Abstract
High-resolution structure elucidation has been challenging for the large group of host-defense peptides that form helices on or within membranes but do not manifest a strong folding propensity in aqueous solution. Here we report the crystal structure of an analogue of the widely studied host-defense peptide magainin 2. Magainin 2 (S8A, G13A, G18A) is a designed variant that displays enhanced antibacterial activity relative to the natural peptide. The crystal structure of magainin 2 (S8A, G13A, G18A), obtained for the racemic form, features a dimerization mode that has previously been proposed to play a role in the antibacterial activity of magainin 2 and related peptides.
Publication types
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Research Support, N.I.H., Extramural
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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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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology*
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Bacillus subtilis / drug effects
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Crystallography, X-Ray
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Dimerization
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Dose-Response Relationship, Drug
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Enterococcus faecium / drug effects
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Escherichia coli / drug effects
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Magainins / chemical synthesis
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Magainins / chemistry
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Magainins / metabolism*
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Microbial Sensitivity Tests
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Models, Molecular
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Phenylalanine / chemistry*
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Staphylococcus aureus / drug effects
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Structure-Activity Relationship
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Xenopus Proteins / chemical synthesis
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Xenopus Proteins / chemistry
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Xenopus Proteins / metabolism*
Substances
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Anti-Bacterial Agents
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Magainins
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Xenopus Proteins
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magainin 2 peptide, Xenopus
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Phenylalanine