uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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
Nanoparticle decorated surfaces with potential use in glycosylation analysis
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
2005 (English)In: Colloids and Surfaces B: Biointerfaces, Vol. 46, 84–91- p.Article in journal (Refereed) Published
Abstract [en]

A majority of all biologically active proteins are glycosylated and various diseases have proven to correlate with alterations in protein glycosylation. Sensitive identification of different glycoprotein glycoforms is therefore of great diagnostic value. Here we describe a method with potential for glycoprotein profiling, based on lectins as capture probes immobilized on particulate substrates in the nm-range. The nanoparticles present high concentrations of attachment sites for specific ligands and cause minimal steric hindrance to binding. In the present model study the mannose-binding lectin ConA has been coupled to polystyrene nanoparticles via a poly(ethyleneoxide) linker which protects the protein conformation and activity and prevents unspecific protein adsorption. The ConA-coated particles are accommodated at different spots on the analytical surface via oligonucleotide linkage. This attachment, which relies on the hybridization of complementary oligonucleotides, allows firm fixation of the particles at specific positions. The ConA attached to the particles has retained conformation and activity and binds selectively to a series of different glycoproteins. The results indicate the potential for using a multi-lectin nanoparticle array in glycoprotein mapping.

Place, publisher, year, edition, pages
2005. Vol. 46, 84–91- p.
Keyword [en]
Nanoparticles, Glycoprotein, Glycosylation
Identifiers
URN: urn:nbn:se:uu:diva-25395OAI: oai:DiVA.org:uu-25395DiVA: diva2:53169
Available from: 2007-02-12 Created: 2007-02-12 Last updated: 2011-01-12

Open Access in DiVA

No full text

Other links

http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TFS-4HK0FHW-2&_user=651519&_coverDate=12%2F10%2F2005&_rdoc=5&_fmt=full&_orig=browse&_srch=doc-info(%23toc%235234%232005%23999539997%23611008%23FLA%23display%23Volume)&_cdi=5234&_sort=d&_docanchor=&view=c&_ct=10&_acct=C000035158&_version=1&_urlVersion=0&_userid=651519&md5=fd3e16b705da86edba808c89745736a9

Authority records BETA

Fromell, KarinAndersson, MargarethaCaldwell, Karin

Search in DiVA

By author/editor
Fromell, KarinAndersson, MargarethaCaldwell, Karin
By organisation
Surface BiotechnologySurface BiotechnologyDepartment of Physical and Analytical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 355 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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