مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

114
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

89
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

Purification of a Novel Anti-VEGFR2 Single Chain Antibody Fragment and Evaluation of Binding Affinity by Surface Plasmon Resonance

Pages

  64-69

Abstract

 Purpose: The single-chain variable fragment (ScFv) domain of antibodies is now considered as one of the therapeutic tools that can be produced by Phage display technology (PDT). Antibody Purification is one of the most important steps in antibodies production. The aim of study was Purification and characterization of anti-VEGFR2 ScFv antibody fragments. Methods: After the coating of vascular endothelial growth factor receptor 2 (VEGFR2) peptide in ELISA microplates, the Phage display library of Tomlinson was used for antibody isolation. The targeted ScFv was purified by chromatography using a zeolite-based column. The purity and functional assessment of purified ScFv were evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and western blotting techniques, respectively. Affinity binding was evaluated by Surface plasmon resonance (SPR). Results: The desired ScFv was selected after four stages of biopanning. SDS-PAGE analysis showed a 28 kDa ScFv with high purity (>90%). The western bloting analysis confirmed the binding of produced ScFv antibody to the desired peptide. The affinity binding of ScFv antibody analyzed by SPR was about 60 μ M. Conclusion: In this study, the novel ScFv antibody against VEGFR2 peptide was purified by chromatography column containing zeolite. Based on our findings the produced antibody may be applied for diagnosis or targeting of VEGFR2 in antibody-based therapy strategies.

Cites

  • No record.

    • References

  • No record.

    • Cite

    APA: Copy

    Kordi, Shirafkan, RAHMATI YAMCHI, MOHAMMAD, ASGHARI VOSTAKOLAEI, MEHDI, BARZEGARI, ABOLFAZL, & ABDOLALIZADEH, JALAL. (2019). Purification of a Novel Anti-VEGFR2 Single Chain Antibody Fragment and Evaluation of Binding Affinity by Surface Plasmon Resonance. ADVANCED PHARMACEUTICAL BULLETIN, 9(1), 64-69. SID. https://sid.ir/paper/745904/en

    Vancouver: Copy

    Kordi Shirafkan, RAHMATI YAMCHI MOHAMMAD, ASGHARI VOSTAKOLAEI MEHDI, BARZEGARI ABOLFAZL, ABDOLALIZADEH JALAL. Purification of a Novel Anti-VEGFR2 Single Chain Antibody Fragment and Evaluation of Binding Affinity by Surface Plasmon Resonance. ADVANCED PHARMACEUTICAL BULLETIN[Internet]. 2019;9(1):64-69. Available from: https://sid.ir/paper/745904/en

    IEEE: Copy

    Shirafkan Kordi, MOHAMMAD RAHMATI YAMCHI, MEHDI ASGHARI VOSTAKOLAEI, ABOLFAZL BARZEGARI, and JALAL ABDOLALIZADEH, “Purification of a Novel Anti-VEGFR2 Single Chain Antibody Fragment and Evaluation of Binding Affinity by Surface Plasmon Resonance,” ADVANCED PHARMACEUTICAL BULLETIN, vol. 9, no. 1, pp. 64–69, 2019, [Online]. Available: https://sid.ir/paper/745904/en

    Related Journal Papers

  • No record.

    • Related Seminar Papers

  • No record.

    • Related Plans

  • No record.

    • Recommended Workshops






    Move to top
    telegram sharing button
    whatsapp sharing button
    linkedin sharing button
    twitter sharing button
    email sharing button
    email sharing button
    email sharing button
    sharethis sharing button