PMID: 2525918Apr 4, 1989Paper

Conformations and orientations of a signal peptide interacting with phospholipid monolayers

Biochemistry
D G CornellL M Gierasch

Abstract

The interaction of a chemically synthesized 25-residue signal peptide of LamB protein from Escherichia coli with phospholipids has been studied with a film balance technique. The conformation, orientation, and concentration of the peptides in lipid monolayers have been determined from polarized infrared spectroscopy, ultraviolet spectroscopy, and assay of 14C-labeled peptide in transferred films. When the LamB signal peptide is injected into the subphase under a phosphatidylethanolamine-phosphatidylglycerol monolayer at low initial pressure, insertion of a portion of the peptide into the lipid film is evidenced by a rapid rise in film pressure. Spectroscopic results obtained on films transferred to quartz plates and Ge crystals show that the peptide is a mixture of alpha-helix and beta-conformation where the long axis of the alpha-helix penetrates the monolayer plane and the beta-structure is coplanar with the film. By contrast, when peptide is injected under lipid at high initial pressure, no pressure rise is observed, and the spectroscopic results show the presence of only beta-structure which is coplanar with the monolayer. The spectroscopic and radioassay results are all consistent with the picture of a peptide anchored to ...Continue Reading

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Citations

Sep 6, 1994·Chemistry and Physics of Lipids·P K KinnunenP Mustonen
Jan 1, 1991·The International Journal of Biochemistry·T Cserháti, M Szögyi
Jan 1, 1999·Chemistry and Physics of Lipids·L Silvestro, P H Axelsen
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