Abstract
Temporin A and structurally related peptides produced in amphibian dermal granular glands and in wasp venom were tested for growth inhibition of Batrachochytrium dendrobatidis, a pathogen associated with global amphibian declines. Two natural amphibian temporins, a wasp temporin, and six synthetic analogs effectively inhibited growth. Differences in potency due to amino acid substitution suggest that ability to penetrate membranes and form an alpha-helical structure is important for their effectiveness against this pathogen.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Substitution
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Amphibians / microbiology*
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Animal Diseases / transmission*
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Animals
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Anti-Infective Agents / chemical synthesis
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / pharmacology*
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Antimicrobial Cationic Peptides
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Fungi / drug effects*
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Fungi / growth & development
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Microbial Sensitivity Tests
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Mycoses / transmission
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Mycoses / veterinary*
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Population
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Proteins / chemical synthesis
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Proteins / chemistry
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Proteins / pharmacology*
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Wasp Venoms / chemistry
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Proteins
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Wasp Venoms
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temporin