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)=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.
Tay
William M
WM
Department of Chemistry and MBIG, University of South Florida, Tampa, FL 33620-5250, USA.
Hanafy
Ahmed I
AI
Angerhofer
Alexander
A
Ming
Li-June
LJ
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D000935:Antifungal Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D015195:Drug Design; D005658:Fungi / Q000187:drug effects*; D054808:Histatins / Q000737:chemistry*; D006801:Humans; D008826:Microbial Sensitivity Tests; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D010084:Oxidation-Reduction; D012463:Saliva / Q000737:chemistry; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; C068075:HTN3 protein, human; D054808:Histatins; D009942:Organometallic Compounds; D003300:Copper