - 2807 (2013/06/27)
Cathepsin L is a cysteine protease that is upregulated in a variety of malignant tumors and plays a significant role in cancer cell invasion and migration. It is an attractive target for the development of small-molecule inhibitors, which may prove beneficial as treatment agents to limit or arrest cancer metastasis. We have previously identified a structurally diverse series of thiosemicarbazone-based inhibitors that incorporate the benzophenone and thiochromanone molecular scaffolds. Herein we report an important extension of this work designed to explore fused aryl-alkyl ring molecular systems that feature nitrogen atom incorporation (dihydroquinoline-based) and carbon atom exclusivity (tetrahydronaphthalene-based). In addition, analogues that contain oxygen (chromanone-based), sulfur (thiochroman-based), sulfoxide, and sulfone functionalization have been prepared in order to further investigate the structure-activity relationship aspects associated with these compounds and their ability to inhibit cathepsins L and B. From this small-library of 30 compounds, five were found to be strongly inhibitory (IC50 50 = 164 nM. All of the compounds evaluated were inactive (IC50 >10,000 nM) as inhibitors of cathepsin B, thus establishing a high degree (>20-fold) of selectivity (cathepsin L vs. cathepsin B) for the most active cathepsin L inhibitors in this series.
