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- W2024009212 abstract "The effect of gramicidin S (GS) on acyl chain dynamics of 14-doxylstearic acid spin label (14-SASL) monitoring the centre of dimyristoylphosphatidylcholine (DMPC) bilayers was studied with electron paramagnetic resonance (EPR) spectroscopy. The chain-melting transition of DMPC was shifted down and broadened monotonously by several degrees with increasing peptide concentration in the range of lipid/peptide ratios of l/p=5/1–15/1. The effective rotational correlation time τeff of 14-SASL became larger with increasing amounts of peptide bound to fluid membranes of DMPC. From the dependence of τeff on the lipid/peptide molar ratio it was estimated that about 10 DMPC molecules per monomer GS are involved in non-covalent peptide–lipid interaction. Optimized spectral subtractions showed that, well above the chain-melting transition, 90% of the EPR spectral intensity of the spin-labeled peptide–lipid complex (l/p=5/1) originated from spectra recorded in bilayers (without peptide) at lower temperature. This was not the case 6°C above the phase transition where two components with comparable intensities were detected. The two components were identified as different motional modes of the label molecules, rather than distinct mobile/immobile lipid populations." @default.
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- W2024009212 date "2001-05-01" @default.
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- W2024009212 title "Spin label EPR studies of the effect of gramicidin S on lipid chain dynamics" @default.
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- W2024009212 doi "https://doi.org/10.1016/s0022-2860(00)00832-2" @default.
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