301196-52-1

Upstream product

• 531-81-7 2-oxo-2H-chromene-3-carboxylic acid 
• 98-16-8 3-trifluoromethylaniline 
• 90-02-8 salicylaldehyde 
• 93887-31-1 2-oxochroman-3-carboxylic acid 
• 1846-76-0 ethyl coumarin-3-carboxylate 
• 529-20-4 2-methylphenyl aldehyde 
• 161885-45-6 C₁₀H₇ClO₃ 
• 3757-06-0 coumarin 3-carboxylic acid chloride 

Relevant academic research and scientific papers

Design, synthesis and in vitro evaluation of 2-oxo-n-substituted phenyl-2h-chromene-3-carboxamide derivatives as HIV integrase strand transfer inhibitors

Background: A series of eighteen 2-Oxo-N-substituted phenyl-2H-chromene-3-carboxamide analogues has been evaluated for HIV-1 integrase (IN) inhibition. Methods: The derivatives were synthesized via a two-step pathway commencing with 2-hydroxybenzaldehyde and diethyl malonate followed by hydrolysis of ester and coupling with various aromatic amines. The HIV-1 IN inhibitory potential of these compounds has been studied relative to dolutegravir, a known HIV-1 IN inhibitor using a standard available kit. Results: Six molecules (compounds 13h, 13i, 13l, 13p to 13r) showed significant inhibition of HIV-1 integrase 3′-strand transfer with IC50 values less than 1.7 μM. The presence of chromene-3-carboxamide motif was shown to be crucial for the enzymatic activity. In addition, molecular modelling studies were also done to justify the IN inhibition and in vitro-in silico correlation was drawn. Conclusion: However, these compounds did not show HIV-1 and HIV-2 inhibition below their cytotoxic concentration indicating that these compounds cannot be taken further for anti-HIV activity as such and require structural modification.

New 2H-chromene-3-carboxamide derivatives: Design, synthesis and use as inhibitors of hMAO

A series new 2H-chromene-3-carboxamide derivatives 4a-4t were synthesized and evaluated as monoamine oxidase A and B (MAO-A and MAO-B) inhibitors. Among them, compound 4d (IC50 = 0.93 μM, IC50 iproniazid = 7.80 μM) showed the most ac

Synthesis, molecular modeling, and selective inhibitory activity against human monoamine oxidases of 3-carboxamido-7-substituted coumarins

A large series of 3-carboxamido-7-substituted coumarins have been synthesized and tested in vitro for their human monoamine oxidase A and B (hMAO-A and hMAO-B) inhibitory activity. Taking into account all the relevant structural information on MAOs reported in the literature, we made some changes in the coumarin nucleus and examined with particular attention the effect on activity and selectivity of substituting at position 3 with N-aryl or N-alkyl carboxamide and at position 7 with a benzyloxy or a 4'-F-benzyloxy group. Some of the assayed compounds proved to be potent, selective inhibitors of hMAO-B with IC50 values in the micromolar range. To better understand the enzyme-inhibitor interaction and to explain the selectivity of the most active compounds toward hMAOs, molecular modeling studies were carried out on new, high resolution, hMAO-A and hMAO-B crystallographic structures. ?2009 American Chemical Society.