Affordable Access

Solid-state NMR investigations of interaction contributions that determine the alignment of helical polypeptides in biological membranes.

Authors
  • Bechinger, B
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Aug 31, 2001
Volume
504
Issue
3
Pages
161–165
Identifiers
PMID: 11532448
Source
Medline
License
Unknown

Abstract

Helical peptides reconstituted into oriented phospholipid bilayers were studied by proton-decoupled 15N solid-state NMR spectroscopy. Whereas hydrophobic channel peptides, such as the N-terminal region of Vpu of HIV-1, adopt transmembrane orientations, amphipathic peptide antibiotics are oriented parallel to the bilayer surface. The interaction contributions that determine the alignment of helical peptides in lipid membranes were analysed using model sequences, and peptides that change their topology in a pH-dependent manner have been designed. The energy contributions of histidines, lysines, leucines and alanines as well as the alignment of peptides and phospholipids under conditions of hydrophobic mismatch have been investigated in considerable detail.

Report this publication

Statistics

Seen <100 times