Guevara Elmer A C, de Lourdes Barriviera Maria, Hassón-Voloch Aída, Louro Sonia R W
Department of Physics, Pontifícia Universidade Católica do Rio de Janeiro, Rio de Janeiro, Brazil.
Photochem Photobiol. 2007 Jul-Aug;83(4):914-9. doi: 10.1111/j.1751-1097.2007.00077.x.
This work reports the results of ultraviolet irradiation on the interaction of the phototoxic antipsychotic drug chlorpromazine (CPZ) with the sodium pump Na+, K+-ATPase. The study was performed by monitoring the fluorescence modifications of CPZ itself and of the specific probe anthroylouabain (AO). CPZ association with Na+, K+-ATPase was found to modify the kinetics of CPZ-photodegradation. It was demonstrated that UV irradiation produces a stable fluorescent photoproduct of CPZ covalently bound to Na+, K+-ATPase. The fluorescent probe AO, which specifically binds to the extracellular ouabain site of the pump, was used to localize the CPZ binding site. UV-irradiation of AO-labeled Na+, K+-ATPase treated with CPZ at concentration about 20 microM produced dose-dependent modifications of the AO fluorescence, e.g. increased quantum yield and blue shift. The results demonstrated that CPZ binds near the ouabain site. The photo-induced reaction of CPZ with AO-labeled Na+, K+-ATPase protected the ouabain site from the aqueous environment. It was also found that UV irradiation of CPZ-treated enzyme obstructs the binding of AO, which suggested occlusion of the ouabain site. This effect can be evaluated for a potential use of CPZ in photochemotherapy.
这项工作报告了紫外线照射对光毒性抗精神病药物氯丙嗪(CPZ)与钠泵Na +,K + -ATP酶相互作用的影响。该研究通过监测CPZ本身以及特异性探针蒽基哇巴因(AO)的荧光变化来进行。发现CPZ与Na +,K + -ATP酶的结合改变了CPZ光降解的动力学。结果表明,紫外线照射产生了一种与Na +,K + -ATP酶共价结合的稳定的CPZ荧光光产物。特异性结合泵细胞外哇巴因位点的荧光探针AO用于定位CPZ结合位点。用浓度约为20 microM的CPZ处理AO标记的Na +,K + -ATP酶后进行紫外线照射,产生了剂量依赖性的AO荧光变化,例如量子产率增加和蓝移。结果表明CPZ在哇巴因位点附近结合。CPZ与AO标记的Na +,K + -ATP酶的光诱导反应使哇巴因位点免受水环境的影响。还发现紫外线照射CPZ处理过的酶会阻碍AO的结合,这表明哇巴因位点被封闭。这种效应可用于评估CPZ在光化学疗法中的潜在用途。