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Various chemical modifications of hemoglobin (Hb) including PEGylation have been investigated to produce red blood cell substitutes. Some of those modifications are designed on the premise that the α 2 β 2 etrameric structure of Hb is fundamentally stable and that it rarely dissociates into two αβ dimers in a physiological condition. However, in the present work using the "clipping" method we detected and quantitatively analyzed the considerable degree of exchange reaction of αβ subunits between β93Cys-bis-PEGylated and native Hbs through dissociation into αβ dimers and restructuring to α 2 β 2 etramer in a physiological condition. The equilibrium constant ( K eq ) of subunit exchange reactions increased from 0.82 to 2.86 with increasing molecular weight of PEG from 2 to 40 kDa, indicating that longer PEG chains enhanced such exchange reaction. The results suggest that the exchange might occur for other modified Hbs even at a practically high concentration for use as a red blood cell substitute.

biomacromolecules

Analysis of Dimeric αβ Subunit Exchange between PEGylated and Native Hemoglobins (α<sub>2</sub>β<sub>2</sub> Tetramer) in an Equilibrated State by Intramolecular ββ-Cross-Linking

Analysis of Dimeric αβ Subunit Exchange between PEGylated and Native Hemoglobins (α2β2 Tetramer) in an Equilibrated State by Intramolecular ββ-Cross-Linking

Analysis of Dimeric αβ Subunit Exchange between PEGylated and Native Hemoglobins (α₂β₂ Tetramer) in an Equilibrated State by Intramolecular ββ-Cross-Linking