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Studies of unspecific interaction between the Aβ antibody 6E10 and blood coagulation protein factor X
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
2012 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Alzheimer’s disease is neurodegenerative with amyloid plaque and neurofibrillary tangles as pathological hallmarks. The most abundant component in the amyloid plaque is the amyloid-β (Aβ) peptide, with presence of both isoform Aβ40 and Aβ42. In immunological methods studying the Aβ peptide a specific monoclonal antibody, 6E10, is routinly being used. In this master thesis work unspecific binding of 6E10 antibody to the blood coagulating protein factor X has been investigated. Factor X is a protein in the blood coagulation cascade where it forms protein complex that activates thrombin. Non-hemostatic functions with connections to nerves and Aβ peptide are also known. Studies with Western blot show clear binding of 6E10 to denatured factor X. Interaction studies with ELISA gives uncertain results, where binding is found but no clear binding curve is obtained. Studies with native factor X in real time measurements with SPR gave no binding at all. These results suggest binding to denatured factor X. Immunohistochemistry studies of colocalisation of factor X and Aβ peptide gave clear evidence that factor X and Aβ are found near each other in mouse brain tissue. Factor X is located outside the blood vessels and Aβ is located at the inside. 

Place, publisher, year, edition, pages
2012. , 61 p.
Keyword [en]
Alzheimer’s disease, 6E10, Aβ, Factor X, SPR, ELISA
National Category
Other Chemistry Topics
URN: urn:nbn:se:liu:diva-82346ISRN: LITH-­IFM-­A-­EX-­-­12/2584-­-­SEOAI: diva2:558079
Subject / course
Physics, Chemistry, Mathematics
Available from: 2012-10-02 Created: 2012-10-01 Last updated: 2012-10-02Bibliographically approved

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Karlsson, Cecilia
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Department of Physics, Chemistry and BiologyThe Institute of Technology
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