Self-Immobilizing Quinone Methides for the Fluorescent Sensing of Enzyme Activity

6Citations
Citations of this article
5Readers
Mendeley users who have this article in their library.

Abstract

Gaining insight into biological processes relies on sensitive analytical techniques. These often require labeling of biomolecules that help visualize them. Selective covalent labeling without preliminary modification of the biomolecules is an advantageous method. For example, this can be achieved by using probes that are capable of in situ quinone methide (QM) formation. The QM can be masked to give a stable precursor, and the highly reactive form is only generated upon activation by a specific trigger. The in situ formed QM then binds covalently to the nucleophilic side chains of either the target protein or a protein in close proximity. Using fluorogenic probes further improves this method by reducing non-specific background signals, thus improving signal-to-noise ratios. In this review we summarize the development of quinone methide-based probes from mechanism-based inactivation to red-emitting, fluorogenic activity probes, focusing on enzyme-triggered activation.

Cite

CITATION STYLE

APA

Kern, D., & Kormos, A. (2023, March 1). Self-Immobilizing Quinone Methides for the Fluorescent Sensing of Enzyme Activity. Chemosensors. Multidisciplinary Digital Publishing Institute (MDPI). https://doi.org/10.3390/chemosensors11030155

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free