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Biophys J, January 1999, p. 333-341, Vol. 76, No. 1
Biophysics Group, State Key Laboratory of Biomembrane, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China
The interaction of rabbit C-reactive protein (rCRP) with
a supported monolayer containing a phosphorylcholine moiety was
studied. Three types of phospholipids were synthesized, each containing a insertion spacer of eight, six, or three atoms between the
phosphorylcholine group and hydrophobic tail. By varying the length of
the insertion spacer, we can vary the extension of the
phosphorylcholine group from the membrane surface. By varying the
monolayer composition, we can control the lateral distance between the
exposed phosphorylcholine groups. Using the surface plasmon resonance
technique (SPR), we demonstrated that the calcium-dependent binding of
rCRP to the model membrane is governed not only by the ability of the
ligand to access the binding pocket fully (spacer length), but also by lateral hindrance within the two-dimensional plane of the membrane. The
value of the apparent binding constant was estimated by theoretical analysis, which is obviously dependent on the composition of the lipid
mixture, and a maximum of (9.9 ± 1.5) × 106
M
1 was obtained.
Biophys J, January 1999, p. 333-341, Vol. 76, No. 1
© 1999 by the Biophysical Society 0006-3495/99/01/333/09 $2.00
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