Abstract
Skin secretions of amphibia of the Bombina genus contain two families of antimicrobial peptides, the bombinins (bombinin-like peptides) and the bombinins H (H for hydrophobic and hemolytic). The latter family includes a number of peptides containing a D-amino acid in the second position, in addition to their corresponding all L-isomers. The antimicrobial activity of three pairs of bombinin H isomers, H2/H4, H6/H7 and GH-1D/GH-1L, has been investigated. The first two pairs of peptides were actually isolated from the secretion, whereas the third was synthesized according to the sequence deduced from a gene coding for a bombinin-like peptide in Bombina orientalis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry
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Animals
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Anti-Bacterial Agents / pharmacology
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Antimicrobial Cationic Peptides
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Anura
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Cell Membrane / drug effects
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Cytoplasm / metabolism
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Dose-Response Relationship, Drug
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Erythrocytes / drug effects
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Escherichia coli / drug effects
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Humans
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Peptides / chemistry*
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Peptides / metabolism
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Peptides / physiology
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Potassium / metabolism
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Skin / metabolism*
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Stereoisomerism
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Structure-Activity Relationship
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Time Factors
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Yersinia pseudotuberculosis / drug effects
Substances
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Amino Acids
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Peptides
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gene-drived bombinin H-like peptide
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Potassium