�y��vlog

And perhaps most importantly, the modifications resulted in a molecule that bound and inhibited signal peptidase in a completely novel way, overcoming known arylomycin-resistance mutations.

The frequently mutated apoptosis gene CASP8 displayed clustered missense and other inactivating mutations in the first death effector, intron and caspase peptidase domains.

We generated over a thousand new molecules until we found ones that could penetrate the outer membrane and engage the signal peptidase with exquisite affinity.

Because signal peptidase is essential for bacterial survival, it’s an obvious antibiotic target.

Our discovery efforts started with arylomycins, a class of molecules that target a protein called signal peptidase, which lies just beneath the outer membrane in gram-negative bacteria.