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Histatins: salivary peptides with copper( II )‐ and zinc( II )‐binding motifs
Author(s) -
Melino Sonia,
Santone Celeste,
Di Nardo Paolo,
Sarkar Bibudhendra
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12612
Subject(s) - proteases , peptide , antimicrobial peptides , biochemistry , cysteine , computational biology , chemistry , microbiology and biotechnology , biology , enzyme
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.