92900-78-2Relevant academic research and scientific papers
2-(β-Arylethylamino)- and 4-(β-Arylethylamino)quinazolines as Phosphodiesterase Inhibitors
Millen, J.,Riley, T. N.,Waters, I. W.,Hamrick, M. E.
, p. 12 - 17 (1985)
The existence of several forms of cAMP phosphodiesterase having different kinetic characteristics suggests the feasibility of developing tissue-selective inhibitors of this enzyme.This observation is of particular importance in the development of therapeutic agents for the management of reversible obstructive airways disorders.The present report describes the design, synthesis and pharmacological characterization of a series of 6,7-dimethoxyquinazoline derivatives having β-arylethylamine substituents at the 2- or 4- positions.The quinazoline nucleus is intended to confer a high degree of inhibitory activity for phosphodiesterase while the β-arylethylamine moieties are designed to provide selectivity for adrenergically innervated tissue.The target compounds of this study, 6 and 7 were prepared via β-arylethylamine displacement of chloride from an appropriate chloroquinazoline intermediate.The resulting products were evaluated for their ability to relax guinea pig tracheal smooth muscle and as inhibitors of phosphodiesterase.
Molecular features of the prazosin molecule required for activation of Transport-P
da Silva, Joaquim Fernando Mendes,Walters, Marcus,Al-Damluji, Saad,Ganellin, C. Robin
, p. 7254 - 7263 (2008/12/23)
Closely related structural analogues of prazosin have been synthesised and tested for inhibition and activation of Transport-P in order to identify the structural features of the prazosin molecule that appear to be necessary for activation of Transport-P. So far, all the compounds tested are less active than prazosin. It is shown that the structure of prazosin appears to be very specific for the activation. Only quinazolines have been found to activate, and the presence of the 6,7-dimethoxy and 4-amino groups appears to be critically important.
