Immune thrombocytopenic purpura (ITP) is an autoimmune disorder determined
by immune-mediated platelet demolition and reduction of platelet production. Romiplostim
is a new thrombopoiesis motivating peptibody that binds and stimulates the human thrombopoietin
receptor. It is used to treat thrombocytopenia in patients with chronic immune
thrombocytopenic purpura. Romiplostim is a 60 kDa peptibody designed to inhibit crossreacting
immune responses. It consists of four high-affinity TPO-receptor binding domains
for the Mpl receptor and one human IgG1 Fc domain. Escherichia coli is a good host for
the fabrication of recombinant proteins such as romiplostim. The expression of a gene intended
in E. coli is dependent on many factors such as a protein’s inherent ability to fold,
mRNA’s secondary structure, its solubility, its toxicity preferential codon use, and its need
for post-translational modification (PTM). This review focuses on the structure, function,
mechanism of action, and expressive approach to romiplostim in E. Coli.
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