Abstract
In recent years, several endogenous mammalian antibacterial peptides have been described. An amphipathic cationicalpha-helix is a common feature in many cases; therefore, other peptides with this characteristic might also possess antibiotic activity. In fact, a 30-mer peptide of apoprotein E 133-162 (LRVRLASHLRKLRKRLLRDADDLQKRLAVY) was found to have antibiotic activity comparable to those of a classic antibiotic (Gentamicin) and a neutrophil-derived antibiotic peptide (CAP18). Calculation of cationicity, hydrophobicity, and hydrophobic moment and the helical wheel diagram of apoprotein E 133-162 revealed close similarities to CAP18.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides*
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Apolipoproteins E / chemistry*
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Apolipoproteins E / pharmacology*
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Bacteria / drug effects*
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Carrier Proteins / pharmacology
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Cathelicidins
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Drug Resistance, Multiple
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Escherichia coli / drug effects
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Gentamicins / pharmacology
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Humans
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology*
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Protein Structure, Secondary
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Pseudomonas aeruginosa / drug effects
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Salmonella / drug effects
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Staphylococcus aureus / drug effects
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Apolipoproteins E
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Carrier Proteins
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Cathelicidins
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Gentamicins
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Peptide Fragments