Loss of apoB-100 secondary structure and conformation in hydroperoxide rich, electronegative LDL (LDL-). (Articolo in rivista)

Type
Label
  • Loss of apoB-100 secondary structure and conformation in hydroperoxide rich, electronegative LDL (LDL-). (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0891-5849(01)00555-X (literal)
Alternative label
  • Parasassi T., Bittolo Bon G., Brunelli R., Cazzolato G., Krasnowska E.K., Mei G., Sevanian A., Ursini F. (2001)
    Loss of apoB-100 secondary structure and conformation in hydroperoxide rich, electronegative LDL (LDL-).
    in Free radical biology & medicine
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Parasassi T., Bittolo Bon G., Brunelli R., Cazzolato G., Krasnowska E.K., Mei G., Sevanian A., Ursini F. (literal)
Pagina inizio
  • 82 (literal)
Pagina fine
  • 89 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 31 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Farmacologia Traslazionale, CNR, Roma Centro Regionale per l'Aterosclerosi, Ospedale Civile di Venezia, Venezia I Clinica Ostetrica e Ginecologica, Universita' di Roma La Sapienza Dipartimento di Medicina Sperimentale e Scienze Biochimiche Department of Molecular Pharmacology and Toxicology, School of Pharmacy, University of Southern California, Los Angeles (literal)
Titolo
  • Loss of apoB-100 secondary structure and conformation in hydroperoxide rich, electronegative LDL (LDL-). (literal)
Abstract
  • A subpopulation of low-density lipoproteins (LDL) is present in human plasma that contains lipid hydroperoxides and is more negatively charged (LDL-) than normal native LDL. By circular dichroism and tryptophan lifetime measurements we found that apoB-100 secondary structure is markedly decreased and its conformation is severely altered in LDL-. The low tryptophan fluorescence intensity confirms the oxidative degradation of the lipoprotein, and the very long lifetime value of one of its decay components indicates a low polarity environment for the remaining unbleached residues. Either a peculiar folding or, most likely, a sinking of the apoB-100 into the lipid core can account for the observed long lifetime component. Oxidation in vitro produces a similar unfolding of the apolipoprotein but the lifetime of tryptophan fluorescence is shifted to lower values, indicating that the denatured apoprotein remains at the hydrophilic surface of the lipoprotein particle. A disordering and an increased polarity of the LDL- surface lipids was demonstrated by measuring the generalized polarization of 2-dimethylamino-6-lauroylnaphthalene (Laurdan). The looser monolayer packing apparently favors the new conformation of apoB-100 and its sinking into a more hydrophobic environment, possibly accounting for it reduced receptor binding properties. (literal)
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