Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs

Perspectives for biomedical applications

Authors

  • Sonia Melino,

    Corresponding author
    1. Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Italy
    • Correspondence

      S. Melino, Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, via della Ricerca Scientifica, 00133 Rome, Italy

      Fax: +39 067 259 4328

      Tel: +39 067 259 4449

      E-mail: sonia.melino@uniroma2.it

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  • Celeste Santone,

    1. Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Italy
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  • Paolo Di Nardo,

    1. Department of Medical Sciences and Translational Medicine, University of Rome Tor Vergata, Italy
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  • Bibudhendra Sarkar

    1. Department of Molecular Structure and Function, The Hospital for Sick Children, University of Toronto, Ontario, Canada
    2. Department of Biochemistry, University of Toronto, Ontario, Canada
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Abstract

Natural antimicrobial peptides represent a primordial mechanism of immunity in both vertebrate and nonvertebrate organisms. Among them, histatins belong to a family of human salivary metal-binding peptides displaying potent antibacterial, antifungal and wound-healing activities. These properties, along with the ability of histatins to inhibit collagenases and cysteine proteases, have attracted much attention for their potential use in the treatment of several oral diseases. This review critically assesses the studies carried out to date in order to provide a comprehensive and systematic vision of the information accumulated so far. In particular, the relationship between metal-binding and peptide activity is extensively analysed. The review provides important clues for developing possible therapeutic applications of histatins and their synthetic peptide analogues by creating a set of necessary resource materials to support investigators and industries interested in exploiting their unique properties.

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