Direct measurement of a tethered ligand-receptor interaction potential.
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.
Wong
J Y
JY
Department of Chemical Engineering, University of California, Santa Barbara, CA 93106, USA. jywong@engineering.ucsb.edu
Kuhl
T L
TL
Israelachvili
J N
JN
Mullah
N
N
Zalipsky
S
S
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D001710:Biotin / Q000737:chemistry / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008024:Ligands; D008051:Lipid Bilayers; D008433:Mathematics; D008956:Models, Chemical; D008968:Molecular Conformation; D011092:Polyethylene Glycols / Q000737:chemistry / Q000378:metabolism*; D019809:Streptavidin
D001426:Bacterial Proteins; D008024:Ligands; D008051:Lipid Bilayers; D011092:Polyethylene Glycols; D001710:Biotin; D019809:Streptavidin