Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5.

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  • Additional Information
    • Source:
      Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, American Chemical Society.
    • Subject Terms:
      Antifungal Agents/*metabolism ; Deoxyribonucleases/*metabolism ; Histatins/*metabolism ; Salivary Proteins and Peptides/*metabolism; Amino Acid Sequence ; Antifungal Agents/chemistry ; Candida albicans/growth & development ; Copper/chemistry ; Copper/metabolism ; Deoxyribonucleases/chemistry ; Histatins/chemistry ; Humans ; Molecular Sequence Data ; Nickel/chemistry ; Nickel/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Salivary Proteins and Peptides/chemistry
    • Abstract:
      The salivary antimicrobial peptide histatin 5 is characterized by its cationic nature, structural flexibility, and the presence of two metal-binding sites (the ATCUN motif and a Zn-binding motif). These properties make this peptide a good model for the design of new drugs of low molecular weight. In this work, we have synthesized and studied a new peptide, an analogue of the histatin 5 named ATCUN-C16, which contains both metal-binding centers. The results show that our 20-residue-derived peptide preserves anticandidal activity and exhibits a higher propensity to assume a stable conformation in a hydrophobic environment than do histatin 5 and the C16 peptide that contains the 16 residues of the C-terminal part of histatin 5, although overall our peptide remains a flexible molecule. ACTUN-C16 was found to bind DNA in a gel retardation assay and to have a nuclease activity in the presence of copper and zinc ions and ascorbate. Its nuclease activity can be attributed to the synergistic action of oxidative and hydrolytic activities due to the Cu-ATCUN complex and to the zinc ion coordination, respectively. The results show a new property of this family of salivary peptides and suggest a novel use of this peptide as a small nuclease and biotechnological tool.
    • Accession Number:
      0 (Antifungal Agents)
      0 (HTN3 protein, human)
      0 (Histatins)
      0 (Peptide Fragments)
      0 (Salivary Proteins and Peptides)
      789U1901C5 (Copper)
      7OV03QG267 (Nickel)
      EC 3.1.- (Deoxyribonucleases)
    • Publication Date:
      Date Created: 20061221 Date Completed: 20080111 Latest Revision: 20131121
    • Publication Date:
      20231215
    • Accession Number:
      10.1021/bi0615137
    • Accession Number:
      17176059