Mechanistic Study of the sPLA-Mediated Hydrolysis of a Thio-ester Pro Anticancer Ether Lipid.

Secretory phospholipase A (sPLA) is an interesting enzyme for triggered liposomal drug delivery to tumor tissue due the overexpression of sPLA in cancerous tissue. A drug delivery system based on the triggered release of therapeutics from sPLA-sensitive liposomes constituted of pro anticancer ether...

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Publicado en:Journal of the American Chemical Society Vol. 131; no. 34; pp. 12193 - 12201
Autores principales: Linderoth, Lars, Fristrup, Peter, Hansen, Martin, Melander, Fredrik, Madsen, Robert, Andresen, Thomas L., Peters, Günther H.
Formato: Artículo
Publicado: American Chemical Society 9/2/2009
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      dt: 9/2/2009
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      pub: American Chemical Society
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        10.1021/ja901412j
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        atl: Mechanistic Study of the sPLA-Mediated Hydrolysis of a Thio-ester Pro Anticancer Ether Lipid.
      aug:
        au:
          Linderoth, Lars
          Fristrup, Peter
          Hansen, Martin
          Melander, Fredrik
          Madsen, Robert
          Andresen, Thomas L.
          Peters, Günther H.
        affil:
          Department of Chemistry, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
          Novo Nordisk A/S, Protein and Peptide Chemistry 3, Novo Nordisk Park, DK-2760 Måløv, Denmark
          Materials and Process Simulation Center (139-74), California Institute of Technology, Pasadena, California 91125
          LiPlasome Pharma A/S, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
          DTU Nanotech, Technical University of Denmark, DK-4000 Roskilde, Denmark
          Department of Chemistry, MEMPHYS-Center for Biomembrane Physics, Technical University of Denmark, DK-2800 Kgs. Lyngby Denmark
      su:
        Density functionals
        Hydrolysis
        Phospholipids
        Liposomes
        Cytoplasm
        Ethers
      sug:
        subj:
          Density functionals
          Hydrolysis
          Phospholipids
          Liposomes
          Cytoplasm
          Ethers
      ab: Secretory phospholipase A (sPLA) is an interesting enzyme for triggered liposomal drug delivery to tumor tissue due the overexpression of sPLA in cancerous tissue. A drug delivery system based on the triggered release of therapeutics from sPLA-sensitive liposomes constituted of pro anticancer ether lipids, which become cytotoxic upon sPLA-catalyzed hydrolysis has previously been established. To optimize the hydrolysis rate of the lipids and thereby optimizing the release profile of the drugs from the liposomes, we have synthesized a thio-ester pro anticancer ether lipid. Liposomes constituted of this lipid showed an altered rate of hydrolysis by sPLA. We have tested the cytotoxicity of the thio-ester pro anticancer ether lipids toward cancer cells, and the results showed that the cytotoxicity is indeed maintained upon sPLA exposure. To further understand the origin for the observed different hydrolysis rates for the esters, we have applied molecular dynamics simulations and density functional theory. The combination of these theoretical methods has given valuable insight into the molecular mechanism for sPLA action on sulfur-containing phospholipids. It appears that the enzyme-catalyzed hydrolysis of thio-esters follow a different pathway compared to the hydrolysis pathway of the free thio-ester.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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          year: 2009
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