Neutron diffraction studies of amphipathic helices in phospholipid bilayers.

J. P. Bradshaw, K. C. Duff, P. J. Gilchrist, A. M. Saxena

Research output: Chapter or section in a book/report/conference proceedingChapter or section

5 Citations (SciVal)


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.

Original languageEnglish
Title of host publicationNeutrons in Biology
EditorsB. P. Schoenborn, R. B. Knott
Number of pages12
ISBN (Electronic)978-1-4615-5847-7
Publication statusPublished - 1 Jan 1996

Publication series

NameBasic life sciences
ISSN (Print)0090-5542

ASJC Scopus subject areas

  • Medicine(all)


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