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

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1813-1817
Number of pages5
JournalBiological and Pharmaceutical Bulletin
Volume40
Issue number10
DOIs
Publication statusPublished - 2017
Externally publishedYes

Keywords

  • Antioxidative property
  • Domain I
  • Human serum albumin
  • Ligand-binding

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

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