Kappacin, a novel antibacterial peptide from bovine milk
AuthorMalkoski, M; Dashper, SG; O'Brien-Simpson, NM; Talbo, GH; Macris, M; Cross, KJ; Reynolds, EC
Source TitleAntimicrobial Agents and Chemotherapy
PublisherAMER SOC MICROBIOLOGY
University of Melbourne Author/sDashper, Stuart; O'Brien-Simpson, Neil; Cross, Keith; Reynolds, Eric; MALKOSKI, MARINA; TALBO, GERT HOY
Document TypeJournal Article
CitationsMalkoski, M., Dashper, S. G., O'Brien-Simpson, N. M., Talbo, G. H., Macris, M., Cross, K. J. & Reynolds, E. C. (2001). Kappacin, a novel antibacterial peptide from bovine milk. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 45 (8), pp.2309-2315. https://doi.org/10.1128/AAC.45.8.2309-2315.2001.
Access StatusAccess this item via the Open Access location
Open Access at PMChttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC90647
C1 - Journal Articles Refereed
Caseinomacropeptide (CMP) is a heterogeneous C-terminal fragment (residues 106 to 169) of bovine milk kappa-casein composed of glycosylated and phosphorylated forms of different genetic variants. We have demonstrated that CMP has growth-inhibitory activity against the oral opportunistic pathogens Streptococcus mutans and Porphyromonas gingivalis and against Escherichia coli. CMP was fractionated using reversed-phase high-performance liquid chromatography (RP-HPLC), and each fraction was tested for activity against S. mutans in a 96-well-plate broth assay. Fractions were characterized by N-terminal sequence analysis and mass spectrometry. The active form of CMP was shown to be the nonglycosylated, phosphorylated kappa-casein (residues 106 to 169) [kappa-casein(106--169)], which we have designated kappacin. Endoproteinase Glu-C was used to hydrolyze CMP, and the generated peptides were separated using RP-HPLC and gel filtration-HPLC and then tested for activity against S. mutans. The peptide Ser(P)(149)kappa-casein-A(138--158) was the only peptide generated by endoproteinase Glu-C digestion that exhibited growth-inhibitory activity. Peptides corresponding to the sequences of the inhibitory peptide Ser(P)(149)kappa-casein-A(138--158) and its nonphosphorylated counterpart kappa-casein-A(138--158) were chemically synthesized and tested for antibacterial activity. The synthetic Ser(P)(149) kappa-casein-A(138--158) displayed growth-inhibitory activity against S. mutans (MIC, 59 microg/ml [26 microM]). The nonphosphorylated peptide, however, did not inhibit growth at the concentrations tested, indicating that phosphorylation is essential for activity.
KeywordsBacteriology ; Infectious Agents; Dentistry not elsewhere classified ; Treatments (e.g. Chemicals; Antibiotics); Dental Health
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