Stradomers come in a wide variety of shapes and sizes, including trimers, hexamers, and higher order multimers. Each one presents multiple immunoglobulin Fc to some or all of its many ligands and receptors simultaneously. GL-2045 is the first of our general stradomers, a multimerized cluster stradomer that binds avidly to a wide range of receptors and ligands to which immunoglobulin IgG1 Fc normally has affinity. It is being developed as a recombinant mimetic of the pooled human blood product IVIG for autoimmunity. GL-0719 is another example. It preferentially binds complement C1q better than Fc receptors, making it a complement-preferential stradomer. Gliknik also has generated stradomers that preferentially bind FcγRI, FcγRIIb, FcRn, or that preferentially binds Fc receptors preferentially over complement C1q.
Depending on the purpose, Gliknik stradomers are comprised of mutated or non-mutated IgG1, IgG4, or IgG3. They may be cluster, serial, or core in structure. They may also be combinations of various immunoglobulin components and structures.