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• W2022229739 endingPage "2910" @default.
• W2022229739 startingPage "2904" @default.
• W2022229739 abstract "High-resolution 31P magic angle spinning (MAS) NMR spectroscopy is presented as a direct and non-perturbing method for measuring changes in surface charge density occurring in mixed phospholipid membranes upon binding of charged surface-active peptides. 31P MAS NMR was used to investigate mixed lipid membranes of neutral phosphatidylcholine and negatively charged phosphatidylglycerol where the molar fraction of the charged lipid was varied from 0 to 1. The chemical shifts of the individual membrane lipids showed a simple variation in response to changes in the fraction of the negatively charged component phosphatidylglycerol. Addition of the positively charged amyloid-β1-40 peptide, a key substance in Alzheimer's disease, resulted in changes in the isotropic chemical shifts of the membrane lipid phosphates in a way consistent with reduction in the negative surface charge of the mixed lipid bilayers. Binding of different amounts of the positively charged peptide pentalysine to L-α-dioleoylphosphatidylcholine/L-α-dioleoylphosphatidylglycerol (DOPC/DOPG) vesicles (2:1 molar ratio) also showed a systematic variation of both chemical shift values. These changes were described by a simple two-site model and indicate purely electrostatic binding of pentalysine." @default.
• W2022229739 created "2016-06-24" @default.
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• W2022229739 date "2001-01-01" @default.
• W2022229739 modified "2023-09-23" @default.
• W2022229739 title "Electrostatic peptide–lipid interactions of amyloid-β peptide and pentalysine with membrane surfaces monitored by 31P MAS NMR" @default.
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• W2022229739 doi "https://doi.org/10.1039/b103352m" @default.
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