Peptides Codex
Home
Glycopeptide antibiotic (complex)

Teicoplanin

Teicoplanin is a glycopeptide antibiotic complex first isolated in 1978 from Actinoplanes teichomyceticus, sharing the mechanism of vancomycin. It binds the D-alanyl-D-alanine terminus of peptidoglycan precursors, preventing cross-linking and blocking Gram-positive cell-wall synthesis. Marketed as Targocid in many countries (not the U.S.), it treats serious infections including MRSA. This page is educational and not medical advice.

By The Peptides Codex Editorial TeamReviewed July 10, 2026
Length
n/a
Class
Glycopeptide antibiotic (complex)
Function
Binds the D-Ala-D-Ala terminus of peptidoglycan precursors
Context
Approved (outside the U.S.) antibiotic for serious Gram-positive infections

A vancomycin-class glycopeptide, produced as several related A2 components, that caps cell-wall precursors.

Also known as: teichomycin A2 · Targocid

Part of the Foundational & therapeutic peptides cluster

Overview

Teicoplanin is a glycopeptide antibiotic complex first isolated in 1978 from Actinoplanes teichomyceticus, sharing the mechanism of vancomycin. It binds the D-alanyl-D-alanine terminus of peptidoglycan precursors, preventing cross-linking and blocking Gram-positive cell-wall synthesis. Marketed as Targocid in many countries (not the U.S.), it treats serious infections including MRSA. This page is educational and not medical advice.

Source & context

Biological / chemical source: Soil actinomycete Actinoplanes teichomyceticus

Primary research or clinical context: Approved (outside the U.S.) antibiotic for serious Gram-positive infections

Structure and mechanism

Teicoplanin is a mixture of closely related components (A2-1 to A2-5) built on a glycosylated heptapeptide core with a lipid side chain. By binding the D-Ala-D-Ala end of the growing peptidoglycan, it sterically blocks the transpeptidation and transglycosylation steps of cell-wall assembly in Gram-positive bacteria.

Clinical profile

Its long half-life allows once-daily dosing, and it is used for endocarditis, bone and soft-tissue infections and MRSA. Teicoplanin is approved across Europe, Asia and South America but not by the U.S. FDA. Research has also examined glycopeptides for antiviral entry inhibition. This page is educational only.

FAQ about Teicoplanin

What is Teicoplanin?+

Teicoplanin is a glycopeptide antibiotic complex first isolated in 1978 from Actinoplanes teichomyceticus, sharing the mechanism of vancomycin. It binds the D-alanyl-D-alanine terminus of peptidoglycan precursors, preventing cross-linking and blocking Gram-positive cell-wall synthesis. Marketed as Targocid in many countries (not the U.S.), it treats serious infections including MRSA. This page is educational and not medical advice.

Is Teicoplanin an approved medicine?+

Teicoplanin: Approved (outside the U.S.) antibiotic for serious Gram-positive infections. Always follow licensed medical guidance for approved products.

What is the typical length of Teicoplanin?+

Teicoplanin is not a classic amino-acid chain peptide in the same sense; see the profile for classification details.

Related peptides

References & further reading

  1. 1.Wikipedia — Teicoplanin
  2. 2.PubChem — compound summary for Teicoplanin (CID 133065662)
Disclaimer: Educational content only. Not medical advice. Not instructions for human use. Research peptides and unapproved products may be restricted or illegal to market for human consumption in your jurisdiction. Consult qualified professionals and applicable law.
You might also like: All peptides · Atlas · Research · Tools
Cite this: Peptides Codex — Teicoplanin educational profile.
Tip: Use browser print (Ctrl/Cmd + P) for a clean PDF of this page.