Impact of Polymer Tether Length on Multiple Ligand-Receptor Bond Formation

• Published in: Science (American Association for the Advancement of Science) 2001-07, Vol.293 (5529), p.465-468
• Main Authors: Jeppesen, Claus, Wong, Joyce Y., Kuhl, Tonya L., Israelachvili, Jacob N., Mullah, Nasreen, Zalipsky, Samuel, Marques, Carlos M.
• Format: Article
• Language: English
• Subjects: Analysis; Biochemistry; Biological and medical sciences; Biotin - chemistry; Biotin - metabolism; Chemical Phenomena; Chemistry, Physical; Dielectric materials; Diffusion; Electrons; Fundamental and applied biological sciences. Psychology; Interactions. Associations; Intermolecular phenomena; Kinetics; Ligand binding (Biochemistry); Ligands; Mathematics; Molecular biophysics; Molecular Structure; Molecules; Monte Carlo Method; Monte Carlo Methods; Oxides; Polyethylene Glycols; Polymers; Polymers - chemistry; Protein Conformation; Receptors; Semiconductors; Silicon; Solvents; Streptavidin - chemistry; Streptavidin - metabolism; Surface Properties; Thermodynamics
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.293.5529.465

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.