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dc.contributor.authorMalkoski, M
dc.contributor.authorDashper, SG
dc.contributor.authorO'Brien-Simpson, NM
dc.contributor.authorTalbo, GH
dc.contributor.authorMacris, M
dc.contributor.authorCross, KJ
dc.contributor.authorReynolds, EC
dc.date.available2014-05-21T19:37:59Z
dc.date.issued2001-08-01
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000169999700018&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=d4d813f4571fa7d6246bdc0dfeca3a1c
dc.identifier.citationMalkoski, 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.
dc.identifier.issn0066-4804
dc.identifier.urihttp://hdl.handle.net/11343/26560
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractCaseinomacropeptide (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.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC MICROBIOLOGY
dc.subjectBacteriology ; Infectious Agents; Dentistry not elsewhere classified ; Treatments (e.g. Chemicals
dc.subjectAntibiotics); Dental Health
dc.titleKappacin, a novel antibacterial peptide from bovine milk
dc.typeJournal Article
dc.identifier.doi10.1128/AAC.45.8.2309-2315.2001
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentDental Science
melbourne.source.titleANTIMICROBIAL AGENTS AND CHEMOTHERAPY
melbourne.source.volume45
melbourne.source.issue8
melbourne.source.pages2309-2315
dc.research.coderfcd270301
dc.research.coderfcd270304
dc.research.coderfcd320899
dc.research.codeseo1998670403
dc.research.codeseo1998730214
melbourne.publicationid1146
melbourne.elementsid247269
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC90647
melbourne.contributor.authorDashper, Stuart
melbourne.contributor.authorO'Brien-Simpson, Neil
melbourne.contributor.authorCross, Keith
melbourne.contributor.authorReynolds, Eric
melbourne.contributor.authorMALKOSKI, MARINA
melbourne.contributor.authorTALBO, GERT HOY
dc.identifier.eissn1098-6596
melbourne.accessrightsAccess this item via the Open Access location


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