Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications.
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.
Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Italy.
Sonia
S
Melino
Celeste
C
Santone
Paolo
P
Di Nardo
Bibudhendra
B
Sarkar
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology* / Q000627:therapeutic use; D000935:Antifungal Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology* / Q000627:therapeutic use; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology* / Q000627:therapeutic use; D003300:Copper / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology / Q000627:therapeutic use; D054808:Histatins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology* / Q000627:therapeutic use; D006801:Humans; D061965:Matrix Metalloproteinase Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology / Q000627:therapeutic use; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology / Q000627:therapeutic use; D014945:Wound Healing / Q000187:drug effects; D015032:Zinc / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D015853:Cysteine Proteinase Inhibitors; D054808:Histatins; D061965:Matrix Metalloproteinase Inhibitors; D020033:Protein Isoforms; D003300:Copper; D015032:Zinc
ACTUN motif; Candida albicans; antimicrobial peptides; histidine rich peptide; metallopeptides; metalloprotease inhibitor; reactive oxygen species; saliva; wound healing