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Interaction of poly(l-lysines) with negatively charged membranes: an FT-IR and DSC study

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Abstract

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 α-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 α-helix to random coil.

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Abbreviations

DPPC:

1,2-Dipalmitoyl-sn-glycero-3-phosphocholine

DPPG:

1,2-Dipalmitoyl-sn-glycero-3-phosphoglycerol

DMPG:

1,2-Myristoyl-sn-glycero-3-phosphoglycerol

PS:

Phosphatidylserine

PA:

Phosphatidic acid

PLL:

Poly(l-lysine)

DSC:

Differential scanning calorimetry

FT-IR:

Fourier transform infrared spectroscopy

CD:

Circular dichroism

NMR:

Nuclear magnetic resonance

ESR:

Electron spin resonance

FRET:

Fluorescent resonance energy transfer

FCS:

Fluorescence correlation spectroscopy

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Acknowledgment

This work was supported by the Fonds der Chemischen Industrie.

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Correspondence to Alfred Blume.

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Dedicated to Prof. K. Arnold on the occasion of his 65th birthday.

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Schwieger, C., Blume, A. Interaction of poly(l-lysines) with negatively charged membranes: an FT-IR and DSC study. Eur Biophys J 36, 437–450 (2007). https://doi.org/10.1007/s00249-006-0080-8

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