Ixori-PVK |
ixosin-B |
chromogranin A (402-438) |
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This peptide (GLHKVMREVLGYERNSYKKFFLR) has been isolated from the salivary glands of the hard tick, Ixodes sinensis. The peptide is derived from a precursor of 79 amino acids. Ixosin has antimicrobial activities against bacteria and fungi (Yu et al, 2006).
Ixosin contains an amino-terminal copper and nickel (ATCUN)-binding sequence that is not essential to the potency of ixosin, but is indispensable to its oxidative mechanism of action. Specifically, the ATCUN motif promotes dioxygen- and copper-dependent lipid (per)oxidation of bacterial membranes. The oxidized phospholipids are utilized as potential targets of ixosin-B, thus resulting in a synergistic effect (Libardo et al, 2016).
For other proteins/peptides with functions in innate immunity and/or antimicrobial activities see also:
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