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Biophys J, February 2001, p. 822-831, Vol. 80, No. 2
*Institute of Medical Physics and Biophysics, University of
Leipzig, D-04103 Leipzig; and Humboldt-University Berlin,
Institute of Biology/Biophysics, D-10115 Berlin, Germany
Location and dynamic reorientation of the fluorophore
7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD) covalently attached to a short (C6) or a long (C12) sn2 acyl chain of a
phosphatidylcholine molecule was investigated by fluorescence and
solid-state NMR spectroscopy. 2H NMR lipid chain order
parameters indicate a perturbation of the phospholipid packing density
in the presence of NBD. Specifically, a decrease of molecular order was
found for acyl chain segments of the lower, more hydrophobic region.
Molecular collision probabilities determined by 1H magic
angle spinning nuclear Overhauser enhancement spectroscopy indicate a
highly dynamic reorientation of the probe in the membrane due to
thermal fluctuations. A broad distribution of the fluorophore in the
lipid bilayer is observed with a preferential location in the upper
acyl chain/glycerol region. The distribution of the NBD group in the
membrane is quite similar for both the long- and the short-chain
analog. However, a slight preference of the NBD group for the
lipid-water interface is found for C12-NBD-PC in comparison with
C6-NBD-PC. Indeed, as shown by dithionite fluorescence assay, the
long-chain analog reacts more favorably with dithionite, indicating a
better accessibility of the probe by dithionite present in the aqueous
phase. Forces determining the location of the fluorophore in the lipid
water interface are discussed.
Biophys J, February 2001, p. 822-831, Vol. 80, No. 2
© 2001 by the Biophysical Society 0006-3495/01/02/822/10 $2.00
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