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.
Department of Chemistry and MBIG, University of South Florida, Tampa, FL 33620-5250, USA.
William M
WM
Tay
Ahmed I
AI
Hanafy
Alexander
A
Angerhofer
Li-June
LJ
Ming
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