2021, Vol.50, No.12
2011-2014
2011-2014
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.
A genetically fused recombinant hemoglobin [rHb(di-α/Cβ120)] was coupled with two human serum albumins (HSAs), yielding a rHb(di-α/Cβ120)–HSA2 trimer as an artificial O2 carrier. The di-α fusion prevents cleavage of the Hb core and haptoglobin binding. O2 affinity can be tuned to the appropriate value by complexation of an inositol hexaphosphate and a Kβ108 mutation into the Hb core.
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