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

FEBS Letters

Bechinger, Burkhard¹ 

[1] Max-Planck-Institute for Biochemistry, Am Klopferspitz 18A, 82152 Martinsried, Germany

关键词: Oriented bilayer;    Transmembrane polypeptide;    Amphipathic peptide;    Membrane equilibrium;    Hydrophobicity scale;    Interface;    di-C10:0-PC;    1;    2-dicapryl-sn-glycero-3-phosphocholine;    HIV;    human immunodeficiency virus;    IP;    in-plane (alignment);    NMR;    nuclear magnetic resonance;    POPC;    1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine;    TM;    transmembrane (alignment);   

DOI  :  10.1016/S0014-5793(01)02741-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown