Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Gold-nanoparticle-assisted self-assembly of chemical gradients with tunable sub-50 nm molecular domains
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Material och ytteknik.ORCID iD: 0000-0002-9377-8924
2014 (English)In: Particle & particle systems characterization, ISSN 0934-0866, E-ISSN 1521-4117, Vol. 31, no 2, p. 209-218Article in journal (Refereed) Published
Abstract [en]

A simple and efficient principle for nanopatterning with wide applicability in the sub-50 nanometer regime is chemisorption of nanoparticles; at homogeneous substrates, particles carrying surface charge may spontaneously self-organize due to the electrostatic repulsion between adjacent particles. Guided by this principle, a method is presented to design, self-assemble, and chemically functionalize gradient nanopatterns where the size of molecular domains can be tuned to match the level corresponding to single protein binding events. To modulate the binding of negatively charged gold nanoparticles both locally (<100 nm) and globally (>100 μm) onto a single modified gold substrate, ion diffusion is used to achieve spatial control of the particles' mutual electrostatic interactions. By subsequent tailoring of different molecules to surface-immobilized particles and the void areas surrounding them, nanopatterns are obtained with variable chemical domains along the gradient surface. Fimbriated Escherichia coli bacteria are bound to gradient nanopatterns with similar molecular composition and macroscopic contact angle, but different sizes of nanoscopic presentation of adhesive (hydrophobic) and repellent poly(ethylene) glycol (PEG) domains. It is shown that small hydrophobic domains, similar in size to the diameter of the bacterial fimbriae, supported firmly attached bacteria resembling catch-bond binding, whereas a high number of loosely adhered bacteria are observed on larger hydrophobic domains. Chemical gradients with the resolution needed to address complex biological binding events at the single protein level are prepared using surface-deposited gold nanoparticles as a versatile template for orthogonal chemicalmodifications. The effect of hydrophobic domain arrangement on the sub-50 nm scale is shown to influence binding of fimbriae carrying E. coli bacteria. 

Place, publisher, year, edition, pages
2014. Vol. 31, no 2, p. 209-218
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-6711DOI: 10.1002/ppsc.201300154Scopus ID: 2-s2.0-84893984535Local ID: 23710OAI: oai:DiVA.org:ri-6711DiVA, id: diva2:964551
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2019-08-14Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textScopus

Authority records BETA

Berglin, Mattias

Search in DiVA

By author/editor
Berglin, Mattias
By organisation
Material och ytteknik
In the same journal
Particle & particle systems characterization
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 8 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
v. 2.35.7