@article{49a866e764054b729468c92f28928225,
title = "Membrane thinning effect of the β-sheet antimicrobial protegrin",
abstract = "Lipid bilayers containing the antimicrobial peptide protegrin-1 (PG-1) were studied by lamellar X-ray diffraction. Previously, we have shown that the peptide exists in two distinct states when associated with lipid bilayers depending on the peptide concentration [Heller, W. T., Waring, A. J., Lehrer, R. I., and Huang, H. W. (1998) Biochemistry 37, 17331-17338]. For concentrations below a lipid-dependent threshold, PG-1 exhibits a unique oriented circular dichroism spectrum called the S state. X-ray experiments show that in this state PG-1 decreases the thickness of the lipid bilayer in proportion to the peptide concentration, similar to alamethicin's membrane thinning effect. This indicates that the S state is adsorbed in the headgroup region of the lipid bilayer, where the peptide is in an inactive state. For PG-1 above the threshold concentration, X-ray diffraction shows that the interaction between the peptide and the bilayer changes significantly. These results suggest that PG-1 has the same concentration-gated mechanism of action as alamethicin.",
author = "Heller, {William T.} and Waring, {Alan J.} and Lehrer, {Robert I.} and Harroun, {Thad A.} and Weiss, {Thomas M.} and Lin Yang and Huang, {Huey W.}",
year = "2000",
month = jan,
day = "11",
doi = "10.1021/bi991892m",
language = "English",
volume = "39",
pages = "139--145",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "1",
}