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
Thermodynamic and kinetic approaches for evaluation of monoclonal antibody - Lipoprotein interactions.
University of Helsinki, Finland..ORCID iD: 0000-0002-8717-8842
Uppsala universitet.
Uppsala universitet.
Karlstad University, Faculty of Health, Science and Technology (starting 2013), Department of Engineering and Chemical Sciences.
Show others and affiliations
2016 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 518, 25-34 p.Article in journal (Refereed) Published
Abstract [en]

Two complementary instrumental techniques were used, and the data generated was processed with advanced numerical tools to investigate the interactions between anti-human apoB-100 monoclonal antibody (anti-apoB-100 Mab) and apoB-100 containing lipoproteins. Partial Filling Affinity Capillary Electrophoresis (PF-ACE) combined with Adsorption Energy Distribution (AED) calculations provided information on the heterogeneity of the interactions without any a priori model assumptions. The AED calculations evidenced a homogenous binding site distribution for the interactions. Quartz Crystal Microbalance (QCM) studies were used to evaluate thermodynamics and kinetics of the Low-Density Lipoprotein (LDL) and anti-apoB-100 Mab interactions. High affinity and selectivity were observed, and the emerging data sets were analysed with so called Interaction Maps. In thermodynamic studies, the interaction between LDL and anti-apoB-100 Mab was found to be predominantly enthalpy driven. Both techniques were also used to study antibody interactions with Intermediate-Density (IDL) and Very Low-Density (VLDL) Lipoproteins. By screening affinity constants for IDL-VLDL sample in a single injection we were able to distinguish affinity constants for both subpopulations using the numerical Interaction Map tool.

Place, publisher, year, edition, pages
Academic Press, 2016. Vol. 518, 25-34 p.
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kau:diva-47574DOI: 10.1016/j.ab.2016.10.024ISI: 000392461000004PubMedID: 27984014OAI: oai:DiVA.org:kau-47574DiVA: diva2:1061990
Available from: 2017-01-04 Created: 2017-01-04 Last updated: 2017-07-03Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Multia, EvgenSamuelsson, JörgenForssén, PatrikFornstedt, TorgnyÖörni, Katariina
By organisation
Department of Engineering and Chemical Sciences
In the same journal
Analytical Biochemistry
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 56 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