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Structure-activity studies of human beta2-glycoprotein I using capillary electrophoresis
Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
2011 (Engelska)Konferensbidrag, Publicerat paper (Refereegranskat)
Abstract

We have investigated various modes of CE to evaluate the interaction between beta2-glycoprotein I (b2gpI) and a number of anionic ligands to contribute to the elucidation of the structure-function relationship of b2gpI. b2gpI is a plasma protein which is involved in the blood coagulation cascade under normal, physiological conditions, however, its precise function is undefined. It is also involved in pathological conditions such as the so-called anti-phospholipid syndrome, where anti-b2gpI autoantibodies induce a prothrombotic state. Therefore, functional characterization of b2gpI under near physiological conditions is of interest.

To avoid charge-dependent analyte adsorption to the inner surface of the capillary wall, we have utilized the pH hysteresis effect, where an acidic pretreatment of the capillary made it possible to perform subsequent CE analyses of b2gpI at neutral pH.

The interaction between b2gpI and the anionic ligand heparin was studied with migration shift ACE, where the ionic strength, temperature and conformation of b2gpI were easily varied. The interaction between b2gpI and phosphatidylcholine/phosphatidylserine liposomes are subject to an ongoing investigation by means of migration shift ACE, frontal analysis CE, partial filling CE and pre-equilibration partial filling ACE.

We conclude that differential, but relatively low binding affinities that are highly dependent on electrostatic interactions and on a preserved conformation of the protein, characterize its interactions with ligands that in vivo will be present in multiple copies on e.g. cell surfaces. The CE procedure for this study is simple, fast and automatic and quantitative binding affinity parameters are conveniently obtained using small amounts of biological materials.

Ort, förlag, år, upplaga, sidor
2011.
Nationell ämneskategori
Kemi
Forskningsämne
Kemi
Identifikatorer
URN: urn:nbn:se:kau:diva-10742OAI: oai:DiVA.org:kau-10742DiVA, id: diva2:494294
Konferens
Joint congress 2011: Microscale Bioseparations San Diego
Tillgänglig från: 2012-02-08 Skapad: 2012-02-08 Senast uppdaterad: 2013-06-12Bibliografiskt granskad

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Bohlin, MariaBlomberg, Lars G

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Totalt: 115 träffar
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