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- W2000400897 abstract "Human serum albumin (HSA) is a versatile protein found at high concentration in blood plasma and binds a range of insoluble endogenous and exogenous compounds. We have shown that complexation of functional molecules into HSA creates unique proteins never seen in nature. Complexing an ironprotoporphyrin IX into a genetically engineered heme pocket of recombinant HSA (rHSA) generates an artificial hemoprotein, which binds O2 reversibly in much the same way as hemoglobin. A pair of site-specific mutations, (i) introduction of a proximal histidine at the Ile-142 position and (ii) substitution of Tyr-161 with Phe or Leu, allows the heme to bind O2. Additional modification on the distal side of the heme pocket provides rHSA(triple mutant)-heme complexes with a variety of O2 binding affinity. Complexing a carboxy-C60-fullerene (CF) into HSA generates a protein photosensitizer for photodynamic cancer therapy. Energy transfer occurs from a photoexcited triplet-state of HSA-CF (HSA-3CF*) to O2, forming singlet oxygen (1O2). This protein does not show dark cytotoxicity, but induceds cell death under visible light irradiation." @default.
- W2000400897 created "2016-06-24" @default.
- W2000400897 creator A5068012041 @default.
- W2000400897 creator A5070166950 @default.
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- W2000400897 date "2009-01-01" @default.
- W2000400897 modified "2023-10-18" @default.
- W2000400897 title "Structural and Mutagenic Approach to Create Human Serum Albumin-Based Oxygen Carrier and Photosensitizer" @default.
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- W2000400897 doi "https://doi.org/10.2133/dmpk.24.287" @default.
- W2000400897 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19745556" @default.
- W2000400897 hasPublicationYear "2009" @default.
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