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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
PubMed

Insights

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.
  • 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.

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