Abstract
The human airways are protected from pathogenic colonization by a blanket of fluid impregnated with innate antimicrobial effector molecules. Among several previously uncharacterized components, we isolated a peptide that had activity primarily targeting Gram-negative bacteria. We named the peptide 'calcitermin' since its amino acid sequence and mass were equivalent to the 15 C-terminal residues of the S100 protein, calgranulin C. The antimicrobial activity of calcitermin was enhanced in acidic buffers (pH 5.4) and in the presence of micromolar concentrations of ZnCl(2). Analysis revealed a putative zinc-binding consensus sequence as well as an alpha-helical conformation in structure-promoting solvents.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / isolation & purification*
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Anti-Bacterial Agents / pharmacology
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Antimicrobial Cationic Peptides
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Circular Dichroism
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Escherichia coli / drug effects
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Humans
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Hydrogen-Ion Concentration
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Listeria monocytogenes / drug effects
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Nasal Mucosa / metabolism*
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification*
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Peptide Fragments / pharmacology
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Peptides
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Protein Conformation
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S100 Proteins / chemistry
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S100 Proteins / isolation & purification*
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S100 Proteins / pharmacology
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Sequence Homology, Amino Acid
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Spectrophotometry, Atomic
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Zinc / pharmacology
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Peptide Fragments
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Peptides
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S100 Proteins
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calcitermin peptide, human
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Zinc