کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5371343 1503948 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Does azurin bind to the transactivation domain of p53? A Trp phosphorescence study
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Does azurin bind to the transactivation domain of p53? A Trp phosphorescence study
چکیده انگلیسی

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 μM 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.

Highlights► N-transactivation domain of p53 interacts with azurin by inducing structural changes. ► The estimated dissociation constant of the complex ranges from 5 to 10 μM. ► The binding site of azurin on p53 seems to differ from that of MDM2.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 159, Issues 2–3, December 2011, Pages 287-293
نویسندگان
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