Abstract
Temporin A (TA) and a cecropin A-temporin A hybrid peptide (CATA) were synthesized and assayed for their hemolytic, anticoagulant, and antifungal properties. CATA retains significant antifungal activity, is less hemolytic than TA, and inhibits blood coagulation. These results recommend further studies of the biological activities of CATA.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acids / chemistry
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / pharmacology*
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Antifungal Agents / chemistry
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Antifungal Agents / pharmacology*
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / pharmacology*
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Blood Coagulation / drug effects
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Erythrocytes / metabolism
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Hemolysis
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Humans
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Molecular Sequence Data
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Peptide Biosynthesis
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Peptides / chemistry
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Protein Structure, Tertiary
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Proteins / chemistry
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Proteins / pharmacology*
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Prothrombin / chemistry
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Prothrombin / pharmacology
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Thromboplastin / chemistry
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Thromboplastin / pharmacology
Substances
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Amino Acids
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Anti-Infective 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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temporin
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cecropin A
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Prothrombin
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Thromboplastin