New insights into the most abundant protein in blood published in Nature Communications Biology
Assistant Professor Esben Trabjerg and Professor Kasper Dyrberg Rand from Protein Analysis Group have published the results of their research on Albumin in the prestigious journal Nature Communications Biology.
The paper, entitled An intact C-terminal end of albumin is required for its long half-life in humans is the first paper issued from a fruitful collaboration between the Department’s Protein Analysis Group and the Laboratory of Adaptive Immunity and Homeostasisat, lead by Jan Terje Andersen at Oslo University Hospital. Read the article online.
Albumin is the most abundant serum protein and has a remarkable long half-life in the human body on approximately 3 weeks. The long half-life is due to its pH dependent interaction with the Neonatal Fc Receptor (FcRn). In the current study, it is demonstrated that deletion of the C-terminal residue in albumin (L585), observed in patients with acute pancreatitis, dramatically decreases the half-life of albumin.
By comparing the hydrogen/deuterium exchange of wildtype Albumin and the truncated form Albumin (L585X), Esben Trabjerg and Kasper Dyrberg Rand could reveal that removal of the C-terminal residue causes a structural stabilization in the DIII domain of Albumin.
This structural stabilization causes a decrease in affinity of Albumin towards FcRn. Thus, the conformational dynamics of the DIII domain is important to secure a long half-life of Albumin, a finding that sheds new light on acute pancreatic disease and has broad implications for the design of albumin-based biopharmaceuticals.