Label-free multimodal protease detection based on protein/perylene dye coassembly and enzyme-triggered disassembly

Anal Chem. 2014 Jul 1;86(13):6410-7. doi: 10.1021/ac500777r. Epub 2014 Jun 10.

Abstract

The development of novel assays for protease sensing plays an important role in clinical diagnostics and therapeutics. Herein, we report a supramolecular platform for label-free protease detection, based on protein/dye self-assembly and enzyme-triggered disassembly. In a typical case, coassembly of protamine sulfate and perylene dye via electrostatic attractions and π-π interactions caused significant colorimetric and fluorescent responses. Subsequent addition of trypsin was found to cleave the amide bonds of protein, triggering the dissociation of protein/dye aggregates and the release of perylene dyes. The enzyme-triggered disassembly was transduced into multiple readouts including absorption, fluorescence, and polarization, which were exploited for trypsin detection and inhibitor testing. This assay was also used for turn-on fluorescence detection of cathepsin B, an enzyme known to be overexpressed in mammalian cancer cells. The integration of supramolecular self-assembly into enzyme detection in this work has provided a novel label-free biosensing platform which is highly sensitive with multimodal readouts. The relative simplicity of the approach avoids the need for time-consuming substrate synthesis, and is also amenable to naked eye detection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biosensing Techniques / methods*
  • Cathepsin B / analysis*
  • Cattle
  • Fluorescence
  • Fluorescent Dyes / chemistry*
  • Humans
  • Perylene / chemistry*
  • Salmon
  • Spectrometry, Fluorescence / methods
  • Trypsin / analysis*

Substances

  • Fluorescent Dyes
  • Perylene
  • Trypsin
  • Cathepsin B