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Three branched peptides, namely pentapeptide A and the two decapeptides B and C corresponding respectively to the monomer and the two dimer peptide fragments of the M. lysodeikticus cell wall peptidoglycan, were synthetized by adequate methods of peptide synthesis in homogeneous phase. The synthetized peptides showed the same electrophoretic and chromatographic behavior as the natural peptide fragments. Only decapeptide B was hydrolysed by the Myxobacter AL-1 protease by cleavage of the D-Ala-L-Ala bond and inversely, only decapeptide C was digested by the Streptomyces albus ML endopeptidase by cleavage of the D-Ala-epsilon-Lys linkage. In both enzymatic hydrolyses the pentapeptide monomer was formed.
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