Abstract
All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic alpha-helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.
MeSH terms
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Amino Acid Sequence
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Anti-Infective Agents / chemistry*
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Antimicrobial Cationic Peptides*
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Chymotrypsin
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Hemolysis / drug effects
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Humans
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Indicators and Reagents
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Magainins
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Microbial Sensitivity Tests
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / isolation & purification
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Peptides / chemical synthesis
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Peptides / chemistry*
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Peptides / pharmacology
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Protein Conformation
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Stereoisomerism
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Trypsin
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Xenopus Proteins*
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Indicators and Reagents
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Magainins
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Peptide Fragments
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Peptides
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Xenopus Proteins
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magainin 2 peptide, Xenopus
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Chymotrypsin
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Trypsin