Difference between revisions of "Part:BBa K3672001"
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| − | + | TGF-β is a key factor in triggering fibrosis by inducing the activation and differentiation of myofibroblasts, which leads to excessive production of extracellular matrix then forming fibrosis in organs or tissues.After modeling evaluation, we select M7824 rather than other 3 peptides (domains form P144, TMED10 and one unnamed peptide) as TGF-β blocking domain.M7824 consists of an IgG1 targeting programmed death ligand 1 (PD-L1) moiety fused via peptide linkers to the extracellular domain of two TGF-β receptor II molecules designed to ‘trap’ TGF-β. It has been used in the treatment of cancer and achieved remarkable results and its active region has been proved to be efficient. Consequently, we selected the active domain to capture TGF-β, as one of the active regions of drug proteins, so that TGF-β can be inactivated. Therefore, the course of fibrosis can be interrupted. | |
Latest revision as of 02:25, 28 October 2020
TGF-β is a key factor in triggering fibrosis by inducing the activation and differentiation of myofibroblasts, which leads to excessive production of extracellular matrix then forming fibrosis in organs or tissues.After modeling evaluation, we select M7824 rather than other 3 peptides (domains form P144, TMED10 and one unnamed peptide) as TGF-β blocking domain.M7824 consists of an IgG1 targeting programmed death ligand 1 (PD-L1) moiety fused via peptide linkers to the extracellular domain of two TGF-β receptor II molecules designed to ‘trap’ TGF-β. It has been used in the treatment of cancer and achieved remarkable results and its active region has been proved to be efficient. Consequently, we selected the active domain to capture TGF-β, as one of the active regions of drug proteins, so that TGF-β can be inactivated. Therefore, the course of fibrosis can be interrupted.