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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Does azurin bind to the transactivation domain of p53? A Trp phosphorescence study.
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Does azurin bind to the transactivation domain of p53? A Trp phosphorescence study.

机译：硫林是否与p53的反膜激活结构域结合？ TRP磷光研究。

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摘要

The bacterial redox protein azurin has been shown to be able to enter into cancer cells and induce apoptosis by stabilizing p53. Although the formation of a complex between the two proteins has been demonstrated, little is known about their binding features. We investigated the interaction between the transcription activation domain of p53 (p53(1-63)) and Pseudomonas aeruginosa azurin using fluorescence and phosphorescence spectroscopic techniques. Trp phosphorescence lifetime measurements revealed conformational changes in azurin induced by the interaction with p53(1-63). Acrylamide quenching of Trp phosphorescence also indicated a significant increase in the overall flexibility of azurin upon binding to p53(1-63). We show that azurin binds to the N-terminal region of p53 with a dissociation constant in the 5-10 muM range. No change in the fluorescence and phosphorescence emission of p53(1-63) was detected in the presence of azurin. This result indicated that no Trp residue of p53(1-63) is located in the interaction site with azurin and therefore suggested that the azurin binding site does not overlap that of MDM2, the protein that plays a crucial role in the p53 regulation. The present results may assist in the design of novel cancer treatments based on p53 stabilization by azurin.
机译：已经证明细菌氧化还原蛋白氮素能够通过稳定P53进入癌细胞并诱导细胞凋亡。尽管已经证明了两种蛋白质之间的复合物的形成，但对于它们的结合特征很少。我们研究了使用荧光和磷光光谱技术的P53（P53（1-63））和假单胞菌铜绿假单胞菌的转录激活结构域之间的相互作用。 TRP磷光寿命测量显示通过与P53（1-63）相互作用诱导的紫红素的构象变化。 TRP磷光的丙烯酰胺猝灭还表明紫红素的总体柔韧性显着增加，在结合p53时（1-63）。我们表明硫林素在5-10毫米范围内具有解离常数与P53的N-末端区域结合。在含氮素存在下检测P53（1-63）的荧光和磷光发射的变化。该结果表明，P53（1-63）的NO TRP残基位于与硫脲的相互作用位点，因此建议硫林结合位点与MDM2的蛋白质不重叠，该蛋白质在P53调节中起到至关重要的作用。目前的结果可以帮助基于氮素的P53稳定性设计新型癌症处理。

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