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Partial-filling affinity capillary electrophoresis and quartz crystal microbalance with adsorption energy distribution calculations in the study of biomolecular interactions with apolipoprotein E as interaction partner
Laboratory of Analytical Chemistry, Department of Chemistry, P.O. Box 55, FIN-00014 University of Helsinki, Helsinki, Finland.
Laboratory of Analytical Chemistry, Department of Chemistry, P.O. Box 55, FIN-00014 University of Helsinki, Helsinki, Finland.
Karlstad University, Faculty of Health, Science and Technology (starting 2013), Department of Engineering and Chemical Sciences.ORCID iD: 0000-0003-1819-1709
National Institute for Health and Welfare and FIMM, Institute of Molecular Medicine Finland, Biomedicum, Haartmaninkatu 8, FIN-00290 Helsinki,.
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2014 (English)In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 406, no 17, 4137-4146 p.Article in journal (Refereed) Published
Abstract [en]

Adsorption energy distribution (AED) calculations were successfully applied to partial-filling affinity capillary electrophoresis (PF-ACE) to facilitate more detailed studies of biomolecular interactions. PF-ACE with AED calculations was employed to study the interactions between two isoforms of apolipoprotein E (apoE) and dermatan sulfate (DS), and a quartz crystal microbalance (QCM) was used in combination with AED calculations to examine the interactions of the 15-amino-acid peptide fragment of apoE with DS. The heterogeneity of the interactions was elucidated. Microscale thermophoresis was used to validate the results. The interactions studied are of interest because, in vivo, apolipoprotein E localizes on DS-containing regions in the extracellular matrix of human vascular subendothelium. Two-site binding was demonstrated for the isoform apoE3 and DS, but only one-site binding for apoE2–DS. Comparable affinity constants were obtained for the apoE2–DS, apoE3–D3, and 15-amino-acid peptide of apoE–DS using the three techniques. The results show that combining AED calculations with modern biosensing techniques can open up another dimension in studies on the heterogeneity and affinity constants of biological molecules.

Place, publisher, year, edition, pages
2014. Vol. 406, no 17, 4137-4146 p.
Keyword [en]
Adsorption energy distribution, analytical chemistry, Apolipoprotein E, Biochemistry, general, Characterization and Evaluation of Materials, Dermatan sulfate, Environmental Monitoring/Analysis, Food Science, Laboratory Medicine, Microscale thermophoresis, Partial-filling affinity capillary electrophoresis, Quartz crystal microbalance
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kau:diva-34384DOI: 10.1007/s00216-014-7821-9ISI: 000337787400011PubMedID: 24788890ISBN: 1618-2642, 1618-2650OAI: oai:DiVA.org:kau-34384DiVA: diva2:755873
Available from: 2014-10-15 Created: 2014-10-15 Last updated: 2016-01-12Bibliographically approved

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Samuelsson, JörgenFornstedt, Torgny
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