Imaging farnesyl protein transferase using a topologically activated probe

被引：5

作者：

Pham, Wellington ^{[1
]}

Pantazopoulos, Pamela ^{[1
]}

Moore, Anna ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Massachusetts Gen Hosp,Dept Radiol, Mol Imaging Lab,Athinoula A Martinos Ctr Biomed I, Charlestown, MA 02129 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 36期

关键词：

D O I：

10.1021/ja063599x

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report on the development and application of a "smart" activatable peptide-based probe for detection of Ras-related farnesyl protein transferase (FPT). Upon farnesylation by FPT, the probe was brought close to a hydrophobic milieu and as a consequence emitted fluorescent light that could be detected by several media, such as fluorescence microscopy, a plate reader, and an optical imaging system. A FPT activity assay confirmed the specificity of the probe (IC50 = 1.2 μM) for FPT compared to that of the native peptide (IC50 = 0.17 μM). In addition, the probe has remarkable binding constant, Kd = 26 nM. The specificity of enzyme activation was proved in pure enzyme assays as well as in cell-based assays. Furthermore, the fluorescent enhancement of the probe was 30-fold stronger than the control peptide in a live cell assay. Copyright © 2006 American Chemical Society.

引用

页码：11736 / 11737

页数：2

共 12 条

[1] ISOPRENYLATION IS REQUIRED FOR THE PROCESSING OF THE LAMIN-A PRECURSOR [J].