Bacterial resistance against clinically used antibiotics is an emerging health concern in contemporary healthcare.1 The suggested long-term solution to tackle the globally prevalent multidrug resistance is to explore new classes of antibiotics.2 Bacterial cell-wall peptidoglycan layer biosynthesis has been promising antibacterial target for decades -lactam (penicillin) and glycopeptide (vancomycin) classes of antibiotics.3 However, current cell wall inhibitors target the late extracellular steps of peptidoglycan synthesis. The early intracellular steps of peptidoglycan synthesis are not well explored clinically, therefore provide an exciting opportunity to explore the current need for novel targets.4 The transmembrane enzyme MraY (phospho-Nacetylmuramoyl-pentapeptide-transferase) is one such intracellular enzyme, which fulfils the requirement of a novel target.5 MraY catalyses the first membrane-associated step of peptidoglycan formation which involves transfer of an UDP-N-acetylmuramoyl (UDP-MurNAc) pentapeptide (-L-Ala1-D--Glu2-Lys/DAP3-D-Ala4-D-Ala5-COOH) (Park’s nucleotide) to the membrane-soluble C55 isoprenoid carrier lipid known as bactoprenol-phosphate (bactoprenol-P), resulting in the formation of lipid I (undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide).6 MraY enzyme (translocase I) is the target of nucleoside antibiotics, class of natural products containing a nucleoside core structure.7 The muraymycins, belongs to the family of ribosamino-uridines class of nucleoside antibiotics, were first discovered as promising structures acting against MraY enzyme in year 2002.8 Though naturally occurring muraymycins quenched the contemporary need of novel structures acting against clinically unexplored target MraY, the challenge faced, to move forward in drug discovery, was their complex and synthetically challenging structures. To address this issue, we are investigating a bioactive, structurally simplified muraymycin analogues acting against a range of bacterial strains.