title: Impact of polymer tether length on multiple ligand-receptor bond formation.
abstract: The promoters of cell adhesion are ligands, which are often attached to flexible tethers that bind to surface receptors on adjacent cells. Using a combination of Monte Carlo simulations, diffusion reaction theory, and direct experiments (surface force measurements) of the biotin-streptavidin system, we have quantified polymer chain dynamics and the kinetics and spatial range of tethered ligand-receptor binding. The results show that the efficiency of strong binding does not depend solely on the molecular architecture or binding energy of the receptor-ligand pair, nor on the equilibrium configuration of the polymer tether, but rather on its "rare" extended conformations.
authors.affiliation: Materials Research Laboratory, Department of Chemical Engineering, University of California, Santa Barbara, CA 93106, USA.
authors.forename: C
authors.initials: C
authors.lastname: Jeppesen
authors.forename: J Y
authors.initials: JY
authors.lastname: Wong
authors.forename: T L
authors.initials: TL
authors.lastname: Kuhl
authors.forename: J N
authors.initials: JN
authors.lastname: Israelachvili
authors.forename: N
authors.initials: N
authors.lastname: Mullah
authors.forename: S
authors.initials: S
authors.lastname: Zalipsky
authors.forename: C M
authors.initials: CM
authors.lastname: Marques
mesh_terms: D001710:Biotin / Q000737:chemistry* / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004058:Diffusion; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D009010:Monte Carlo Method; D011092:Polyethylene Glycols; D011108:Polymers / Q000737:chemistry*; D011487:Protein Conformation; D019809:Streptavidin / Q000737:chemistry* / Q000378:metabolism; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011108:Polymers; D011092:Polyethylene Glycols; D001710:Biotin; D019809:Streptavidin