Biotechnology Letters

, Volume 28, Issue 24, pp 1971–1982

Protein biosensors based on the principle of fluorescence resonance energy transfer for monitoring cellular dynamics

Authors

  • Isaac T. Li
    • Institute of Biomaterials and Biomedical EngineeringUniversity of Toronto
    • Edward S. Rogers Sr. Department of Electrical and Computer EngineeringUniversity of Toronto
  • Elizabeth Pham
    • Institute of Biomaterials and Biomedical EngineeringUniversity of Toronto
    • Edward S. Rogers Sr. Department of Electrical and Computer EngineeringUniversity of Toronto
    • Institute of Biomaterials and Biomedical EngineeringUniversity of Toronto
    • Edward S. Rogers Sr. Department of Electrical and Computer EngineeringUniversity of Toronto
Review

DOI: 10.1007/s10529-006-9193-5

Cite this article as:
Li, I.T., Pham, E. & Truong, K. Biotechnol Lett (2006) 28: 1971. doi:10.1007/s10529-006-9193-5

Abstract

Genetically-coded, fluorescence resonance energy transfer (FRET) biosensors are widely used to study molecular events from single cells to whole organisms. They are unique among biosensors because of their spontaneous fluorescence and targeting specificity to both organelles and tissues. In this review, we discuss the theoretical basis of FRET with a focus on key parameters responsible for designing FRET biosensors that have the highest sensitivity. Next, we discuss recent applications that are grouped into four common biosensor design patterns—intermolecular FRET, intramolecular FRET, FRET from substrate cleavage and FRET using multiple colour fluorescent proteins. Lastly, we discuss recent progress in creating fluorescent proteins suitable for FRET purposes. Together these advances in the development of FRET biosensors are beginning to unravel the interconnected and intricate signalling processes as they are occurring in living cells and organisms.

Keywords

Fluorescence resonance energy transfer (FRET)Genetically coded biosensorGreen fluorescent protein (GFP)Intermolecular FRETIntramolecular FRETProtein conformational changesProtein–substrate interactionSubstrate cleavageTransgenic organisms

Copyright information

© Springer Science+Business Media B.V. 2006