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
Interaction forces between BSA layers adsorbed on silica surfaces measured with an atomic force microscope
Show others and affiliations
2004 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 108, no 17, 5365-5371 p.Article in journal (Refereed) Published
Abstract [en]

The interaction forces between bovine serum albumin (BSA) layers adsorbed on silica surfaces have been measured using an atomic force microscope (AFM) in Conjunction with the colloid probe technique. Measurements of force-distance curves were made at different pH values and electrolyte concentrations (NaCl and CaCl2). The interaction at long range is dominated by electrical double-layer forces, while at short surface separations an additional repulsion due to the compression of the adsorbed protein layers appears. However, prior to this steric interaction, when the pH is above the isoelectric point of the protein and at high salt concentration, a non-DLVO repulsive interaction is observed. This behavior is explained if the presence of hydration forces in the system is assumed. Theoretical predictions including a hydration term in the DLVO theory fit the experimental results satisfactorily. The results presented in this article provide a direct confirmation that the AFM colloid probe technique can provide a useful way of directly quantifying the interaction of biological macromolecules.

Place, publisher, year, edition, pages
2004. Vol. 108, no 17, 5365-5371 p.
Keyword [en]
aqueous-electrolyte solutions, hydration forces, colloidal stability, mica surfaces, long-range, solid-surfaces, protein layers, particles, adsorption, aggregation
National Category
Other Chemistry Topics
Identifiers
URN: urn:nbn:se:kth:diva-23355DOI: 10.1021/jp0374197ISI: 000220997300035Scopus ID: 2-s2.0-2442587880OAI: oai:DiVA.org:kth-23355DiVA: diva2:342053
Note
QC 20100525Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2011-11-01Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Feiler, AdamRutland, Mark W
By organisation
Chemistry
In the same journal
Journal of Physical Chemistry B
Other Chemistry Topics

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 38 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