title: Controlling Multivalent Binding through Surface Chemistry: Model Study on Streptavidin.
abstract: Although multivalent binding to surfaces is an important tool in nanotechnology, quantitative information about the residual valency and orientation of surface-bound molecules is missing. To address these questions, we study streptavidin (SAv) binding to commonly used biotinylated surfaces such as supported lipid bilayers (SLBs) and self-assembled monolayers (SAMs). Stability and kinetics of SAv binding are characterized by quartz crystal microbalance with dissipation monitoring, while the residual valency of immobilized SAv is quantified using spectroscopic ellipsometry by monitoring binding of biotinylated probes. Purpose-designed SAv constructs having controlled valencies (mono-, di-, trivalent in terms of biotin-binding sites) are studied to rationalize the results obtained on regular (tetravalent) SAv. We find that divalent interaction of SAv with biotinylated surfaces is a strict requirement for stable immobilization, while monovalent attachment is reversible and, in the case of SLBs, leads to the extraction of biotinylated lipids from the bilayer. The surface density and lateral mobility of biotin, and the SAv surface coverage are all found to influence the average orientation and residual valency of SAv on a biotinylated surface. We demonstrate how the residual valency can be adjusted to one or two biotin binding sites per immobilized SAv by choosing appropriate surface chemistry. The obtained results provide means for the rational design of surface-confined supramolecular architectures involving specific biointeractions at tunable valency. This knowledge can be used for the development of well-defined bioactive coatings, biosensors and biomimetic model systems.
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.|PPSM CNRS UMR8531, ENS Cachan, Université Paris-Saclay , 61 Avenue du Président Wilson, 94235 Cachan, France.
authors.forename: Galina V
authors.identifier: 0000-0003-1417-5381
authors.initials: GV
authors.lastname: Dubacheva
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.
authors.forename: Carolina
authors.initials: C
authors.lastname: Araya-Callis
authors.affiliation: Leiden Institute of Chemistry, Leiden University , P.O. Box 9502, 2300 RA Leiden, The Netherlands.
authors.forename: Anne
authors.initials: A
authors.lastname: Geert Volbeda
authors.affiliation: Department of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, United Kingdom.
authors.forename: Michael
authors.initials: M
authors.lastname: Fairhead
authors.affiliation: Leiden Institute of Chemistry, Leiden University , P.O. Box 9502, 2300 RA Leiden, The Netherlands.
authors.forename: Jeroen
authors.identifier: 0000-0003-3531-2138
authors.initials: J
authors.lastname: Codée
authors.affiliation: Department of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, United Kingdom.
authors.forename: Mark
authors.initials: M
authors.lastname: Howarth
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.|School of Biomedical Sciences and School of Physics and Astronomy, University of Leeds , Leeds LS2 9JT, United Kingdom.|Laboratory of Interdisciplinary Physics, University Grenoble Alpes - CNRS , 140 Rue de la Physique, 38402 Saint Martin d'Hères, France.
authors.forename: Ralf P
authors.initials: RP
authors.lastname: Richter
mesh_terms: D001665:Binding Sites; D008958:Models, Molecular; D008968:Molecular Conformation; D010316:Particle Size; D019809:Streptavidin / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D019809:Streptavidin