Recombinant human serum albumin containing 3 copies of domain I, Has significant in vitro antioxidative capacity compared to the wild-type

Sadaharu Matsushita, Koji Nishi, Yasunori Iwao, Yu Ishima, Hiroshi Watanabe, Kazuaki Taguchi, Keishi Yamasaki, Toru Maruyama, Masaki Otagiri

研究成果: Article

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Human serum albumin (HSA), the most abundant protein in serum, functions as carrier of drugs and contributes to maintaining serum colloid osmotic pressure. We report herein on the preparation of a genetic recombinant HSA, in which domains II and III were changed to domain I (triple domain I; TDI). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results indicated that the purity of the TDI was equivalent to that of the wild type (WT). Both far- and near-UV circular dichroism (CD) spectra of the TDI showed that its structural characteristics were similar to the WT. Ligand binding capacity was examined by an ultrafiltration method using 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF) and ketoprofen as markers for site I and site II, respectively. The binding capacity of TDI for both ligands was lower than that for the wild type. TDI significantly suppressed the oxidation of dihydrorhodamine 123 (DRD) by H2O2 compared to the WT. Our current results suggest that TDI has great potential for further development as HSA a product having antioxidative functions.

元の言語English
ページ(範囲)1813-1817
ページ数5
ジャーナルBiological and Pharmaceutical Bulletin
40
発行部数10
DOI
出版物ステータスPublished - 2017

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

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