23806-63-5

Upstream product

• 303-38-8 2,3-Dihydroxybenzoic acid 
• 100-39-0 benzyl bromide 
• 24677-78-9 2,3-dihydroxybenzaldehyde 
• 5779-91-9 2,3-bis(benzyloxy)benzaldehyde 
• 86734-59-0 3-benzyloxy-2-hydroxybenzaldehyde 
• 74272-78-9 2,3-dibenzyloxybenzoic acid 
• 2169-27-9 Methyl 2,3-bis(benzyloxy)benzoate 
• 2411-83-8 methyl-2,3-dihydroxybenzoate 
• 124-38-9 carbon dioxide 

Downstream Products

• 303-38-8 2,3-Dihydroxybenzoic acid 
• 1332325-05-9 3-(benzyloxy)-N-(4-fluorobenzyl)-2-hydroxybenzamide 
• 26486-92-0 6-deoxyisojacareubin 
• 2169-23-5 methyl 3-(benzyloxy)-2-hydroxybenzoate 
• 77376-43-3 3-benzyloxy-2-(9-hydroxy-5-oxononyloxy)benzoic acid lactone 

Relevant academic research and scientific papers

Design of a Functional Chromene-Type Kobayashi Precursor: Gram-Scale Total Synthesis of Natural Xanthones by Highly Regioselective Aryne Annulation

The 2,2-dimethyl-2H-chromene motif is widely found in many bioactive molecules, and is a privileged structure in the pharmaceutical arena. We have developed a concise and regioselective approach to chromenes and chromanes through an aryne-based synthetic

DOUBLE-HEADED PROTEASE INHIBITOR

The present invention provides a compound that is highly safe and useful in the prevention, alleviation, and/or treatment of various diseases involving enteropeptidase inhibition and/or trypsin inhibition, a pharmaceutical composition containing the compo

CONDENSED HETEROCYCLIC COMPOUND

The present invention relates to a condensed heterocyclic compound that has an enteropeptidase inhibitory effect and is useful in the treatment or prevention of obesity, diabetes mellitus, or the like, and a medicament containing the same. Specifically, t

Design of HIV-1 integrase inhibitors targeting the catalytic domain as well as its interaction with LEDGF/p75: A scaffold hopping approach using salicylate and catechol groups

HIV-1 integrase (IN) is a validated therapeutic target for antiviral drug design. However, the emergence of viral strains resistant to clinically studied IN inhibitors demands the discovery of novel inhibitors that are structurally as well mechanistically different. Herein, we describe the design and discovery of novel IN inhibitors targeting the catalytic domain as well as its interaction with LEDGF/p75, which is essential for the HIV-1 integration as an IN cofactor. By merging the pharmacophores of salicylate and catechol, the 2,3-dihydroxybenzamide (5a) was identified as a new scaffold to inhibit the strand transfer reaction efficiently. Further structural modifications on the 2,3-dihydroxybenzamide scaffold revealed that the heteroaromatic functionality attached on the carboxamide portion and the piperidin-1-ylsulfonyl substituted at the phenyl ring are beneficial for the activity, resulting in a low micromolar IN inhibitor (5p, IC50 = 5 μM) with more than 40-fold selectivity for the strand transfer over the 3′-processing reaction. More significantly, this active scaffold remarkably inhibited the interaction between IN and LEDGF/p75 cofactor. The prototype example, N-(cyclohexylmethyl)-2,3- dihydroxy-5-(piperidin-1-ylsulfonyl) benzamide (5u) inhibited the IN-LEDGF/p75 interaction with an IC50 value of 8 μM. Using molecular modeling, the mechanism of action was hypothesized to involve the chelation of the divalent metal ions inside the IN active site. Furthermore, the inhibitor of IN-LEDGF/p75 interaction was properly bound to the LEDGF/p75 binding site on IN. This work provides a new and efficient approach to evolve novel HIV-1 IN inhibitors from rational integration and optimization of previously reported inhibitors.