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. 2009 Dec 1;19(23):6709-12.
doi: 10.1016/j.bmcl.2009.09.119. Epub 2009 Oct 3.

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

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

William M Tay et al. Bioorg Med Chem Lett. .

Abstract

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 12.8mM H(2)O(2), respectively). The significant oxidative activity may contribute to the biological activity of this antibiotic metallopeptide.

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