Histatin-5 (Hist-5) is a polycationic, histidine-rich antimicrobial peptide with potent antifungal activity against the opportunistic fungal pathogen <i>Candida albicans</i>. Hist-5 has the ability to bind several metals in vitro and metals have been shown to alter the fungicidal activity of the peptide. The goal of this work is to further elucidate the mechanism of action of Hist-5 and understand how biologically relevant metals may affect that mechanism. Toward this goal, we prepared a fluorescently labeled Hist-5 peptide called Hist-5Mca-ABD to visualize the internalization and localization the peptide in fungal cells. Cellular growth assays show that Hist-5Mca-ABD retains its antifungal activity against <i>C. albicans</i> and cotreatment with varying concentrations of Cu(II), Fe(III), or Zn(II) result in metal-dependent peptide activity. Internalization of Hist-5Mca-ABD was observed through confocal fluorescence microscopy. Overall, our data provide evidence that metals can play a role in modulating the biological activity of Hist-5.

Understanding the metal mediated mode of action of the antimicrobial peptide Histatin-5

ACS Spring Meeting 2021

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