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Background and Aim: Conventional treatments have shown little success in cancer treatment. Using antibody fragments conjugated with specific proteins and targeting specific receptors is a new strategy for producing anticancer drugs. Despite the advantages of prokaryotic hosts, protein expression in the form of inclusion bodies (cytoplasmic) has been challenging and leads to subsequent difficulties. Production of proteins as soluble forms will significantly help to solve this problem. The primary purpose of this study was to clone and express Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) conjugated with anti CD 20 single chain fragment variable (scFV) region of anti-CD 20 antibody as a soluble protein using a small ubiquitin-related modifier (SUMO) fusion protein system in E. coli as a new method for optimal production of anticancer drugs.
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Rasekhian et al. (2023) studied this question.
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