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Headgroup structure and fatty acid chain length of the acidic phospholipids modulate the interaction of membrane mimetic vesicles with the antimicrobial peptide protegrin‐1
Author(s) -
Jing Weiguo,
Prenner Elmar J.,
Vogel Hans J.,
Waring Alan J.,
Lehrer Robert I.,
Lohner Karl
Publication year - 2005
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.702
Subject(s) - liposome , chemistry , vesicle , peptide , phospholipid , membrane , thermotropic crystal , biophysics , antimicrobial peptides , biological membrane , biochemistry , stereochemistry , phase (matter) , organic chemistry , biology , liquid crystalline
The interaction of protegrin‐1 (PG‐1), a small β‐sheet antimicrobial peptide with acidic phospholipid model membranes was investigated by differential scanning calorimetry. We found that PG‐1 can distinguish between liposomes of the anionic phospholipids DPPG, DPPS and DPPA, eventhough the headgroups of these phospholipids all have the same net charge and they carry the same hydrocarbon chains. Specifically, PG‐1 had only a minor effect on the thermotropic phase behavior of DPPA liposomes, while it interacted preferentially with the fluid phase of DPPS. Furthermore, PG‐1 could induce a phase separation in DPPG liposomes resulting in the formation of peptide‐rich domains even at low concentrations of the peptide. However, this peptide‐rich domain was not evident when the fatty acyl chains were longer or shorter by two carbon atoms. In addition, PG‐1 can also form peptide‐rich domains in DPPS vesicles but only at high concentrations of the peptide. These results suggest that in addition to an overall negative charge, the structural features of the phospholipid headgroups, lipid packing and thus membrane fluidity will influence the interaction with PG‐1, thereby modulating its biological activity. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.