Interaction of tachykinins with phospholipid membranes: A neutron diffraction study

Malcolm J.M. Darkes, Sarah M.A. Davies, Jeremy P. Bradshaw

Research output: Contribution to journalArticlepeer-review

2 Citations (SciVal)


Tachykinins are a group of peptides which bind to G-protein-coupled receptors. Receptor affinity appears to depend on different secondary structures of tachykinin which share the same Hydrophobic carboxy-terminal sequence, FXGLM. Receptor activation is thought to be due to the carboxy-terminal submerging into the bilayer and the amino-terminal binding on the surface. Binding of tachykinins to phospholipid bilayers may take place both on the aqueous membrane surface and in the hydrophobic region. The two-state equilibrium appears to depend on the surface charge of the membrane. Deuterating substance P and neurokinin A at their carboxy-terminals, our results show two populations of label for each peptide. One is very close to the water-hydrocarbon interface, the other some 13 Å deeper. We report that the bilayer location of the two tachykinins is remarkably similar, thereby inferring that receptor specificity must be controlled by finer levels of structure.

Original languageEnglish
Pages (from-to)1144-1147
Number of pages4
JournalPhysica B: Condensed Matter
Publication statusPublished - 1 Jan 1997


  • Neurokinin A
  • Neutron diffraction
  • Substance P
  • Tachykinins

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Electrical and Electronic Engineering


Dive into the research topics of 'Interaction of tachykinins with phospholipid membranes: A neutron diffraction study'. Together they form a unique fingerprint.

Cite this