Using surface plasmon resonance to study the binding of vancomycin and its dimer to self-assembled monolayers presenting D-Ala-D-Ala

The binding of vancomycin and its dimer to self-organized monolayers presenting the C-terminal D-Ala-D-Ala group of Gram-positive bacterial cell wall precursors has been investigated. The objective was to examine the influence of divalency on the binding in the structurally well-characterized model system. Results showed that divalency plays an important role in the antibacterial activity of a divalent variant of vancomycin against vancomycin-resistant bacteria, which is indicated by the values of binding constants.