Papers

May, 2008

Liposome modified with Mn-porphyrin complex can simultaneously induce antioxidative enzyme-like activity of both superoxide dismutase and peroxidase

LANGMUIR
  • Hiroshi Umakoshi
  • ,
  • Kengo Morimoto
  • ,
  • Yuji Ohama
  • ,
  • Hideto Nagami
  • ,
  • Toshinori Shimanouchi
  • ,
  • Ryoichi Kuboi

Volume
24
Number
9
First page
4451
Last page
4455
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1021/la800174n
Publisher
AMER CHEMICAL SOC

An antioxidative liposome catalysis that mimics both superoxide dismutase (SOD) and peroxidase (POD) activities has been developed by using the liposomes modified with lipophilic Mn - (5,10,15,20-tetrakis[1-hexadecylpyridium-4-yl]-21H,23H-porphyrin) (Mn - HPyP). The SOD- and POD-like activities of the Mn - HPyP-modified liposome were first investigated by varying the type of phospholipid, such as 1,2-distearyl-sn-glycero-3-phosphocholine (DSPC), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), and 1,2-dilauroyi-sn-glycero-3-phosphocholine (DLPC). Higher SOD-like activity was obtained in the case of DLPC and DMPC liposomes, in which the ligands were well-dispersed on the membrane in the liquid crystalline phase. The POD-like activity was maximal in the case of DMPC liposome, in which the Mn - HPyP complex was appropriately clustered on the membrane in the gel phase. On the basis of the above results, the co-induction of the SOD and POD activities to eliminate the superoxide and also hydrogen peroxide as a one-pot reaction was finally performed by using the Mn - HPyP-modified DMPC liposome, resulting in an increase in the efficiency of the elimination of both superoxide and hydrogen peroxide.

Link information
DOI
https://doi.org/10.1021/la800174n
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/18366234
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000255432000008&DestApp=WOS_CPL
URL
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=44249106879&origin=inward
ID information
  • DOI : 10.1021/la800174n
  • ISSN : 0743-7463
  • Pubmed ID : 18366234
  • SCOPUS ID : 44249106879
  • Web of Science ID : WOS:000255432000008

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