Especially, HER2 and Sonic Hedge Hog protein (Hh), an over expressed surface receptor on breast cancer cells, is selected for targeted therapy and also selected TLR-5 immunomodulation. Hence, the current study, we employed in silico procedures to design a specific antibody-antigen complex, comprised of HER2/Hh specific Scfv derived from the Herceptin conjugated Hh, as a targeting molecule and bacterial toxin segment obtained from flagellar antigens FliC (E.coli) were conjugated to HER2/Hh specific Scfv via a flexible linker. A 3D model for this chimeric protein was constructed and its structure, stability, solubility and binding to targeted HER2, Hh and TLR-5 were predicted and, then, evaluated, using insilico procedures. Analysis showed that the chimeric protein could be a stable and soluble protein and the secondary structure of its parts would not change and the protein had a robust 3D structure that might have a stable mRNA structure and the PyDock server results showed that this antibody/antigen chimeric protein can bind to our proposed three targets such as HER2 and Hh receptors with high affinity and specificity and also good immunomodulatory binding of TLR-5.
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