1573010-11-3

Upstream product

• 95-01-2 2,4-Dihydroxybenzaldehyde 
• 69019-75-6 3-acetamido-2-oxo-2H-chromen-7-yl acetate 
• 100-39-0 benzyl bromide 
• 1573010-09-9 N-(7-(benzyloxy)-2-oxo-2H-chromen-3-yl)acetamide 

Downstream Products

• 1630958-13-2 C₁₆H₁₁FO₃ 
• 79418-41-0 3-amino-7-hydroxy-2H-chromen-2-one 

Relevant academic research and scientific papers

Novobiocin–ferrocene conjugates possessing anticancer and antiplasmodial activity independent of HSP90 inhibition

Abstract: A series of tailored novobiocin–ferrocene conjugates was prepared in moderate yields and investigated for in vitro anticancer and antiplasmodial activity against the MDA-MB-231 breast cancer line and Plasmodium falciparum 3D7 strain, respectively. While the target compounds displayed moderate anticancer activity against the breast cancer cell line with IC50 values in the mid-micromolar range, compounds 10a–c displayed promising antiplasmodial activity as low as 0.889?μM. Furthermore, the most promising compounds were tested for inhibitory effects against a postulated target, heat shock protein 90 (Hsp90). Graphical abstract: A selection of tailored novobiocin derivatives bearing the organometallic ferrocene unit were synthesized and characterized by common spectroscopic techniques. The target compounds were investigated for in vitro anticancer and antimalarial activity against the MDA-MB-231 breast cancer cell line and Plasmodium falciparum 3D7 strain, respectively.[Figure not available: see fulltext.].

Defining a minimum pharmacophore for simocyclinone D8 disruption of DNA gyrase binding to DNA

The increasing occurrence of drug-resistant bacterial infections in the clinic has created a need for new antibacterial agents. Natural products have historically been a rich source of both antibiotics and lead compounds for new antibacterial agents. The natural product simocyclinone D8 (SD8) has been reported to inhibit DNA gyrase, a validated antibacterial drug target, by a unique catalytic inhibition mechanism of action. In this work, we have used a deconstruction-reconstruction approach to prepare analogs of the coumarin subunit of SD8 and evaluated their ability to disrupt binding of the DNA gyrase enzyme to DNA in a surface plasmon resonance assay. This has led to a minimum pharmacophore required for disruption of binding. Springer Science+Business Media 2014.