Teicoplanin

Teicoplanin is a lipoglycopeptide complex first reported from Actinoplanes teichomyceticus in 1978. Teicoplanin is a mixture of several compounds; 5 major compounds, Teicoplanin A2-1 thru A2-5, and 4 minor compounds, referred to as related substances 1 to 4 or teicoplanin RS1-4. All teicoplanin compounds share the same glycopeptide core, termed teicoplanin A3-1, a fused ring structure to which two carbohydrates (mannose and N-acetylglucosamine) are attached.

Teicoplanin has a similar spectrum of activity as vancomycin and is effective against gram-positive bacteria, including methicillin-resistant Staphylococcus aureus (MRSA) and Enterococcus faecalis.
Teicoplanin is a cell wall synthesis inhibitor that works by inhibiting peptidoglycan synthesis and polymerization in two ways. One mechanism inhibits N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) from coming together to form the peptidoglycan backbone. Another mechanism prevents cross-linking between amino acid residues in the peptidoglycan chain.
Teicoplanin is sparingly soluble in water.

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Background

Teicoplanin prevents peptidoglycan synthesis and polymerization by two separate mechanisms. One mechanism prevents N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) from linking together forming the peptidoglycan backbone. The second mechanism prevents cross-linking between amino acid residues in the peptidoglycan chain. This mechanism is nearly identical to vancomycin; however, teicoplanin is considered a safer drug due to its lower nephrotoxicity and ototoxicity.