teicoplanin-aglycone and Sepsis

A series of peptide derivatives of teicoplanin A2 (CTA) and deglucoteicoplanin (TD) was prepared by condensation of the 63-carboxyl function with the alpha-amino group of selected amino acids and their derivatives. The modification of the ionic character of CTA and TD influenced their in vitro and in vivo antimicrobial properties to a different extent, depending on the structure of the amino acidic moiety at C-63. A certain effect on binding strength to Ac2-L-Lys-D-Ala-D-Ala, a synthetic model of the antibiotic's target peptide, was also observed.

Topics: Animals; Anti-Bacterial Agents; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Glycopeptides; Gram-Positive Bacteria; Mice; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides, Cyclic; Sepsis; Streptococcal Infections; Structure-Activity Relationship; Teicoplanin