Proteases play a crucial role in the regulation of several physiological processes and have been linked to diseases such as human immunodeficiency virus (HIV),  Alzheimer's disease and various cancers.   This close relationship between proteases and diseases provides a strong motivation for developing sensitive and selective methods for the quantitative detection of proteases.  Fluorescence is one of the most effective ways to monitor biomolecular interactions and protease activity.  However, these fluorescence-based probes have a limited increment of signal change; attributed to unquenched fluorophore leading to high background signal and low sensitivity.  To increase the sensitivity, we have molecularly assembled an array of quencher molecules to produce a series of highly sensitive fluorogenic probes. We monitored the effect of the number of quencher molecules and spacing on the enzymatic activity and fluorescence enhancement.  Finally, we analyzed the fluorogenic probes for both homogeneous and heterogeneous assay operation modes.

Design, synthesis, and evaluation peptide-based Fluorescence Resonance Energy Transfer (FRET) probes for the development of protease activity assays

2019 Spring National Meeting

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