Secondary structure and location of a magainin analogue in synthetic phospholipid bilayers

被引:120
作者
Hirsh, DJ
Hammer, J
Maloy, WL
Blazyk, J
Schaefer, J
机构
[1] WASHINGTON UNIV, DEPT CHEM, ST LOUIS, MO 63130 USA
[2] OHIO UNIV, COLL OSTEOPATH MED, DEPT CHEM, ATHENS, OH 45701 USA
[3] MAGAININ PHARMACEUT INC, PLYMOUTH MEETING, PA 19462 USA
关键词
D O I
10.1021/bi961468a
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. Ala(19)-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 Ala(19)-magainin 2 amide is bound near the phospholipid head groups.
引用
收藏
页码:12733 / 12741
页数:9
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