109702-97-8Relevant articles and documents
4-Acylhydrazinomethylene-2-phenyloxazol-5(4H)-ones as acylating agents: Synthesis of salicylanilides and 1,2,4-triazolo[4,3-b] pyridazines
Po?gan, Franc,Polanc, Slovenko,Ko?evar, Marijan
, p. 1011 - 1019 (2007/10/03)
A simple and general method for the acylation of an amino or hydrazino group by the application of hydrazides has been developed. It starts from hydrazides (2), which are converted with 4-ethoxymethylene-2-phenyl-oxazol-5(4H)-one (1) to the corresponding 4-acylhydrazinomethylene-2-phenyloxazol-5(4H)-ones (3). The latter react with nitrogen-containing nucleophiles in 1,4-dioxane in the presence of triethylamine or zirconium(IV) chloride to give the corresponding amides (7) or mixtures of hydrazides (12) and 1,2,4-triazolo[4,3-b]pyridazines (11). Upon prolonged heating, compounds (11) are the main products.
Evaluation and Synthesis of Aminohydroxyisoxazoles and Pyrazoles as Potential Glycine Agonists
Drummond, J.,Johnson, G.,Nickell, D. G.,Ortwine, D. F.,Bruns, R. F.,Welbaum, B.
, p. 2116 - 2128 (2007/10/02)
Except for structurally similar small amino acids, such as alanine, β-alanine, and serine, compounds acting as glycine-receptor agonists are an unknown class of pharmacological agents.To investigate the potential of small, substituted heterocycles to act as glycine agonists, we have evaluated the similarities between glycine and a series of hydroxy- and amino-substituted pyrazoles and isoxazoles through complementary molecular modeling techniques.Using a "scorecard approach" to determine the overall similarity of projected agonist structures to glycine, we prioritized synthesis and subsequently prepared several novel derivatives.The biological activity of these compounds was compared to that of glycine by using a strychnine-mediated glycine receptor binding assay.Despite the close similarity in the calculated parameters when compared to glycine, no significant receptor-binding activity was observed for the targeted analogues.These results illustrate the structurally exacting nature of the glycine receptor.
