Direct measurement of a tethered ligand-receptor interaction potential

Science. 1997 Feb 7;275(5301):820-2. doi: 10.1126/science.275.5301.820.

Abstract

Many biological recognition interactions involve ligands and receptors that are tethered rather than rigidly bound on a cell surface. A surface forces apparatus was used to directly measure the force-distance interaction between a polymer-tethered ligand and its receptor. At separations near the fully extended tether length, the ligands rapidly lock onto their binding sites, pulling the ligand and receptor together. The measured interaction potential and its dynamics can be modeled with standard theories of polymer and colloidal interactions.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Biotin / chemistry
  • Biotin / metabolism*
  • Chemical Phenomena
  • Chemistry, Physical
  • Ligands
  • Lipid Bilayers
  • Mathematics
  • Models, Chemical
  • Molecular Conformation
  • Polyethylene Glycols / chemistry
  • Polyethylene Glycols / metabolism*
  • Streptavidin

Substances

  • Bacterial Proteins
  • Ligands
  • Lipid Bilayers
  • Polyethylene Glycols
  • Biotin
  • Streptavidin