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Interferon beta R27T is a hyperglycosylated recombinant human interferon-beta-1a (rhIFN-β) mutein. Developed by ABION Inc., it is primarily intended for the treatment of relapsing-remitting multiple sclerosis (RRMS). The molecule is engineered via site-directed mutagenesis, replacing arginine at position 27 with threonine (R27T), which creates an additional N-glycosylation site at the 25th amino acid residue. This modification improves the protein's biophysical properties, including increased solubility, stability, and productivity, while also enhancing its pharmacokinetic profile. Mechanistically, it acts as an agonist for the type I interferon receptors IFNAR1 and IFNAR2. The altered glycosylation pattern destabilizes the interaction with IFNAR2 while enhancing the interaction with IFNAR1, leading to prolonged signaling and potent anti-proliferative and immunomodulatory effects. It has also been investigated as a therapeutic payload in antibody-cytokine fusion proteins, such as trastuzumab-IFN-β-R27T, for cancer therapy.
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