High impact information on Azidoprazosin

• Photolabelling experiments indicate that Mdr3 synthesized in yeast cells binds the drug analog [125I]iodoaryl azidoprazosin, this binding being competed for by vinblastine and tetraphenylphosphonium bromide, two known multidrug resistance drugs [1].
• These effects were observed for ST concentrations much lower than those required to displace the P-gp-binding probe azidoprazosin, suggesting that ST might act through its PKC inhibitory effect and not through P-gp binding [2].

Biological context of Azidoprazosin

• The [125I]iodoaryl azidoprazosin photoaffinity drug binding sites in P-glycoprotein have been mapped by immunological analysis [3].
• The phenotype was associated with an impaired ability to photoaffinity label the chimeric P-glycoprotein with [125I]iodoaryl azidoprazosin [4].

Associations of Azidoprazosin with other chemical compounds

• Despite its specific interaction with P-glycoprotein, neither iodoaryl azidoprazosin nor prazosin markedly reversed resistance compared with verapamil or azidopine [5].
• Protease digestion of [125I]ASA-BZ photoaffinity labelled P-glycoprotein yielded two peptides that were similar to those obtained with other P-glycoprotein-associated drugs, e.g. azidopine and iodoaryl azidoprazosin [6].
• P-glycoprotein of MBEC4 specifically bound [125I]iodoaryl azidoprazosin, and the binding was inhibited by cyclosporin A and vincristine [7].

Analytical, diagnostic and therapeutic context of Azidoprazosin

• Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12 [3].

References