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Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy

✍ Scribed by Burkhard Bechinger; Michael Zasloff; Stanley J. Opella

Publisher
Cold Spring Harbor Laboratory Press
Year
1993
Tongue
English
Weight
729 KB
Volume
2
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One‐ and two‐dimensional solid‐state ^15^N NMR spectra of specifically ^15^N‐labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is α‐helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.

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