Abstract: The increasing problem of antimicrobial resistance (AMR) has made it more difficult to treat even common infections, especially Urinary Tract Infections (UTIs) and Bloodstream Infections (BSIs). These infections are often caused by bacteria resistant to multiple antibiotics, limiting treatment options. Among the most common pathogens responsible for these infections is Escherichia coli (E. coli), which has shown increasing resistance to several frontline antibiotics. In this study, multitargeted docking of the FDA-approved library from DrugBank was performed against crucial proteins from E. coli such as FimH (PDB ID: 1UWF), PNAG N-deacetylase (PDB ID: 4F9D), and Purine nucleoside phosphorylase (PDB ID: 4TS3) involved in UTIs, and BtuF (PDB ID: 1N4A), Uridine phosphorylase (PDB ID: 1RXC), and LpxH (PDB ID: 8QJZ) involved in BSIs. This study explored the potential of repurposing Dopexamine, a drug initially used to support heart function, as a possible solution to target key bacterial proteins involved in AMR. An in-silico approach was employed to investigate Dopexamine’s ability to inhibit mutated bacterial proteins associated with E. coli-mediated UTIs and BSIs. Comprehensive computational analyses were performed, including molecular docking to assess binding interactions, molecular dynamics (MD) simulations to evaluate complex stability, MM/GBSA (Molecular Mechanics/Generalized Born Surface Area) calculations to evaluate binding free energies, Water Map analysis to understand hydration patterns, and Density Functional Theory (DFT) to investigate the electronic properties of Dopexamine. The results revealed favourable binding affinities, stable interactions, and promising physicochemical properties, indicating Dopexamine’s potential as a broad-spectrum inhibitor against AMR-related targets. These findings suggest Dopexamine as a valuable candidate for drug repurposing