Aluminum binding to phosphatidylcholine lipid bilayer membranes: 27Al and 31P NMR spectroscopic studiesChemistry and Physics of Lipids (2004)
Abstract27Al and 31P nuclear magnetic resonance (NMR) spectroscopies were used to investigate aluminum interactions at pH 3.4 with model membranes composed of 1-palmitoyl 2-oleoyl-sn-glycero-3-phosphocholine (POPC). A solution state 27Al NMR difference assay was developed to quantify aluminum binding to POPC multilamellar vesicles (MLVs). Corresponding one-dimensional (1D) fast magic angle spinning (MAS) 31P NMR spectra showed that aluminum induced the appearance of two new isotropic resonances for POPC shifted to −6.4 ppm and −9.6 ppm upfield relative to, and in slow exchange with, the control resonance at −0.6 ppm. Correlation of the 27Al and 31P NMR binding data revealed a 1:2 aluminum:phospholipid stoichiometry in the aluminum-bound complex at −9.6 ppm and a 1:1 aluminum:phospholipid stoichiometry in that at −6.4 ppm. Slow MAS 31P NMR spectra demonstrated shifts in the anisotropic chemical shift tensor components of the aluminum-bound POPC consistent with a close coordination of aluminum with phosphorus. A model of the aluminum-bis-phospholipid complex is proposed on the basis of these findings.
- Nuclear magnetic resonance,
- Lipid bilayer membranes,
- Aluminum binding
Publication DateNovember, 2004
Citation InformationNeil MacKinnon, Kevin J Crowell, Andrew K Udit and Peter M Macdonald. "Aluminum binding to phosphatidylcholine lipid bilayer membranes: 27Al and 31P NMR spectroscopic studies" Chemistry and Physics of Lipids Vol. 132 Iss. 1 (2004)
Available at: http://works.bepress.com/udit/15/