Zn2+ Ions Selectively Induce Antimicrobial Salivary Peptide Histatin-5 To Fuse Negatively Charged Vesicles. Identification and Characterization of a Zinc-Binding Motif Present in the Functional Domain
| العنوان: | Zn2+ Ions Selectively Induce Antimicrobial Salivary Peptide Histatin-5 To Fuse Negatively Charged Vesicles. Identification and Characterization of a Zinc-Binding Motif Present in the Functional Domain |
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| المؤلفون: | Stefano Rufini, Sonia Melino, Raffaele Petruzzelli, Maurizio Paci, Marco Sette, Alessandro Grottesi, Roberto D. Morero |
| المصدر: | Biochemistry. 38:9626-9633 |
| بيانات النشر: | American Chemical Society (ACS), 1999. |
| سنة النشر: | 1999 |
| مصطلحات موضوعية: | Secondary, Circular dichroism, Conformational change, dimethyl sulfoxide, Peptide, Membrane Fusion, Biochemistry, Protein Structure, Secondary, Anti-Infective Agents, alpha helix, protein tertiary structure, Protein secondary structure, chemistry.chemical_classification, conformational transition, histatin, isoprotein, trifluoroethanol, water, zinc ion, amino acid sequence, antimicrobial activity, article, binding site, carboxy terminal sequence, concentration response, metal binding, molecular dynamics, priority journal, protein aggregation, protein binding, protein determination, protein domain, regulatory mechanism, structure analysis, Amino Acid Sequence, Animals, Circular Dichroism, Humans, Liposomes, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Protein Binding, Salivary Proteins, Sequence Analysis, Solutions, Trifluoroethanol, Zinc, Vesicle, Amino acid, Protein Structure, Nuclear Magnetic Resonance, Histatins, Settore BIO/09, Consensus sequence, Settore BIO/10, Salivary Proteins and Peptides, chemistry, Histatin, Biophysics, Biomolecular |
| الوصف: | The salivary antimicrobial peptide histatin-5 is able to aggregate and fuse negatively charged small unilamellar vesicles, and this fusogenic activity is selectively induced by the presence of zinc ions. Circular dichroism spectroscopy shows that histatin-5, in the presence of negatively charged vesicles and zinc ions, undergoes a conformational change leading to the stabilization of an alpha-helical secondary structure. We attribute the specific action of the zinc ions to the presence of a consensus sequence, HEXXH, located in the C-terminal functional domain of histatin-5, a recognized zinc-binding motif in many proteins. Two-dimensional proton NMR spectroscopy of histatin-5 in a trifluoroethanol/water mixture (a membrane mimetic environment) has been performed and the results analyzed by means of distance geometry and restrained molecular dynamics simulations. Our results reveal that the peptide chain, including the Zn-binding consensus sequence corresponding to residues 15-19, is in a helicoidal conformation. Comparison of the chemical shifts of the individual amino acids in histatin-5 with those recently reported in other solvents indicates that trifluoroethanol/water has a structuring capability somewhere between water and dimethyl sulfoxide. The mechanism of action of this antimicrobial peptide is discussed on the basis of its structural characteristics with particular attention to the Zn-binding motif. |
| تدمد: | 1520-4995 0006-2960 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6f9583011fabee0c33d4776d09c2828Test https://doi.org/10.1021/bi990212cTest |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....a6f9583011fabee0c33d4776d09c2828 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15204995 00062960 |
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