TY - JOUR
T1 - Gp120 binds cooperatively to several biologically relevant glycosphingolipids
T2 - Quantitative measurements at equilibrium by total internal reflection fluorescence microscopy
AU - Conboy, John C.
AU - McReynolds, Katherine D.
AU - Gervay-Hague, Jacquelyn
AU - Saavedra, S. Scott
PY - 2000/8/18
Y1 - 2000/8/18
N2 - The binding of The HIV-1 surface glycoprotein gp120 to several glycosphingolipides, reconstituted into planar lipid bilayers (see scheme; small circle= 2-oleoyl-1-palmitoylphosphatidylcholine (POPC), arrow = glycosylceramide recognition element; left: low and right: high protein concentrations), has been quantitatively measured under quilibrium conditions. Complex binding behavior was observed, which suggests that the induced aggregation of gp120 molecules at a ligand-bearing membrane surface may be an important step in the mechanism of HIV-1 infection of a host cell.
AB - The binding of The HIV-1 surface glycoprotein gp120 to several glycosphingolipides, reconstituted into planar lipid bilayers (see scheme; small circle= 2-oleoyl-1-palmitoylphosphatidylcholine (POPC), arrow = glycosylceramide recognition element; left: low and right: high protein concentrations), has been quantitatively measured under quilibrium conditions. Complex binding behavior was observed, which suggests that the induced aggregation of gp120 molecules at a ligand-bearing membrane surface may be an important step in the mechanism of HIV-1 infection of a host cell.
KW - Fluorescence spectroscopy
KW - Glycolipids
KW - Structure-activity relationships
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U2 - 10.1002/1521-3773(20000818)39:16
DO - 10.1002/1521-3773(20000818)39:16
M3 - Article
SN - 1433-7851
VL - 39
SP - 2882
EP - 2884
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 16
ER -