Two-dimensional (2D) kinetics of receptor-ligand interactions governs cell adhesion in many biological processes. While the dissociation kinetics of receptor-ligand bond is extensively investigated, the association kinetics has much less been quantified. Recently receptor-ligand interactions between two surfaces were investigated using a thermal fluctuation assay upon biomembrane force probe technique (Chen et al. in Biophys J 94:694-701, 2008). The regulating factors on association kinetics, however, are not well characterized. Here we developed an alternative thermal fluctuation assay using optical trap technique, which enables to visualize consecutive binding-unbinding transition and to quantify the impact of microbead diffusion on receptor-ligand binding. Three selectin constructs (sLs, sPs, and PLE) and their ligand P-selectin glycoprotein ligand 1 were used to conduct the measurements. It was indicated that bond formation was reduced by enhancing the diffusivity of selectin-coupled carrier, suggesting that carrier diffusion is crucial to determine receptor-ligand binding. It was also found that 2D forward rate predicted upon first-order kinetics was in the order of sPs > sLs > PLE and bond formation was history-dependent. These results further the understandings in regulating association kinetics of surface-bound receptor-ligand interactions.
Sun GY,Zhang Y,Huo B,et al. Surface-Bound Selectin-Ligand Binding Is Regulated By Carrier Diffusion[J]. European Biophysics Journal With Biophysics Letters,2009:701-711.
APA
孙淦云,章燕,霍波,龙勉,&Long M.(2009).Surface-Bound Selectin-Ligand Binding Is Regulated By Carrier Diffusion.European Biophysics Journal With Biophysics Letters,701-711.
MLA
孙淦云,et al."Surface-Bound Selectin-Ligand Binding Is Regulated By Carrier Diffusion".European Biophysics Journal With Biophysics Letters (2009):701-711.
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