1620488-63-2

Upstream product

• 3545-80-0 hydroxyiminoacetic acid 
• 1620488-61-0 3-azido-1-phenylpropylamine 
• 1620488-67-6 C₁₅H₂₁N₅O₄ 
• 1620488-58-5 tert-butyl (3-azido-1-phenylpropyl)carbamate 
• 218449-48-0 (3-hydroxy-1-phenylpropyl)carbamate tert-butyl ester 
• 91230-12-5 (1-phenyl-allyl)-carbamic acid tert-butyl ester 
• 31767-14-3 ethyl 2-(hydroxyimino)acetate 
• 4393-21-9 1-(phenyl)allylamine 
• 1630028-91-9 C₆H₁₁NO₅*C₉H₁₂N₄ 

Relevant academic research and scientific papers

Design and synthesis of N-substituted-2-hydroxyiminoacetamides and interactions with cholinesterases

Within this study, we designed and synthesized four new oxime compounds of the N-substituted 2-hydroxyiminoacetamide structure and evaluated their interactions with acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Our aim was to explore the possibility of extending the dual-binding mode of interaction between the enzyme and the inhibitor to a so-called triple-binding mode of interaction through the introduction of an additional binding moiety. N-substituted 2-hydroxyiminoacetamide 1 was prepared via BOP catalyzed amidation of hydroxyiminoacetic acid with 3-azido-1-phenylpropylamine. An azide group enabled us to prepare more elaborate structures 2–4 by the copper-catalyzed azide-alkyne cycloaddition. The new compounds 1–4 differed in their presumed AChE peripheral site binding moiety, which ranged from an azide group to functionalized heterocycles. Molecular docking studies revealed that all three binding moieties are involved in the non-covalent interactions with ChEs for all of the four compounds, albeit not always in the complete accordance with the proposed hypothesis. All of the four compounds reversibly inhibited the ChEs with their inhibition potency increasing in the same order for both enzymes (1?A higher preference for binding to BChE (KI from 0.30?μmol/L to 130?μmol/L) over AChE (KI from 50?μmol/L to 1200?μmol/L) was observed for all of the compounds. Compounds were screened for reactivation of cyclosarin-, sarin- and VX-inhibited AChE and BChE.

Enzyme-catalyzed cascade synthesis of hydroxyiminoacetamides

In order to synthesize N-(3-azido-1-phenylpropyl)-2-hydroxyiminoacetamide, a key compound for the preparation of acetylcholinesterase (AChE) reactivators of the N-substituted 2-hydroxyiminoacetamide type, it was necessary to develop a method for forming a