http://www.cnr.it/ontology/cnr/individuo/prodotto/ID271433
Design of a novel LOX-1 receptor antagonist mimicking the natural substrate (Articolo in rivista)
- Type
- Label
- Design of a novel LOX-1 receptor antagonist mimicking the natural substrate (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbrc.2013.07.073 (literal)
- Alternative label
Falconi, Mattia; Ciccone, Sarah; D'Arrigo, Paola; Viani, Fiorenza; Sorge, Roberto; Novelli, Giuseppe; Patrizi, Patrizia; Desideri, Alessandro; Biocca, Silvia (2013)
Design of a novel LOX-1 receptor antagonist mimicking the natural substrate
in Biochemical and biophysical research communications (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Falconi, Mattia; Ciccone, Sarah; D'Arrigo, Paola; Viani, Fiorenza; Sorge, Roberto; Novelli, Giuseppe; Patrizi, Patrizia; Desideri, Alessandro; Biocca, Silvia (literal)
- Pagina inizio
- Pagina fine
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WoS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- University of Rome Tor Vergata; University of Rome Tor Vergata; University of Rome Tor Vergata; Polytechnic University of Milan; Polytechnic University of Milan; Consiglio Nazionale delle Ricerche (CNR); University of Rome Tor Vergata; BIOS FIANO Srl (literal)
- Titolo
- Design of a novel LOX-1 receptor antagonist mimicking the natural substrate (literal)
- Abstract
- The lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1), the major receptor for oxidized low-density lipoprotein (ox-LDL) in endothelial cells, is overexpressed in atherosclerotic lesions. LOX-1 specific inhibitors, urgently necessary to reduce the rate of atherosclerotic and inflammation processes, are not yet available. We have designed and synthesized a new modified oxidized phospholipid, named PLAzPC, which plays to small scale the ligand-receptor recognition scheme. Molecular docking simulations confirm that PLAzPC disables the hydrophobic component of the ox-LDL recognition domain and allows the interaction of the L-lysine backbone charged groups with the solvent and with the charged/polar residues located around the edges of the LOX-1 hydrophobic tunnel. Binding assays, in a cell model system expressing human LOX-1 receptors, confirm that PLAzPC markedly inhibits ox-LDL binding to LOX-1 with higher efficacy compared to previously identified inhibitors. (C) 2013 Elsevier Inc. All rights reserved. (literal)
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