28/10/2026
Can we design protein medicines that last longer and can be delivered without needles?
In our new study in Nature Communications, we explored both possibilities by connecting the therapeutic protein ( ) to an engineered version of human albumin.
The approach builds on a natural partnership: albumin binds to the neonatal Fc receptor ( ), which protects it from degradation but also helps transport it across cellular barriers.
By engineering , we improved the properties of EPO attached to it. In mice expressing human FcRn, we show:
1) A more than fivefold increase in plasma half-life compared with EPO fused to normal albumin, from 1.1 to 5.7 days.
2) Uptake into the bloodstream following administration through the nose, with approximately fivefold greater exposure than the corresponding normal-albumin fusion.
3) Preserved biological activity, supporting a sustained increase in red blood cells.
These are preclinical findings and show how our understanding of complex biology combined with protein engineering can open opportunities for longer-acting biologics and delivery across mucosal barriers.
Congratulations to first author Aina Karen Anthi, Daniela Bejan, Simone Mester Sopisa Benjakul Kristin Hovden Aaen Inger Sandlie and all our collaborators who contributed to this work! Tilman Schlothauer Roche
Nijaguna Bethur and Elena Gonzalo-Gil, PhD for a great collaboration on the use of The Jackson Laboratory human FcRn transgenic mice 🐭
Funded by Norges forskningsråd Novo Nordisk Foundation
This study presents a tailored erythropoietin fused to engineered albumin for extended plasma half-life after intravenous and subcutaneous delivery in mice. Following invasive or intranasal delivery, it promotes sustained erythrocyte proliferation.
