Abstract

Siderophores are low molecular weight ferric ion chelators synthesized by bacteria in iron limiting conditions. These chelators scavenge iron and are recognized in their ferric-bound state by highly conserved surface receptors which promote ATP dependent internalization after which the metal center can be liberated by reduction or fragmentation of the siderophore scaffold. This dissertation sought to answer two primary questions: 1) can rationally designed inhibitors elucidate the mechanism of siderophore biosynthesis by the iterative siderophore synthetase DesD and 2) can the receptor/transporter complexes present in pathogenic bacteria be exploited for targeted imaging of bacterial infection by a radiolabeled siderophore-antibiotic conjugate? Herein, the synthesis of tight binding inhibitors for DesD which mimic the reactive intermediates in the catalytic cycle are reported with crystal structures identifying novel substrate binding modes. A heterobifunctional imaging agent of bacterial infection was also designed and validated in vivo.

Committee Chair

Timothy Wencewicz

Degree

Doctor of Philosophy (PhD)

Author's Department

Chemistry

Author's School

Graduate School of Arts and Sciences

Document Type

Dissertation

Date of Award

6-5-2026

Language

English (en)

Available for download on Sunday, June 04, 2028

Included in

Chemistry Commons

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