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Nazemi Zadeh A, Sarafrazi F, Habibi Fozon Abadi M, Rassouli H. Lab-scale Production of Recombinant Platelet-derived Growth Factor-BB Homodimer (PDGF-BB) in Microbial Expression System. ASWTR 2025; 22 (3) :41-47
URL: http://icml.ir/article-1-690-en.html

Background: In recent years, the number of recombinant proteins used for therapeutic applications has increased dramatically. Among the growth factors, platelet-derived growth factors (PDGFs) are effective in the management of injury and involve many cellular events in the healing process, including inflammatory cell recruitment, fibroblast proliferation and migration, collagen deposition, and granulation tissue formation. During the process of natural wound healing, platelets are one of the first cells that respond at the wound site or around it and play an essential role in wound healing. Platelets are a rich source of growth factors, including PDGF. PDGF is the first and only recombinant growth factor approved by the US Food and Drug Administration (FDA) for topical administration to treat diabetic foot ulcers.
Methods: In this study, we’ve built a microbial expression vector containing the coding sequence for optimized PDGF-BB and transformed it into an E. coli Strain. Then we developed a complete production process that includes: expression, purification using affinity chromatography, and biological activity assay by evaluation of NIH-3T3 cell growth in response to the produced recombinant human PDGF-BB.
Results: The purified PDGF-BB (15 mg⁄L of culture) was well-folded and biologically active. The whole procedure is fast and scalable.
Conclusion: The chosen E. coli Strain can produce and fold recombinant human PDGF-BB. The produced PDGF-BB has biologically active, and could be considered for further investigation.