Some members of this class of drugs inhibit the synthesis of cell walls in susceptible microbes by inhibiting peptidoglycan synthesis. The core class (including vancomycin) binds to acyl--alanyl--alanine in lipid II, preventing the addition of new units to the peptidoglycan. Of this core class, one may distinguish multiple generations: the first generation includes vancomycin and teicoplanin, while the semisynthetic second generation includes lipoglycopeptides like telavancin, oritavancin and dalbavancin. The extra lipophilicity not only enhances Lipid II binding, but also creates a second mechanism of action whereby the antibiotic dissolves into the membrane and makes it more permeable.
Corbomycin and complestatin are structurally and ancestrally related to vancomycin, but they work by inhibiting autolysins through binding to peptidoglycan, therefore preventing cell division, neither is an approved drug.
Ramoplanin, although a "glycopeptide" in the literal sense, has a quite different structural core. It not only binds to Lipid II, but also attacks MurG and transglycosylases (glycosyltransferases) which polymerize amino acid/sugar building blocks into peptidoglycan. It has been described as a "first-in-class" antibiotic, representing glycolipodepsipeptide antibiotics.
Bleomycin also has a different core. Its mode of action is also unrelated to the cell wall, instead causing DNA damage in tumor cells.