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FRET‐based and other fluorescent proteinase probes
Author(s) -
Hu HaiYu,
Gehrig Stefanie,
Reither Gregor,
Subramanian Devaraj,
Mall Marcus A.,
Plettenburg Oliver,
Schultz Carsten
Publication year - 2014
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201300201
Subject(s) - förster resonance energy transfer , proteases , cathepsin , biology , enzyme , computational biology , biochemistry , proteinase 3 , fluorescence , proteolytic enzymes , microbiology and biotechnology , chemistry , biophysics , immunology , myeloperoxidase , physics , quantum mechanics , inflammation
Abstract The continuous detection of enzyme activities and their application in medical diagnostics is one of the challenges in the translational sciences. Proteinases represent one of the largest groups of enzymes in the human genome and many diseases are based on malfunctions of proteolytic activity. Fluorescent sensors may shed light on regular and irregular proteinase activity in vitro and in vivo and provide a deeper insight into the function of these enzymes and their role in pathophysiological processes. The focus of this review is on Förster resonance energy transfer (FRET)‐based proteinase sensors and reporters because these probes are most likely to provide quantitative data. The medical relevance of proteinases are discussed using lung diseases as a prominent example. Probe design and probe targeting are described and fluorescent probe development for disease‐relevant proteinases, including matrix‐metalloproteinases, cathepsins, caspases, and other selected proteinases, is reviewed.