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A Photoregulated Peptidase Mimic.

Monochura Saha¹, Palash Jana¹, Subhajit Bandyopadhyay¹

¹Department of Chemical Sciences, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur, Nadia, West Bengal, 741246, India.

Angewandte Chemie (International Ed. in English)

|August 4, 2025

Summary

Researchers developed a light-activated enzyme mimic that controls protein and peptide cleavage. This small-molecule light-activated peptidase (SLAP) shows significantly higher activity in its cis isomer, enabling new methods for targeted protein degradation.

Keywords:

Azobenzene Enzyme mimic Molecular photoswitches Peptidase Protein degradation

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Area of Science:

Biochemistry and Chemical Biology
Enzyme Mimicry and Catalysis
Photopharmacology

Background:

Proteases and peptidases are essential enzymes involved in diverse biological functions.
Their activity relies on precise substrate binding and peptide bond hydrolysis.
Controlling enzymatic activity with external stimuli remains a significant challenge.

Purpose of the Study:

To design and synthesize a novel small-molecule light-activated peptidase (SLAP) mimic.
To investigate light-induced control over peptidase activity.
To explore applications in targeted protein degradation.

Main Methods:

Development of a glucose-linked photoswitch-imidazole triad as an enzyme mimic.
Utilizing light to modulate the distance between key catalytic residues and the substrate-binding site.
Assessing catalytic hydrolysis using small molecules, FRET-based substrates, and cellular proteins.

Main Results:

The SLAP mimic demonstrated light-controllable peptidase activity.
The cis isomer showed a ~300-fold increase in catalytic activity compared to the trans isomer.
Successful hydrolysis of various substrates, including complex cellular proteins, was achieved.

Conclusions:

A functional light-activated peptidase mimic was successfully created.
Light provides precise spatiotemporal control over enzymatic activity.
This technology offers novel avenues for applications in targeted protein degradation and chemical biology.