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PEGylation of Human Vascular Endothelial Growth Factor

  • Alena Maria Wolkersdorfer
    Alena Maria Wolkersdorfer
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
  • Isabelle Jugovic
    Isabelle Jugovic
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
  • Lena Scheller
    Lena Scheller
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
  • Marcus Gutmann
    Marcus Gutmann
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
  • Lukas Hahn
    Lukas Hahn
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
    More by Lukas Hahn
  • Joachim Diessner
    Joachim Diessner
    University of Würzburg, Department of Obstetrics and Gynecology, Josef-Schneider-Straße 14, Würzburg DE-97080, Germany
  • Tessa Lühmann*
    Tessa Lühmann
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
    *E-mail: [email protected]
  • , and 
  • Lorenz Meinel*
    Lorenz Meinel
    Institute of Pharmacy and Food Chemistry, University of Würzburg, University, Am Hubland, Würzburg DE-97074, Germany
    Helmholtz Centre for Infection Research, Helmholtz-Institute for RNA-based Infection Research (HIRI), Josef-Schneider-Strasse 2/D15, Würzburg 97080, Germany
    *E-mail: [email protected]
Cite this: ACS Biomater. Sci. Eng. 2024, 10, 1, 149–155
Publication Date (Web):June 9, 2023
https://doi.org/10.1021/acsbiomaterials.3c00253
Copyright © 2023 The Authors. Published by American Chemical Society

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    Abstract

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    Vascular endothelial growth factor A-165 (VEGF-A165) positively modulates neointimal hyperplasia, lumen stenosis, and neovascularization. One challenge for the use of VEGF-A165 for potential therapy is its short serum half-life. Therefore, we are designing VEGF-A165 bioconjugates carrying polyethylene glycol (PEG). The purity of the recombinantly expressed human VEGF-A165 exceeded 90%. The growth factor had a half-maximal effective concentration of 0.9 ng/mL (EC50) and induced tube formation of human umbilical vein endothelial cells. PEGylation was conducted by Schiff base reaction followed by reductive amination. After purification, two species were obtained, with one or two PEG attached per VEGF-A165 dimer. Both resulting bioconjugates had a purity exceeding 90%, wild-type bioactivity, and increased hydrodynamic radii as required for prolonging the half-life.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acsbiomaterials.3c00253.

    • Isolation, cultivation, and cryopreservation of human umbilical cord vein cells (HUVEC); in-gel digest for nanoLC-MS/MS analysis; Sequence S1; chromatogram; 1H NMR spectrum; HPLC analysis; SDS PAGE; induction of tube formation; DLS graph (PDF)

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    Cited By

    This article is cited by 1 publications.

    1. Kirstin Meiners, Prisca Hamm, Marcus Gutmann, Jan Niedens, Agnieszka Nowak-Król, Salvador Pané, Tessa Lühmann. Site-specific PEGylation of recombinant tissue-type plasminogen activator. European Journal of Pharmaceutics and Biopharmaceutics 2023, 192 , 79-87. https://doi.org/10.1016/j.ejpb.2023.09.017