Antifungal resistance poses a significant clinical challenge for treating invasive fungal infections. Candida albicans is responsible for candidiasis including invasive fungal infections, where most patients are immunocompromised. Therefore the success of treatment depends significantly on the effectiveness of the antifungal agent. In this study, sixteen novel furan derivatives containing the azetidinone moiety were designed and synthesized to arrive at potentially effective antifungal agents. In silico antifungal activity was carried out to identify the specificity of the novel furan derivatives for the fungal proteins using 'Glide'. Molecular docking studies were conducted on two antifungal targets; Dihydrofolate reductase of C.albicans (PDB ID: 4HOE); N-myristoyl transferase of C.albicans (PDB ID: 1IYK). Molecular docking was carried out at the Standard Precision (SP) and Extra Precision (XP) mode. The docked poses were ranked according to their docking scores (GScore) and their binding energy with the enzyme. The results obtained for the docking of the title compounds with N-myristoyl transferase of C.albicans is quite promising. Molecular docking suggests that compounds 4d, 4e, and 4h are potential inhibitors of N-myristoyl transferase and are specific in binding at the active site of the enzyme. They form Hbond with THR 211 and pi-pi stacking interactions with PHE 117, TRY 354, and TRY 225 at the active site of the protein, similar to the standard drug. However the test compounds show low docking scores against Dihydrofolate reductase of C.albicans indicating that they may not be effective against it.

Escherichia coli is the predominant gram negative bacteria responsible for a variety of hospital-acquired infections and urinary tract infections. As the bacterial strains are rapidly acquiring resistance to the available antibiotics, there is a need to discover novel antibacterial agents with different scaffolds. In this study, sixteen novel furan derivatives containing the azetidinone moiety were designed and synthesized to arrive at potentially effective antibacterial agents. In silico antibacterial activity was carried out to identify the specificity of the furan derivatives for the antibacterial targets. Molecular docking studies were conducted on four antibacterial targets of E. coli; Dihydrofolate reductase, DNA gyrase, Enoyl reductase and methionine aminopeptidase. Energy minimization of title compounds was carried out and they were docked on to the active site of the enzymes. Ligands were ranked according to their docking scores and their binding energy with the enzyme. The results obtained for the molecular docking of the title compounds with enoyl reductase of E. coli is quite promising. The study suggests that compounds 4E and 4D are potential inhibitors of enoyl reductase and specifically bind to the enzyme.

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