Histatin-5 is an antimicrobial cationic peptide present in mammalian saliva that is most effective at killing the opportunistic fungal pathogen <i>Candida albicans</i>. Histatin-5 localizes to the mitochondria and generates reactive oxygen species (ROS) that are implicated as the cause of fungal cell death; however, details of ROS formation remain unknown. Supplementation with copper improves the activity, suggesting a metal-dependent redox mechanism. The antifungal activity has been correlated with the Cu(I)-binding motif comprised of two adjacent histidine residues (<i>bis</i>-His), but not with the amino-terminal Cu(II)-binding site. Utilizing spectroscopic and mass spectrometric methods, this work investigates how the coordination sphere influences the reactivity of Histatin peptides.

Towards understanding the copper-dependent antimicrobial activity of Histatin peptides

ACS Spring Meeting 2021

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