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    Divalent metal cations increase the activity of the antimicrobial peptide kappacin

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    Author
    Dashper, SG; O'Brien-Simpson, NM; Cross, KJ; Paolini, RA; Hoffmann, B; Catmull, DV; Malkoski, M; Reynolds, EC
    Date
    2005-06-01
    Source Title
    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
    Publisher
    AMER SOC MICROBIOLOGY
    University of Melbourne Author/s
    Dashper, Stuart; O'Brien-Simpson, Neil; Cross, Keith; Paolini, Rita; Hoffmann, Brigitte; Catmull, Deanne; Reynolds, Eric; MALKOSKI, MARINA
    Affiliation
    Dental Science
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Dashper, S. G., O'Brien-Simpson, N. M., Cross, K. J., Paolini, R. A., Hoffmann, B., Catmull, D. V., Malkoski, M. & Reynolds, E. C. (2005). Divalent metal cations increase the activity of the antimicrobial peptide kappacin. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 49 (6), pp.2322-2328. https://doi.org/10.1128/AAC.49.6.2322-2328.2005.
    Access Status
    Access this item via the Open Access location
    URI
    http://hdl.handle.net/11343/26558
    DOI
    10.1128/AAC.49.6.2322-2328.2005
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1140507
    Description

    C1 - Journal Articles Refereed

    Abstract
    Kappacin, nonglycosylated kappa-casein(106-169), is a novel antimicrobial peptide produced from kappa-casein found in bovine milk. There are two major genetic forms of kappacin, A and B, and using synthetic peptides corresponding to the active region, kappa-casein(138-158), of these forms, we have shown that the Asp148 to Ala148 substitution is responsible for the lesser antibacterial activity of kappa-casein-B(106-169). Kappacin was shown to have membranolytic action at concentrations above 30 microM at acidic pH when tested against artificial liposomes. There was little membranolytic activity at neutral pH, which is consistent with the lack of antibacterial activity of kappacin against Streptococcus mutans at this pH. Kappacin specifically bound two zinc or calcium ions per mol, and this binding enhanced antibacterial activity at neutral pH. Nuclear magnetic resonance analysis indicated that a kappa-casein-A(138-158) synthetic peptide undergoes a conformational change in the presence of the membrane solvent trifluoroethanol and excess divalent metal ions. This change in conformation is presumably responsible for the increase in antibacterial activity of kappacin detected in the presence of excess zinc or calcium ions at neutral pH. When tested against the oral bacterial pathogen S. mutans cultured as a biofilm in a constant-depth film fermentor, a preparation of 10 g/liter kappacin and 20 mM ZnCl2 reduced bacterial viability by 3 log10 and suppressed recovery of viability. In contrast 20 mM ZnCl2 alone reduced bacterial viability by approximately 1 log10 followed by rapid recovery. In conclusion, kappacin has a membranolytic, antibacterial effect that is enhanced by the presence of divalent cations.
    Keywords
    Analytical Biochemistry; Bacteriology ; Prevention - Biologicals (e.g. Vaccines); Treatments (e.g. Chemicals; Antibiotics); Dental Health

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