Multivalent ligand-receptor binding on supported lipid bilayers

Hyunsook Jung, Aaron D. Robison, Paul S. Cremer

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

Fluid supported lipid bilayers provide an excellent platform for studying multivalent protein-ligand interactions because the two-dimensional fluidity of the membrane allows for lateral rearrangement of ligands in order to optimize binding. Our laboratory has combined supported lipid bilayer-coated microfluidic platforms with total internal reflection fluorescence microscopy (TIRFM) to obtain equilibrium dissociation constant (KD) data for these systems. This high throughput, on-chip approach provides highly accurate thermodynamic information about multivalent binding events while requiring only very small sample volumes. Herein, we review some of the most salient findings from these studies. In particular, increasing ligand density on the membrane surface can provide a modest enhancement or attenuation of ligand-receptor binding depending upon whether the surface ligands interact strongly with each other. Such effects, however, lead to little more than one order of magnitude change in the apparent KD values. On the other hand, the lipophilicity and presentation of lipid bilayer-conjugated ligands can have a much greater impact. Indeed, changing the way a particular ligand is conjugated to the membrane can alter the apparent KD value by at least three orders of magnitude. Such a result speaks strongly to the role of ligand availability for multivalent ligand-receptor binding.

Original languageEnglish (US)
Pages (from-to)90-94
Number of pages5
JournalJournal of Structural Biology
Volume168
Issue number1
DOIs
StatePublished - Oct 2009

All Science Journal Classification (ASJC) codes

  • Structural Biology

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