page_title: Vancomycin
section_title: Mechanism of action
hierarchical_section_title: Vancomycin / Pharmacology and chemistry / Mechanism of action
caption_attribution_description: This is a picture generated from crystal structure data reported by James R. Knox and R. F. Pratt in Antimicrobial Agents and Chemotherapy, Year 1990, Volume 34, Issue 7, Pages 1342-1347. It shows a short peptide (L-lysyl-D-alanyl-D-alanine), which is a bacterial cell wall precursor, bound to the antibiotic en:vancomycin. The peptide is bound to vancomycin through five hydrogen bonds indicated by the dotted lines. It was made by myself and is free to be used by all.
context_page_description: Vancomycin is an antibiotic used to treat a number of bacterial infections. It is recommended intravenously as a treatment for complicated skin infections, bloodstream infections, endocarditis, bone and joint infections, and meningitis caused by methicillin-resistant Staphylococcus aureus. Blood levels may be measured to determine the correct dose. Vancomycin is also recommended by mouth as a treatment for severe Clostridium difficile colitis. When taken by mouth it is very poorly absorbed.
  Common side effects include pain in the area of injection and allergic reactions. Occasionally, hearing loss, low blood pressure, or bone marrow suppression occur. Safety in pregnancy is not clear, but no evidence of harm has been found, and it is likely safe for use when breastfeeding. It is a type of glycopeptide antibiotic and works by blocking the construction of a cell wall.
  Vancomycin was first sold in 1954. It is on the World Health Organization's List of Essential Medicines. The World Health Organization classifies vancomycin as critically important for human medicine. It is available as a generic medication. Vancomycin is made by the soil bacterium Amycolatopsis orientalis.
context_section_description: Vancomycin acts by inhibiting proper cell wall synthesis in Gram-positive bacteria. Due to the different mechanism by which Gram-negative bacteria produce their cell walls and the various factors related to entering the outer membrane of Gram-negative organisms, vancomycin is not active against them (except some nongonococcal species of Neisseria).
  The large hydrophilic molecule is able to form hydrogen bond interactions with the terminal D-alanyl-D-alanine moieties of the NAM/NAG-peptides. Under normal circumstances, this is a five-point interaction. This binding of vancomycin to the D-Ala-D-Ala prevents cell wall synthesis of the long polymers of N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) that form the backbone strands of the bacterial cell wall, and it prevents the backbone polymers that do manage to form from cross-linking with each other.
caption: Crystal structure of a short peptide L-Lys-D-Ala-D-Ala (bacterial cell wall precursor, in green) bound to vancomycin (blue) through hydrogen bonds[53]
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