Glycopeptide antibiotics.

Numerous glycopeptides continue to be described in the literature. They all share a similar heptapeptidic structure with a fixed spatial configuration that forms the basis of their ability to recognize D-alanyl-D-alanine-containing structures in the cell wall. This complexation results in block of peptiglycan elongation; hence, inhibition of growth; and, eventually, cell death. The great variety of substituents on the heptapeptide forms the basis of a wide gradation of physico-chemical characteristics, namely net charge and lipophilicity, which, in turn, might explain the widely differing pharmacologic properties.