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, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPE), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) 1,2-dioleoyl-sn-glycero-3-phospho-(1'-myo-inositol-4',5'-bisphosphate) (PIP 2 , purified from porcine brain) were purchased from Avanti Polar Lipids (Alabaster, AL) and were received as organic solutions (chloroform and chloroform/methanol/water for PIP 2, vol.20
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, SMA (3:1) in by UV-vis spectroscopy (Jasco V630 spectrophotometer) by measurement of the absorbance at 260 nm and using a molar extinction coefficient ? 260 = 6989, XIRAN® SL25010 P20) was a kind gift from Polyscope, vol.3
, Organic solvents were then evaporated under a gentle stream of nitrogen to form lipid films. In case of mixtures, evaporation was carried out at 50 °C to ensure lipids miscibility. To remove residual solvent traces, the lipid films were further dried in vacuum at room temperature for at least 16 h. The films were then dissolved into a buffer (Hepes 20 mM, NaCl 140 mM, pH 7.4, or 50 mM pH 7.0) to a concentration of 1 mg/mL and were thoroughly agitated at 50 °C for 30 minutes. The resulting multilamellar vesicle suspensions (MLVs) were then submitted to three freeze and thaw cycles (from liquid nitrogen to 50 °C), the case of POPC/POPE (9:1) and DMPC/DMPE, vol.9
, Finally, lipid concentrations were determined by phosphate quantification, vol.47
, Mandelkow) was used to transform Escherichia coli C41(DE3) (F-ompT hsdSB (rB-mB-) gal dcm (DE3)). Several transformants were grown on 120 mL LB + 1% dextrose, 100 mg/L ampicillin. When the culture reached an optical density OD 650 = 0.52, 10 mL was added to 990 mL of ZYM 5052 medium (1% N-Z-amine, 0.5% yeast extract, 25 mM Na 2 HPO 4 , 25 mM KH 2 PO 4 , 50 mM NH 4 Cl, Production and purification of K18 peptide pNG2 K18, vol.5
, After centrifugation, cell pellets were suspended in 50 mL of 2-(N-morpholino)ethanesulfonic acid (MES) pH 6.8 (20 mM), NaCl (500 mM), ethylenediaminetetraacetic acid (EDTA, 1 mM) phenylmethylsulfonyl fluoride (PMSF, 1mM), benzamidine (2 mM) and dithiothreitol, p.5
, After centrifugation (30 min at 15 000 g), the supernatant was then dialyzed for at least 16 h at 4 °C against cation exchange buffer A (20 mM MES pH 6.8, EDTA 1 mM, NaCl 50 mM, DTT (1 mM) with a Spectra/Por Dialysis Membrane (MWCO 3.5 kDa). The dialysate was then cleared (30 min, 15 000g), filtered through a 0.22 µm membrane and apply onto an HiTrap SP (GE Healthcare) equilibrated with the cation exchange buffer A. After washing with 25 mL of the same buffer, the protein was eluted with 25 mL of Buffer B (MES 20 mM pH 6.8, EDTA 1 mM, NaCl 150 mM) and the 5 mL fractions containing most of K18 were pooled and concentrated by ultrafiltration devices (e.g., Ultrafree, Millipore 5 kDa MWCO) to a final volume of 0.5 to 1 mL. Finally, the peptide concentrate was applied onto a gel filtration column (Superdex-75), sonicated four times (1 min cycles on ice; output 5, 50 % duty cycle) and then heated at 80 °C for 20 min
, Negative staining for transmission electron microscopy For EM grid preparations, the sample suspension diluted at 50 µg/mL for LUVs or 2
, Images were recorded under low-dose conditions on transmission electron microscope (Tecnai F20 or CM120, ThermoFischer) using a ThermoFisher Eagle 4k_4k or a GATAN UltraScan
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