In the past 10-15 years biologically active agents with antigen binding activity like antibodies, antibody fragments, antibody like molecules, and scaffold proteins have gained significant relevance.
their therapeutic use has yet been limited because of rapid renal excretion, or poor solubility, or immunogenicity, or reduced binding affinity and/or avidity as compared with native human antibodies. For this reason, many attempts have been made to improve the pharmacological properties of such antigen binding proteins routinely having molecular weights far below 50,000 Dalton. Reviews have been published in Nature Biotechnology Volume 21, Number 4, 2006: 1126-36 or Nature Reviews Immunology, Vol 6, 2006: 343 -357.
celares GmbH and Scil Proteins GmbH have co-developed a multimeric binding agent for the multimerization of antigen binding proteins. This reagent is characterized by a defined structure and adjustable linker length. In this way, it is possible to prepare conjugates with decelerated renal clearance showing a higher avidity compared to the avidity of the monomeric binding molecule.
An example is a TNF-α binding Affilin® molecules. By tetramerization with our agent it has been able to increase its affinity in an in-vitro assay 30-fold.
Affilin® is a registered mark designation owned by Scil Proteins GmbH.