FtsZ is a bacterial cell division protein that polymerizes in a GTP dependent fashion to form what is known as the Z-ring. The formation and constriction of the Z-ring is crucial for cytokinesis. In the event of DNA damage, an endogenous inhibitor, SulA, halts cell division by binding to FtsZ. This mechanism of bacterial survival ensures that daughter cells do not inherit damaged DNA. FtsZ has become a novel target in the effort to find new ways to fight bacterial infections. As revealed by the FtsZ-SulA x-ray co-crystal structure, the closest point of protein-protein interaction occurs at the T7- loop of FtsZ. Aided by docking methodologies, we have design and synthesized a series of small molecules that mimic the T7-loop of FtsZ. These small molecules share a common rigid scaffold that is easily diversified to yield a library of compounds that will potentially disrupt the interactions between FtsZ and SulA.

Design and synthesis of FtsZ-T7-loop mimics

243rd National Meeting (2012)

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