Neutron diffraction studies of amphipathic helices in phospholipid bilayers.
The structural feature which is thought to facilitate the interaction of many peptides with phospholipid bilayers is the ability to fold into an amphipathic helix. In most cases the exact location and orientation of this helix with respect to the membrane is not known, and may vary with factors such as pH and phospholipid content of the bilayer. The growing interest in this area is stimulated by indications that similar interactions can contribute to the binding of certain hormones to their cell-surface receptors. We have been using the techniques of neutron diffraction from stacked phospholipid bilayers in an attempt to investigate this phenomenon with a number of membrane-active peptides. Here we report some of our findings with three of these: the bee venom melittin; the hormone calcitonin; and a synthetic peptide representing the ion channel fragment of influenza A M2 protein.
Bradshaw
J P
JP
Department of Preclinical Veterinary Sciences, University of Edinburgh, Summerhall, United Kingdom.
Duff
K C
KC
Gilchrist
P J
PJ
Saxena
A M
AM
D000595:Amino Acid Sequence; D002116:Calcitonin / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus; D007473:Ion Channels / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008555:Melitten / Q000737:chemistry*; D008961:Models, Structural; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009502:Neutrons; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D014763:Viral Matrix Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction; D000086082:Viroporin Proteins
D002116:Calcitonin; D007473:Ion Channels; D008051:Lipid Bilayers; D008555:Melitten; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins