Jump to main content
Jump to site search

Issue 1, 2021
Previous Article Next Article

Ultrasensitive small molecule fluorogenic probe for human heparanase

Author affiliations

Abstract

Heparanase (HPA) is a critical enzyme involved in the remodeling of the extracellular matrix (ECM), and its elevated expression has been linked with diseases such as various types of cancer and inflammation. The detection of heparanase enzymatic activity holds tremendous value in the study of the cellular microenvironment, and search of molecular therapeutics targeting heparanase, however, no structurally defined probes are available for the detection of heparanase activity. Here we present the development of the first ultrasensitive fluorogenic small-molecule probe for heparanase enzymatic activity via tuning the electronic effect of the substrate. The probe exhibits a 756-fold fluorescence turn-on response in the presence of human heparanase, allowing one-step detection of heparanase activity in real-time with a picomolar detection limit. The high sensitivity and robustness of the probe are exemplified in a high-throughput screening assay for heparanase inhibitors.

Graphical abstract: Ultrasensitive small molecule fluorogenic probe for human heparanase

Back to tab navigation

Supplementary files

Article information


Submitted
03 Sep 2020
Accepted
16 Oct 2020
First published
20 Oct 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2021,12, 239-246
Article type
Edge Article

Ultrasensitive small molecule fluorogenic probe for human heparanase

J. Liu, K. A. Schleyer, T. L. Bryan, C. Xie, G. Seabra, Y. Xu, A. Kafle, C. Cui, Y. Wang, K. Yin, B. Fetrow, P. K. P. Henderson, P. Z. Fatland, J. Liu, C. Li, H. Guo and L. Cui, Chem. Sci., 2021, 12, 239
DOI: 10.1039/D0SC04872K

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements