Title of article
A highly sensitive fluorogenic probe for cytochrome P450 activity in live cells
Author/Authors
Melissa M. Yatzeck، نويسنده , , Luke D. Lavis، نويسنده , , Tzu-Yuan Chao، نويسنده , , Sunil S. Chandran، نويسنده , , Ronald T. Raines، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2008
Pages
3
From page
5864
To page
5866
Abstract
A derivative of rhodamine 110 has been designed and assessed as a probe for cytochrome P450 activity. This probe is the first to utilize a ‘trimethyl lock’ that is triggered by cleavage of an ether bond. In vitro, fluorescence was manifested by the CYP1A1 isozyme with kcat/KM = 8.8 × 103 M−1 s−1 and KM = 0.09 μM. In cellulo, the probe revealed the induction of cytochrome P450 activity by the carcinogen 2,3,7,8-tetrachlorodibenzo-p-dioxin, and its repression by the chemoprotectant resveratrol.
Keywords
cytochrome P450 , dioxin , Fluorogenic substrate , prodrug , Resveratrol , Trimethyl lock , Rhodamine 110 , carcinogen , CYP1A1 isozyme
Journal title
Bioorganic & Medicinal Chemistry Letters
Serial Year
2008
Journal title
Bioorganic & Medicinal Chemistry Letters
Record number
800125
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