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Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

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Targeted protein oxidation using a chromophore-modified rapamycin analog.

Taylor M Courtney¹, Chasity P Hankinson¹, Trevor J Horst¹

¹Department of Chemistry, University of Pittsburgh Pittsburgh PA 15260 USA deiters@pitt.edu.

Chemical Science

|November 15, 2021

Summary

Researchers developed BORap, a novel rapamycin analog. This tool enables light-activated deactivation of biological processes by generating reactive oxygen species to inactivate target proteins.

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Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

Chemically induced dimerization (CID) using rapamycin links FKBP and FRB proteins.
This FKBP-rapamycin-FRB complex formation is typically irreversible and used to activate biological processes.
A need exists for temporal control to deactivate biological processes initiated by CID.

Purpose of the Study:

To develop a novel rapamycin analog for light-inducible deactivation of biological processes.
To create a tool for temporal control over FKBP-FRB dimerization-mediated cellular functions.

Main Methods:

Synthesis of a BODIPY-rapamycin analog (BORap).
Utilizing BORap to induce FKBP-FRB dimerization.
Irradiation of BORap-induced complexes with 530 nm light to generate singlet oxygen.
Assessing protein inactivation via singlet oxygen-mediated oxidation.

Main Results:

BORap successfully dimerized FKBP and FRB proteins.
Upon 530 nm light irradiation, BORap generated singlet oxygen.
The generated singlet oxygen oxidized and inactivated proteins fused to FKBP/FRB.

Conclusions:

BORap is the first reactive oxygen species-generating rapamycin analog.
BORap enables light-controlled, reversible deactivation of biological processes mediated by FKBP-FRB dimerization.
This provides a new method for temporal control in chemical biology applications.