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
Rok vydání: 1996
Předmět:
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