Secondary Structure and Location of a Magainin Analogue in Synthetic Phospholipid Bilayers
Autor: | Jacob Schaefer, Donald J. Hirsh, Janet L. Hammer, Jack Blazyk, W L Maloy |
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Rok vydání: | 1996 |
Předmět: |
Staphylococcus aureus
Magnetic Resonance Spectroscopy Lipid Bilayers Molecular Sequence Data Population Phospholipid Xenopus Proteins Magainins Biochemistry Protein Structure Secondary chemistry.chemical_compound Amide Spectroscopy Fourier Transform Infrared Escherichia coli Amino Acid Sequence Lipid bilayer education Protein secondary structure Phospholipids education.field_of_study Temperature Magainin Nuclear magnetic resonance spectroscopy Anti-Bacterial Agents Crystallography chemistry Dipalmitoylphosphatidylcholine Pseudomonas aeruginosa Peptides Antimicrobial Cationic Peptides Protein Binding |
Zdroj: | Biochemistry. 35:12733-12741 |
ISSN: | 1520-4995 0006-2960 |
DOI: | 10.1021/bi961468a |
Popis: | Magainins are cationic, membrane-active peptides which show broad-spectrum antimicrobial activity. We have investigated the secondary structure and location of an analogue of magainin 2 in synthetic phospholipid bilayers using a combination of Fourier transform infrared (FTIR) spectroscopy and solid-state nuclear magnetic resonance (NMR) spectroscopy. Ala19-magainin 2 amide exhibits both alpha-helix and beta-sheet secondary structures in lipid bilayers containing either dipalmitoylphosphatidylglycerol (DPPG) or a 1:1 molar mixture of DPPG and dipalmitoylphosphatidylcholine (DPPC). The combination of FTIR and solid-state NMR results suggests that there are two populations of peptide. The secondary structure of one population is alpha-helix while that of the other population is beta-sheet. We demonstrate that the solid-state NMR technique, rotational-echo double resonance (REDOR), can be used to measure both intra- and intermolecular dipole-dipole interactions in membrane-bound peptides. Our REDOR experiments indicate that alpha-helical Ala19-magainin 2 amide is bound near the phospholipid head groups. |
Databáze: | OpenAIRE |
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