I’m reminded how important it is to stay open-minded: proximity-induced modalities are still new to me in antivirals, but already well established in oncology – which made the discussions especially rewarding.

#DPhG2025

As a molecular virologist, it’s humbling and inspiring to exchange ideas with experts in medicinal chemistry and drug development at the interface of chemistry and virology.

#DPhG2025

This work proves that targeted protein degradation can go beyond enzymatic targets—opening up new viral proteins and ligands for therapeutic intervention. A promising step forward for antiviral PROTACs.

We show that inactive ligands, binding outside of catalytic pockets, can still serve as potent warheads—expanding the antiviral degrader design space to new viral targets.

Our lead compound, LLP019, robustly degraded Mpro in a cereblon-dependent manner and significantly reduced viral titers—despite its warhead being inactive as an inhibitor. Consequently, degradation, not inhibition, drove the antiviral effect.

We redesigned pelitinib, an allosteric binder of SARS-CoV-2 Mpro, to create a series of degraders—leveraging its binding mode to go beyond conventional targeting of catalytic clefts.

We asked: can ligands that bind outside—or in absence of—a catalytic cleft act as warheads for antiviral PROTACs? Until now, most such degraders targeted active sites. We set out to challenge that paradigm.

While this marks the end of an important chapter in my life, I see it as the beginning of a new journey—one that I hope will lead me to exciting destinations, surrounded by inspiring mentors, colleagues, and friends in academia.
#PhDone #OneDegreeHotter

A heartfelt thank you to everyone who has supported me throughout this journey. I am especially grateful to Prof. Becker, whose guidance made all of this possible in the first place, and to Dr. Anke Werner, who has been not only an incredible mentor but also a dear friend.