Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/12876
Title: Rational Design of a Novel Fluorescent Biosensor for β-Lactam Antibiotics from a Class A β-Lactamase
Authors: Chan, PH
Liu, HB
Chen, YW
Chan, KC
Tsang, CW
Leung, YC 
Wong, KY 
Issue Date: 2004
Source: Journal of the American Chemical Society, 2004, v. 126, no. 13, p. 4074-4075 How to cite?
Journal: Journal of the American Chemical Society 
Abstract: A rational design strategy was used to construct a sensitive "turn-on" biosensor for β-lactam antibiotics and β-lactamase inhibitors from a class A β-lactamase mutant with suppressed hydrolytic activity. A fluorescein molecule was attached to the 166 position on the Ω-loop of the E166C mutant close to the active site of the β-lactamase. Upon binding with antibiotics or inhibitors, the flexibility of the Ω-loop allows the fluorescein molecule to move out from the active site and be more exposed to solvent. This process is accompanied by an increase in the fluorescence of the labeled enzyme. The fluorescence intensity of the biosensor increases with the concentration of antibiotics or inhibitors, which can detect penicillin G at concentrations as low as 50 nM in water. This approach opens a possibility for converting highly active and nonallosteric enzymes into substrate-binding proteins for biosensing purposes.
URI: http://hdl.handle.net/10397/12876
ISSN: 0002-7863
DOI: 10.1021/ja038409m
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