The problem of a growing resistance of bacteria and other microorganisms to conventional antibiotics gave rise to a search for new potent antimicrobial agents. Insect antimicrobial peptides (AMPs) seem to be promising novel potential anti-infective therapeutics. The dipeptide β-alanyl-tyrosine (β-Ala-Tyr) is one of the endogenous insect toxins exhibiting antibacterial activity against both Gram-negative and Gram-positive bacteria. Prior to testing its other antimicrobial activities, it has to be prepared in a pure form. In this study, we have developed a capillary zone electrophoresis (CZE) method for analysis of β-Ala-Tyr isolated from the extract of the hemolymph of larvae of the fleshfly Neobellieria bullata by reversed-phase high-performance liquid chromatography (RP-HPLC). Based on our previously described correlation between CZE and free-flow zone electrophoresis (FFZE), analytical CZE separation of β-Ala-Tyr and its admixtures have been converted into preparative purification of β-Ala-Tyr by FFZE with preparative capacity of 45.5 mg per hour. The high purity degree of the β-Ala-Tyr obtained by FFZE fractionation was confirmed by its subsequent CZE analysis.

• Keywords
• antimicrobial peptides, beta-alanyl-tyrosine, capillary zone electrophoresis, free-flow zone electrophoresis, peptide analysis, peptide purification,
• MeSH
• Anti-Infective Agents chemistry   isolation & purification   MeSH
• Dipeptides chemistry   isolation & purification   MeSH
• Electrophoresis methods   MeSH
• Hemolymph chemistry   MeSH
• Larva chemistry   MeSH
• Sarcophagidae chemistry   MeSH
• Chromatography, High Pressure Liquid MeSH
• Animals MeSH
• Check Tag
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• alanyltyrosine MeSH Browser
• Anti-Infective Agents MeSH
• Dipeptides MeSH