Christopher Frøhlich 🇪🇺🇳🇴🇨🇦🇩🇪🏳️‍🌈

Are you interested how #epistasis shapes the AMR evolution?

We showed that epistasis can be caused by independently modulating substrate binding and the chemical step ultimately changing the rate-limiting step in the catalytic cycle. @NatureCatalysis

nature.com/articles/s4192…

We studied the causes of #collateralsensitivity from a single enzyme perspective and how stable such #tradeoffs are during #coselection.

In short, resistance evolution can cause strong but migigatable trade-offs.

Preproof is now available @JMB:

sciencedirect.com/science/articl…

🚨PREPRINT🚨

Enzyme function does not rely only on static structure 🧩, but also on the rate at which functional sub-states interconvert ⏱️, making this interconversion subject to natural selection 🧬.

#OXA48 #ceftazidime #enzymeevolution

biorxiv.org/content/10.648…

Living in the Arctic 🥶 means Christmas comes early 🎁🥳
10 MNOK (≈1 MUSD) Early Career Investigator grant from the Research Council of Norway to work with the fabulous @AdrianBunzel (Max Planck Institute) on uncovering the molecular mechanisms of antibiotic resistance. #AMR

Interested in β-lactamase inhibitors? 🧪

Our new mSphere paper shows how a covalent boronic-acid + chelator fusion ⚗️ can restore β-lactam susceptibility in metallo-β-lactamase producers, even in variants that are difficult to inhibit with taniborbactam.

journals.asm.org/doi/full/10.11…