It is used in the prophylaxis and treatment of serious infections caused by Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus and Enterococcus faecalis.

[3] Teicoplanin is widely available in many European, Asian, and South American countries, however it is not currently approved by the US Food and Drug Administration and is not commercially available in the United States.

[13] Studies have investigated the use of oral teicoplanin in the treatment of pseudomembranous colitis and Clostridioides difficile-associated diarrhea, finding it to demonstrate efficacy comparable to that of vancomycin.

Teicoplanin is ineffective against Gram-negative bacteria as the large, polar molecules of the compound are unable to pass through the external membrane of these organisms.

[13] The following represents MIC susceptibility data for a few medically significant pathogens:[4] Due to poor oral absorption, teicoplanin requires intravenous or intramuscular administration for systemic effect.

The drug exhibits high protein binding (90-95%) and is primarily eliminated through the kidneys unchanged, with minimal liver metabolism (2-3%) via hydroxylation.

It binds to the D-alanyl-D-alanine (D-Ala-D-Ala) terminus of the peptidoglycan precursor, preventing the transpeptidation reaction necessary for cell wall cross-linking.

[6] In addition to its binding to the D-Ala-D-Ala terminus, teicoplanin may also interact with the lipid II substrate in the bacterial cell membrane through its hydrophobic tail.

While there is potential for nephrotoxicity and ototoxicity, the incidence of such organ toxicity is rare if recommended serum concentrations are successfully maintained.

The major and minor components also contain a third carbohydrate moiety — β-D-glucosamine — and differ only by the length and conformation of a side-chain attached to it.

Teicoplanin refers to a complex of related natural products isolated from the fermentation broth of a strain of Actinoplanes teichomyceticus,[21] consisting of a group of five structures.

These structures possess a common aglycone, or core, consisting of seven amino acids bound by peptide and ether bonds to form a four-ring system.

The presence of the * symbol means a gene is found after NRPs, which are represented by A, B, C, and D. Based on the figure from: Li, T-L.; Huang, F.; Haydock, S. F.; Mironenko, T.; Leadlay, P. F.; Spencer, J.

The heptapeptide backbone of teicoplanin is assembled by the nonribosomal peptide synthetases (NRPSs) TeiA, TeiB, TeiC and TeiD.

The activated amino acids are covalently bound to the NRPS as thioesters by a phosphopantetheine cofactor, which is attached to the peptidyl carrier protein (PCP) domain.

[28] The regioselectivity and atropisomer selectivity of these probable one-electron coupling reactions has been suggested to be due to the folding and orientation requirements of the partially crossed-linked substrates in the enzyme active site.

In vitro experiments have demonstrated teicoplanin's ability to reduce SARS-CoV-2 infection, with reported IC50 values in the low micromolar range.