Light-Activated Molecules Stop Apoptosis at the Flip of a Switch

A new inhibitor gives researchers the ability to control programmed cell death in cultured human T cells.

Written byJef Akst

| 3 min read

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Scientists know a lot about apoptosis, from its molecular control to pathways that stop the cell death process in its tracks, but being able to control when and where it occurs would help researchers glean more details about its role in development. To that end, chemical biologist Steven Verhelst of KU Leuven in Belgium and his PhD student Suravi Chakrabarty decided to use a technique called photocaging to make an inhibitor of caspases, enzymes involved in apoptosis, that can be controlled by light.

For a small molecule to effectively inhibit a caspase, it needs a negative charge in just the right spot to fit into a positively charged pocket of the enzyme. Verhelst and Chakrabarty decided to develop a molecule that had a photocage, a chemical group that sat on top of that negative charge and prevented the inhibitor from binding and stopping the caspases from ...

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Meet the Author

Jef Akst
Jef (an unusual nickname for Jennifer) got her master’s degree from Indiana University in April 2009 studying the mating behavior of seahorses. After four years of diving off the Gulf Coast of Tampa and performing behavioral experiments at the Tennessee Aquarium in Chattanooga, she left research to pursue a career in science writing. As The Scientist's managing editor, Jef edited features and oversaw the production of the TS Digest and quarterly print magazine. In 2022, her feature on uterus transplantation earned first place in the trade category of the Awards for Excellence in Health Care Journalism. She is a member of the National Association of Science Writers.
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