Resistance to B-Lactam Antibiotics Is Mediated Primarily By Enzymes That Hydrolytically Inactivate the Drugs By One of Two Mechanisms: Serine Nucleophilic Attack or Metaldependent Activation of a Water Molecule. Serine B-Lactamases Are Countered In the Clinic By Several Codrugs That Inhibit These Enzymes, Thereby Rescuing Antibiotic Action. the Synthesis Enabled Confirmation of the Stereochemical Configuration of the Compound and Offers a Route For the Synthesis of Derivatives In the Future of Particular Concern Is the Metallo-Β-Lactamases (Mbls), Which Are a Family of Di-Zinc Containing Metalloenzymes Capable of Hydrolyzing a Very Broad Range of Common Β-Lactam Antibiotics. Mbls Are Not Inhibited By Clavulanic Acid, a Drug Commonly Co-Administered With Β-Lactam Antibiotics As an Inhibitor of Other Serine Β -Lactamases. the Aim of the Research Is to Design, Dock (Computer Calculation of an Optimum Fit of a Molecule into an Enzyme Active Site to Find a Possible Docking Geometry and Energy), Synthesize and Assay of Potent and Selective Inhibitors of Mbls (Imp-1).