Abstract
Three dermaseptins, DS 01, DD K, and DD L, were compared with respect to their structural features and interactions with liposomes. Circular dichroic spectra at alcohols of different chain lengths revealed that DS 01 has the higher helicogenic potential in hydrophobic media. Binding of DS 01, DD K, and DD L to liposomes induced significant blue shifts of the emission spectra of the single tryptophan located at position 3 of all sequences indicating association of the peptides with bilayers. Kinetics evaluation of atomic force microscopy images evidenced the strong fusogenic activity of DS 01 whereas DD K and DD L showed increased lytic activities.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohols / pharmacology
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Amino Acid Sequence
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Amphibian Proteins / chemistry*
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Amphibian Proteins / metabolism*
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Animals
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / metabolism*
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Anura
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Circular Dichroism
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Kinetics
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Liposomes / metabolism*
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Membrane Fusion / physiology*
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Microscopy, Atomic Force
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Microscopy, Fluorescence
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Molecular Sequence Data
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Protein Binding
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Protein Structure, Secondary / drug effects
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Structure-Activity Relationship
Substances
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Alcohols
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Amphibian Proteins
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Antimicrobial Cationic Peptides
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Liposomes
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dermadistinctin K, Phyllomedusa distincta
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dermaseptin