Liposome membrane can act like molecular and metal chaperones for oxidized and fragmented superoxide dismutase

Le Quoc Tuan, Hiroshi Umakoshi, Toshinori Shimanouchi, Ryoichi Kuboi

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

A mechanism for liposome-recruited activity of oxidized and fragmented superoxide dismutase (Fr.-SOD) [Tuan LQ, Umakoshi H, Shimanouchi T, Kuboi R. Liposome-recruited activity of oxidized and fragmented superoxide dismutase. Langmuir 2008;24:350-4] was further investigated, focusing on the secondary structure of Fr.-SOD. Liposome membrane was found to assist the conformational change of Fr.-SOD and reactivate the enzymatic activity, like molecular and metal chaperones. The loss of SOD activity and its secondary structure was observed during 6 h oxidation in 2 mM hydrogen peroxide. The contents of the α-helix and β-sheet structures in the oxidized and fragmented SOD (2 μM) were increased only in the presence of 10 μM Cu2+ and Zn2+ together, or in the presence of 2 mM POPC liposomes. The mixture of all of these elements (fragmented SOD and POPC liposomes with Cu2+ and Zn2+) gave not only the increase of the α-helix and β-sheet contents but also the mediation of the high SOD-like activity.

Original languageEnglish
Pages (from-to)101-106
Number of pages6
JournalEnzyme and Microbial Technology
Volume44
Issue number2
DOIs
Publication statusPublished - Feb 5 2009
Externally publishedYes

Keywords

  • Chaperones
  • Enzymatic activity
  • Hydrogen peroxide
  • Liposomes
  • Superoxide dismutase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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