A Coumarin-Porphyrin FRET Break-Apart Probe for Heme Oxygenase-1.

ABSTRACT: Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations. The overexpression of HO-1 is commonly associated with cardiovascular and neurodegenerative diseases including atherosclerosis and ischemic stroke. Currently, there are no known chemical probes to detect HO-1 activity, limiting its potential as an early diagnostic/prognostic marker in these serious diseases. Reported here are the design, synthesis, and photophysical and biological characterization of a coumarin-porphyrin FRET break-apart probe to detect HO-1 activity, Fe-L¹. We designed Fe-L¹ to "break-apart" upon HO-1-catalyzed porphyrin degradation, perturbing the efficient FRET mechanism from a coumarin donor to a porphyrin acceptor flu

SUBMITTER: Walter ERH 

PROVIDER: S-EPMC8154531 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature