Interaction of poly(L-lysines) with negatively charged membranes: an FT-IR and DSC study.
The influence of the binding of poly(L-lysine) (PLL) to negatively charged membranes containing phosphatidylglycerols (PG) was studied by DSC and FT-IR spectroscopy. We found a general increase in the main transition temperature as well as increase in hydrophobic order of the membrane upon PLL binding. Furthermore we observed stronger binding of hydration water to the lipid head groups after PLL binding. The secondary structure of the PLL after binding was studied by FT-IR spectroscopy. We found that PLL binds in an alpha-helical conformation to negatively charged DPPG membranes or membranes with DPPG-rich domains. Moreover we proved that PLL binding induces domain formation in the gel state of mixed DPPC/DPPG or DMPC/DPPG membranes as well as lipid remixing in the liquid-crystalline state. We studied these effects as a function of PLL chain length and found a significant dependence of the secondary structure, phase transition temperature and domain formation capacity on PLL chain length and also a correlation between the peptide secondary structure and the phase transition temperature of the membrane. We present a system in which the membrane phase transition triggers a highly cooperative secondary structure transition of the membrane-bound peptide from alpha-helix to random coil.
Schwieger
Christian
C
Institute of Physical Chemistry, Martin-Luther-University Halle-Wittenberg, Halle, Germany.
Blume
Alfred
A
D001665:Binding Sites; D002152:Calorimetry, Differential Scanning / Q000379:methods; D008051:Lipid Bilayers / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D008564:Membrane Potentials; D008968:Molecular Conformation; D010715:Phosphatidylglycerols / Q000737:chemistry*; D011107:Polylysine / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D055672:Static Electricity
D008051:Lipid Bilayers; D008081:Liposomes; D010715:Phosphatidylglycerols; D011107:Polylysine