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A protein biosensor for lactate.

S D'Auria¹, Z Gryczynski, I Gryczynski

¹Department of Biochemistry and Molecular Biology, Center for Fluorescence Spectroscopy, University of Maryland at Baltimore, 21201, USA.

Analytical Biochemistry

|August 10, 2000

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This study introduces a novel protein biosensor for detecting blood lactate using lactate dehydrogenase (LDH) labeled with 8-anilino-1-naphthalene sulfonic acid (ANS). The sensor shows promise for point-of-care diagnostics but requires further development for stability.

Area of Science:

Biochemistry
Biotechnology
Biosensor Technology

Background:

Blood lactate is a critical clinical diagnostic marker.
Existing lactate detection methods may have limitations in speed or accessibility.
Lactate dehydrogenase (LDH) is an enzyme involved in lactate metabolism.

Purpose of the Study:

To develop a novel protein biosensor for L-lactate detection.
To utilize lactate dehydrogenase (LDH) for sensing applications.
To explore a new sensing format for potential point-of-care devices.

Main Methods:

Noncovalent labeling of beef heart lactate dehydrogenase (LDH) with 8-anilino-1-naphthalene sulfonic acid (ANS).
Measurement of fluorescence emission intensity changes upon lactate binding to ANS-labeled LDH.

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Exploration of polarization sensing with ANS-labeled LDH for miniaturization.

Main Results:

ANS-labeled LDH exhibited an approximate 40% decrease in emission intensity when binding to lactate.
The observed fluorescence change directly correlates with lactate concentration.
Polarization sensing format demonstrated suitability for miniaturization.

Conclusions:

A functional protein biosensor for L-lactate has been developed using ANS-labeled LDH.
The developed sensing mechanism is sensitive to lactate concentration.
Further protein engineering is necessary to enhance the temporal stability of the biosensor for clinical applications.