Chimeric Fusion Protein to Treat Autoimmune/Inflammatory Diseases

Brigham and Women's Hospital
posted on 05/12/2011

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Technology: Researchers at Brigham and Womens Hospital have developed a novel galectin-1 human immunoglobulin chimeric fusion protein, Gal-1-hFc, to overcome the stability issues encountered with native and recombinant gal-1 preparations. Currently, reducing agents such as DTT and 2-ME are routinely used to prevent oxidative inactivation of Gal-1. Our novel Gal-1hFc mimics the native structure Gal-1, while maintaining functionality, without requiring reducing agents. Applications: The fusion protein can be used for assaying Gal-1, Gal-1 ligand mediated activities in a number of laboratory methods. The fusion protein should also be evaluated as a therapeutic for treating autoimmune disorders. Advantages: -Mimics the native structure Gal-1, while maintaining functionality (e.g., binds canonical ligands without chemical stabilizers), unlike other Gal-1 formulations. -Will avert non-specific Fc-mediated cytoxicity responses, allowing for more accurate interpretation of Gal-1 function in autoimmune/inflammation responses in vivo. -Contains an IgG Fc domain for detection in various laboratory assays. -Does not need reducing agents (e.g., DTT) for structural and functional stabilization, eliminating ancillary effects of these agents such as induction of unnatural protein folding or T cell apoptosis independent of Gal-1 function. . Reference: Cedeno-Laurent, F. et al. Development of a Nascent Galectin-1 Chimeric Molecule for Studying the Role of Leukocyte Galectin-1 Ligands and Immune Disease Modulation. J Immunol 2010;185;4659-4672