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Histone controlled aggregation of tetraphenylethene probe: A new method for the detection of protease activity.
- Source :
-
Sensors & Actuators B: Chemical . Mar2018, Vol. 257, p1143-1149. 7p. - Publication Year :
- 2018
-
Abstract
- A novel fluorescence “turn-on” assay for protease activity based on controlled aggregation of a tetraphenylethene probe is reported. A tetraphenylethene derivative (TPE-2+) with two positive charges is used in this study. TPE-2+ has no emission in an aqueous solution. Heparin is an anionic polymer, which can induce aggregation of TPE-2+. Strong aggregation-induced fluorescence emission (AIE) is observed. Histone is a cationic protein, it binds with heparin via electrostatic attractive interactions, which hinders the binding of TPE-2+ to heparin. TPE-2+ is released, and a decreased emission signal is detected. Upon the addition of a protease, histone is hydrolyzed into small fragments, which weakens its competitive binding to heparin. Free heparin induces aggregation of TPE-2+. A turn-on emission signal is recorded. An efficient and convenient fluorescence assay for protease activity is therefore established. [ABSTRACT FROM AUTHOR]
- Subjects :
- *SERINE proteinases
*PROTEASE inhibitors
*PROTEINASES
*ENDONUCLEASES
*NEUROPEPTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 09254005
- Volume :
- 257
- Database :
- Academic Search Index
- Journal :
- Sensors & Actuators B: Chemical
- Publication Type :
- Academic Journal
- Accession number :
- 126993943
- Full Text :
- https://doi.org/10.1016/j.snb.2017.10.018