A plausible role of salivary copper in antimicrobial activity of histatin-5 —Metal binding and oxidative activity of its copper complex

Histatin-5 (Hn5) is an antimicrobial salivary peptide of 24 amino acids. Two specific metal-binding sites were revealed with electronic, NMR, and EPR spectroscopy. The complex Cu 2 II –Hn5 effectively oxidizes catechol, exhibiting enzyme-like kinetics ( k cat = 0.011 and 0.060 s −1 and k cat/ K m =...

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Veröffentlicht in:Bioorganic & medicinal chemistry letters 2009-12, Vol.19 (23), p.6709-6712
Hauptverfasser: Tay, William M., Hanafy, Ahmed I., Angerhofer, Alexander, Ming, Li-June
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Sprache:eng
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Zusammenfassung:Histatin-5 (Hn5) is an antimicrobial salivary peptide of 24 amino acids. Two specific metal-binding sites were revealed with electronic, NMR, and EPR spectroscopy. The complex Cu 2 II –Hn5 effectively oxidizes catechol, exhibiting enzyme-like kinetics ( k cat = 0.011 and 0.060 s −1 and k cat/ K m = 19 and 50 M −1 s −1 without and with 12.8 mM H 2O 2, respectively). The significant oxidative activity may contribute to the biological activity of this antibiotic metallopeptide.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2009.09.119