Affibody’s Albumod™ technology extends the circulatory half-life of biopharmaceuticals and is protected by separate Affibody intellectual property rights. The core of the technology is the Albumin Binding Domain (ABD) a small binding protein engineered to bind human serum albumin with a very high affinity.
Prolonged Half-Life
Due to the extremely tight binding of ABD to serum albumin, the complex behaves as a serum albumin fusion protein. Thereby, a fusion protein incorporating ABD obtains a half-life comparable to serum albumin.
Rapid & Wide Biodistribution
The ABD fusion protein benefits from the rapid and wide distribution of serum albumin. Albumin is widely distributed in the body with 60% found outside of the blood stream, mainly in the interstitium. This is in contrast to antibodies that circulate primarily in the blood stream.
Increased Solubility
The Albumod™ technology may be applied to increase the solubility of non-polar polypeptides or chemical compounds.
Facilitated Production
The manufacturing is simplified as ABD fusion proteins are readily produced in bacteria. The small size of ABD enables production by peptide synthesis which allows for introduction of various chemical modifications. If the fusion partner is small, the ABD fusion protein may also be generated by peptide synthesis.
New Routes of Administration
Affibody’s Albumod™ technology may be utilized for new routes of administration, utilizing the presence of the neonatal Fc receptor (FcRn) in the airways and in the intestine. Therefore, an aerosol formulation of an albumin complex may allow transport over the lung epithelium and into the blood circulation. Such orally or nasally delivered pharmaceuticals simplify administration and improve patient compliance.
Cross species preclinical validation
Biopharmaceuticals based on the Albumod™ technology can be validated in standard in vivo models since the ABD binds to serum albumin from several species, including rats and primates. This facilitates efficacy studies of candidate molecules, as well as improves predictability of safety data obtained from standard species.