Abstract
A potent and structurally novel antimicrobial peptide was isolated and characterized from the stomach tissue of Bufo bufo gargarizans, an Asian toad. The 39-amino acid peptide, named buforin I, was purified to homogeneity by heparin-affinity column and reverse-phase HPLC. The amino acid sequence of buforin I was identical in 37 of 39 amino-terminal residues of Xenopus histone H2A. The buforin I showed strong antimicrobial activities in vitro against a broad-spectrum of microorganisms and was found to be more potent than magainin 2. In addition, a 21-amino acid peptide, named buforin II, which was derived from buforin I, showed more potent antimicrobial activities than buforin I.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-Bacterial Agents
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / isolation & purification*
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Anti-Infective Agents / pharmacology
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Bufo bufo*
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Chromatography, Affinity
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Chromatography, High Pressure Liquid
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Fungi / drug effects
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Gram-Negative Bacteria / drug effects
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Gram-Positive Bacteria / drug effects
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Histones / chemistry
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Molecular Weight
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Proteins / chemistry
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Proteins / isolation & purification*
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Proteins / pharmacology
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Sequence Homology, Amino Acid
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Stomach / chemistry*
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Xenopus
Substances
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Anti-Bacterial Agents
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Anti-Infective Agents
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Histones
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Proteins
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buforin I
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buforin II