Evidence map›Paper›PMID 28234007›Full record

ArticleJournal of the American Chemical Society2017

Controlling Multivalent Binding through Surface Chemistry: Model Study on Streptavidin.

Galina V Dubacheva, Carolina Araya-Callis, Anne Geert Volbeda, Michael Fairhead, Jeroen Codée, Mark Howarth, Ralf P Richter

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed.

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  19. Significance of Receptor Mobility in Multivalent Binding on Lipid Membranes.Angewandte Chemie (International ed. in English) · 2022
    Review
  20. Streptavidin Coverage on Biotinylated Surfaces.ACS applied materials & interfaces · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Galina V DubachevaBiosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.ORCID 0000-0003-1417-5381
Carolina Araya-CallisBiosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.
Anne Geert VolbedaLeiden Institute of Chemistry, Leiden University , P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Michael FairheadDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, United Kingdom.
Jeroen CodéeLeiden Institute of Chemistry, Leiden University , P.O. Box 9502, 2300 RA Leiden, The Netherlands.ORCID 0000-0003-3531-2138
Mark HowarthDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, United Kingdom.
Ralf P RichterBiosurfaces Lab, CIC biomaGUNE , Paseo Miramon 182, 20014 Donostia - San Sebastian, Spain.

Funding

Biotechnology and Biological Sciences Research Council BB/I006303/1European Research Council 306435
6 · The paper itself

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.

Indexed as

Binding SitesModels, MolecularMolecular ConformationParticle SizeStreptavidinSurface PropertiesStreptavidin

Identifiers

PMID28234007
PMCPMC5364436

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.