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The Molecular Mechanics of P- and L-Selectin Lectin Domains Binding to PSGL-1

Department of Biomedical Engineering, University of Virginia, Charlottesville, Virginia

Correspondence: Address reprint requests to William H. Guilford, Box 800759, University of Virginia, Charlottesville, VA 22908. Tel.: 434-243-2740; E-mail: guilford{at}virginia.edu.

A laser trap was used to compare the load-dependent binding kinetics between truncated P- and L-selectin to their natural ligand, P-selectin glycoprotein ligand-1 (PSGL-1) over the predicted physiological range of loading rates. Human PSGL-1 was covalently coupled to polystyrene beads. Chimeric selectins were adsorbed to nitrocellulose-coated glass beads on a coverslip. A PSGL-1 bead was held in a laser trap and touched to a vertical surface of the glass bead, allowing a bond to form between selectin and ligand. The surface was moved away from the microsphere, applying load at a constant rate until bond rupture. Rupture force for both selectins increased with loading rate, but significant differences in rupture force between P- and L-selectin were observed only above 460 pN/s. These data are best represented as two energy barriers to unbinding, with the transition from the low to high loading rate regime at 260–290 pN/s. The data also allow the first estimate of a two-dimensional specific on-rate for binding of these two selectins to their natural ligand (1.7 µm²/s). These data suggest that P- and L-selectin lectin domains have very similar kinetics under physiological conditions.

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