Molecular Dynamics Simulation of Atomic Interactions in the Vancomycin Binding Site.

ABSTRACT: Vancomycin is a glycopeptide antibiotic produced by Amycolaptopsis orientalis used to treat serious infections by Gram-positive pathogens including methicillin-resistant Staphylococcus aureus. Vancomycin inhibits cell wall biosynthesis by targeting lipid II, which is the membrane-bound peptidoglycan precursor. The heptapeptide aglycon structure of vancomycin binds to the d-Ala-d-Ala of the pentapeptide stem structure in lipid II. The third residue of vancomycin aglycon is asparagine, which is not directly involved in the dipeptide binding. Nonetheless, asparagine plays a crucial role in substrate recognition, as the vancomycin analogue with asparagine substituted by aspartic acid (V_D) shows a reduction in antibacterial activities. To characterize the function of as

SUBMITTER: Olademehin OP 

PROVIDER: S-EPMC7808135 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature