Abstract
HemoCD is an inclusion complex of per-O-methylated β-cyclodextrin dimer and an iron(II) porphyrin, which forms a stable O2 complex in water. Therefore, hemoCD has the potential for use as a synthetic O2 carrier in mammalian blood. In this study, a hemoCD derivative having a maleimide group (Mal-hemoCD) was conjugated to a Cys residue of serum albumin via a Michael addition reaction in order to increase the circulation time of the O2 carrier. The O2 -binding affinities (P1/2 [Torr]) and half-lives (t1/2 [h]) of the O2 adducts at pH 7.4 and 25 °C were determined to be 9 Torr and 23 h for Mal-hemoCD, and 10 Torr and 14 h for albumin-conjugated hemoCD (Alb-hemoCD). Our pharmacokinetic study revealed that renal excretion of Alb-hemoCD was effectively suppressed and that half of injected Alb-hemoCD remained in blood at 3 h after injection. It is noteworthy that Mal-hemoCD also had a long circulation time because of the bioconjugation reaction that occurred during circulation in the bloodstream.
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