Hemoglobin–Albumin Cluster Incorporating a Pt Nanoparticle
| Autor: | Risa Haruki, Kana Yamada, Teruyuki Komatsu, Hitomi Hosaka, Christoph Böttcher |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Molecular Conformation lcsh:Medicine Biochemistry Antioxidants chemistry.chemical_compound Hemoglobins Superoxides Medicine and Health Sciences Hydrogen peroxide lcsh:Science Genetics Multidisciplinary Aqueous solution Hemoproteins biology Chemistry Superoxide Clinical Laboratory Sciences Covalent bond Research Article Biotechnology Protein Binding Superoxide dismutase Biomaterials Inhibitory Concentration 50 Diagnostic Medicine Blood Substitutes Albumins Polymer chemistry Humans Blood Transfusion Hemoglobin Bioinorganic Chemistry Serum Albumin Binding Sites Transfusion Medicine lcsh:R Albumin Biology and Life Sciences Proteins Protein Complexes Hydrogen Peroxide Binding constant Oxygen Kinetics biology.protein Nanoparticles lcsh:Q |
| Zdroj: | PLoS ONE PLoS ONE, Vol 9, Iss 10, p e110541 (2014) |
| Popis: | A covalent core-shell structured protein cluster composed of hemoglobin (Hb) at the center and human serum albumins (HSA) at the periphery, Hb-HSAm, is an artificial O2 carrier that can function as a red blood cell substitute. Here we described the preparation of a novel Hb-HSA3 cluster with antioxidant activities and its O2 complex stable in aqueous H2O2 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 (O2•-) and hydrogen peroxide (H2O2), i.e., superoxide dismutase and catalase activities. Also, Hb-HSA3 captured PtNP into the external albumin unit (K = 1.1×10(7) M(-1)), yielding an Hb-HSA3(PtNP) cluster. The association of PtNP caused no alteration of the protein surface net charge and O2 binding affinity. The peripheral HSA-PtNP shell prevents oxidation of the core Hb, which enables the formation of an extremely stable O2 complex, even in H2O2 solution. |
| Databáze: | OpenAIRE |
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