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 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
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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. |
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ISSN: | 0960-894X 1464-3405 |
DOI: | 10.1016/j.bmcl.2009.09.119 |