2021, Vol.50, No.12
We describe synthesis of a symmetric protein triad comprising a genetically fused recombinant hemoglobin(di-α/Cβ120) center and human serum albumin sides [rHb(di-α/Cβ120)–HSA2]. This trimer is not cleaved at low concentration. It shows adequate resistance to haptoglobin binding as an artificial O2 carrier used as a red blood cell (RBC) substitute. Also, O2 affinity of the trimer was modulated to the appropriate value, similarly to that of RBCs, by complexation of inositol hexaphosphate and a Kβ108 mutation into the Hb core.