Binding of teicoplanin to human serum albumin

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Abstract
The interaction between the main components of the new glycopeptide antibiotic teicoplanin, A2–2, A2–3, A2–4, A2–5 and A3–1, and human serum albumin has been studied in vitro by equilibrium dialysis (pH 7.4, 37°C). From Scatchard analysis of the data, the calculated association constants (Ka) were: A2–2, 2.47×104, A2–3, 2.86×104, A2–4, 2.95×104 and A2–5, 3.87×104 mol·l−1. The number of binding sites per albumin molecule ranged between 1.23 to 1.31. A3–1 had a lower affinity with a Ka of about 5×103 mol·l−1. Extrapolated to the in vivo situation, the data suggested that about 90–95% of A2 components will be bound to serum albumin, and about 68–72% of A3–1. The in vitro findings were confirmed by a pharmacokinetic study in volunteers given [14C] teicoplanin i.v., in whom the fraction of teicoplanin bound to serum protein ranged between 87.6 and 90.8%.

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