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. 2015 Jun 14;7(5):931–945. doi: 10.1080/19420862.2015.1055442

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Eli Lilly and Company

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 1. — Design and molecular structure of bi-functional antibody receptor domain fusion molecule with VEGF capture (bi-AbCap). (A) Cartoon illustration of the designed bi-AbCap fusion molecule. Orange: Anti IGF-IR IgG backbone, IR mAb; Purple: polypeptide linker; Green: extracellular domain 2 of human VEGFR1 (D2). An FcD2 control molecule was made containing the regions of the hinge, Fc, linker and D2. (B) SDS-PAGE of IR mAb, FcD2 and bi-AbCap ID2. (C) Top: linker sequence: G₄SG₄; Bottom: the D2 domain used for fusion encompassing amino acids 129–229 of hVEGFR1. (D) ID2 elutes as a mono-disperse peak by size exclusion chromatograpy (SEC). (E) ID2 displays 3 melting temperatures (Tm) when the thermal stability of ID2 measured by differential scanning calorimetry (DSC). Tm₁ = 64.4 ± 0.0°C, Tm₂ = 76.0 ± 0.0°C, Tm₃ = 82.7 ± 0.1°C. (F) IR mAb displays 3 Tms by DSC: Tm₁ = 72.2 ± 0.1°C, Tm₂ = 76.8 ± 0.0°C, Tm₃ = 83.2 ± 0.1°C.