Abstract
Temporin A, 18 analogs, and a cecropin A-temporin A hybrid peptide were tested with antibiotic sensitive and resistant bacteria, fungi, human erythrocytes, and in clotting assays. Several peptides were active in these assays, and some analogs (D-TA, W1-TA, and Con-L4,G10) may be useful lead compounds for further antibiotics development. The activity of temporin A was found to be dependent upon several of its structural features, including amino acid composition and sequence, chirality, helicity, and positive charge.
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.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology*
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Antifungal Agents / chemistry
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / pharmacology*
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Biological Assay
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Hemolysis / drug effects
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Humans
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Peptides / chemistry
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Proteins / chemistry
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Proteins / pharmacology*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / pharmacology*
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Structure-Activity Relationship
Substances
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Anti-Bacterial Agents
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Antifungal Agents
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Antimicrobial Cationic Peptides
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Peptides
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Proteins
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Recombinant Fusion Proteins
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temporin
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cecropin A