In silico docking analysis of actinobacterial sideromycins with the alanine racemase enzyme of Acinetobacter baumanii

jerrine joseph


Acinetobacter baumannii is opportunistic Gram-negative bacterial pathogen which causes hospital-acquired infections. Existence of numerous antibiotic-resistant strains of A. baumanii emphasizing the need for the development of new antimicrobials to combat them. Alanineracemase (Alr) is a pyridoxal 5'-phosphate dependent enzyme present in A. baumanii is responsible for racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell wall, its inhibition is lethal to prokaryotes, making it an excellent antibiotic drug target. The structure of AlrAba provides the template required for future structure-based drug-design. In this study, insilico docking studies of the sideromycins albomycin and salmycin against alanineracemase was performed. The binding energy and docked poses evaluation enabled us to conclude that the sideromycins could serve as potential inhibitor of alanine racemase which would be useful in the fight against A. baumanii.



Acinetobacter, alanine racemase, sideromycin, Discovery Studio

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