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A covalent core–shell structured protein cluster composed of hemoglobin (Hb) at the center and human serum albumins (HSA) at the periphery, Hb-HSA m , is an artificial O 2  carrier that can function as a red blood cell substitute. Here we described the preparation of a novel Hb-HSA  3   cluster with antioxidant activities and its O 2  complex stable in aqueous H 2 O 2  solution. We used an approach of incorporating a Pt nanoparticle (PtNP) into the exterior HSA unit of the cluster. A citrate reduced PtNP (1.8 nm diameter) was bound tightly within the cleft of free HSA with a binding constant ( K ) of 1.1×10 7  M −1 , generating a stable HSA-PtNP complex. This platinated protein showed high catalytic activities for dismutations of superoxide radical anions (O 2   •– ) and hydrogen peroxide (H 2 O 2 ), i.e., superoxide dismutase and catalase activities. Also, Hb-HSA  3   captured PtNP into the external albumin unit ( K  = 1.1×10 7  M −1 ), yielding an Hb-HSA  3  (PtNP) cluster. The association of PtNP caused no alteration of the protein surface net charge and O 2  binding affinity. The peripheral HSA-PtNP shell prevents oxidation of the core Hb, which enables the formation of an extremely stable O 2  complex, even in H 2 O 2  solution.

Hemoglobin–Albumin Cluster Incorporating a Pt Nanoparticle: Artificial O2 Carrier with Antioxidant Activities