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.

Melino, S.m., Gallo, M., Trotta, E., Mondello, F., Paci, M., Petruzzelli, R. (2006). Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5. BIOCHEMISTRY, 45(51), 15373-15383 [10.1021/bi0615137].

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

MELINO, SONIA MICHAELA;PACI, MAURIZIO;
2006-01-01

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.
2006
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Amino acids; Bioassay; DNA; Hydrophobicity; Molecular weight; Positive ions; Antimicrobial peptide analogue; Salivary peptides; Zinc ion coordination; Enzyme kinetics; ascorbic acid; cation; copper ion; histatin 5; nuclease; peptide derivative; protein ATCUN C16; saliva protein; zinc ion; article; assay; binding site; biotechnology; carboxy terminal sequence; complex formation; enzyme activity; gel retardation assay; hydrolysis; hydrophobicity; metal binding; molecular model; molecular weight; oxidation; priority journal; protein conformation; protein DNA binding; protein family; protein motif; protein stability; protein structure; Amino Acid Sequence; Antifungal Agents; Candida albicans; Copper; Deoxyribonucleases; Histatins; Humans; Molecular Sequence Data; Nickel; Peptide Fragments; Salivary Proteins
Melino, S.m., Gallo, M., Trotta, E., Mondello, F., Paci, M., Petruzzelli, R. (2006). Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5. BIOCHEMISTRY, 45(51), 15373-15383 [10.1021/bi0615137].
Melino, Sm; Gallo, M; Trotta, E; Mondello, F; Paci, M; Petruzzelli, R
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/34560
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