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Production and Characterization of Biparatopic VEGFR-2-binding Affibody Molecule Constructs
KTH, School of Biotechnology (BIO).
2014 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Angiogenesis is the process of forming new blood vessels from pre-existing vasculature and has a central role in tumor progression. VEGFR-2 is the primary regulator of angiogenesis and is considered a promising target for cancer therapy and imaging. Affibody molecules are promising candidates in the field of antibody mimetics and libraries of Affibody molecules with high affinity and specificity to VEGFR-2 have previously been developed.

Protein constructs combining a set of anti-VEGFR-2 Affibody molecules at the N- and C-terminus with a center Albumin Binding Domain were cloned and expressed in Escherichia coli. The binding of the Affibody molecule constructs to VEGFR-2 were characterized with Surface Plasmon Resonance and cell binding experiments tracked by flow cytometry.

The cell binding and Surface Plasmon Resonance experiments showed that biparatopic Affibody molecule constructs had significantly higher binding strength to VEGFR-2 than homodimeric constructs and constructs with only one binding Affibody molecule. The reason is believed to be the effects of the increased binding surface of the two different Affibody molecules as well as an avidity effect caused by the biparatopic nature of the construct. The developed constructs and derivatives hold a potential for cancer therapeutics and as in vivo imaging tracers.

Place, publisher, year, edition, pages
Keyword [en]
Bispecifics, Affibody molecules, VEGFR-2, Biparatopic, Cancer, Affinity proteins
National Category
Engineering and Technology
URN: urn:nbn:se:kth:diva-173577OAI: diva2:853688
Available from: 2015-09-15 Created: 2015-09-14 Last updated: 2015-09-15Bibliographically approved

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