

Spring Mill Pharma is developing a novel class of non-beta-lactam molecules that kill bacteria by the same selective mechanism as beta-lactams — blocking cell wall synthesis via binding to the bacterial penicillin binding proteins (PBPs). Chemically distinct from the beta-lactams, these new molecules have been designed to be impervious to degradation by any beta-lactamases. By circumventing over seventy years of beta-lactamase-driven resistance, this new class of PBP inhibitors has the potential to usher in a new wave of antibacterial therapeutics.
Spring Mill Pharma has in its portfolio a penicillin-binding protein inhibitor (PBPi; SMP-14079; formerly VNRX-14079) to address the growing problem of resistance by Neisseria gonorrhoeae to ceftriaxone, the last resort cephalosporin-class beta-lactam for outpatient use. The Spring Mill Pharma discovery team has identified and optimized a series of non-beta-lactam transpeptidase inhibitors that are rapidly bactericidal, impervious to beta-lactamases, and show promising selective activity against gonococci, including both wild-type strains and isolates with PBP variants that confer ceftriaxone resistance. SMP-14079 therefore has the potential to maintain PBP inhibition as a core mechanism of action for future anti-gonococcal therapy.