http://www.cnr.it/ontology/cnr/individuo/prodotto/ID318364
Binding of a Monoclonal Antibody to the Phospholamban Cytoplasmic Domain Interferes with the Channel Activity of Phospholamban Reconstituted in a Tethered Bilayer Lipid Membrane (Articolo in rivista)
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- Label
- Binding of a Monoclonal Antibody to the Phospholamban Cytoplasmic Domain Interferes with the Channel Activity of Phospholamban Reconstituted in a Tethered Bilayer Lipid Membrane (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/la501660u (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Serena Smeazzetto (1); Alessio Sacconi (1); Adrian L. Schwan (2); Giancarlo Margheri (3); Francesco Tadini-Buoninsegni (1) (literal)
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- Publication Date (Web): August 14, 2014. (literal)
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- http://pubs.acs.org/doi/abs/10.1021/la501660u (literal)
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- (1) Department of Chemistry \"Ugo Schiff\", University of Florence, 50019 Sesto Fiorentino, Italy
(2) Department of Chemistry, University of Guelph, Guelph, ON Canada, N1G 2W1
(3) Institute for Complex Systems, National Research Council, 50019 Sesto Fiorentino, Italy (literal)
- Titolo
- Binding of a Monoclonal Antibody to the Phospholamban Cytoplasmic Domain Interferes with the Channel Activity of Phospholamban Reconstituted in a Tethered Bilayer Lipid Membrane (literal)
- Abstract
- Phospholamban (PLN), a membrane protein present in the sarcoplasmic reticulum of cardiac myocytes, is a crucial regulator of cardiac function. It is known that PLN appears as a monomer and as a pentamer. However, the role of the PLN pentamer and its ability to generate an ion channel are a matter of debate. To address this issue we employed an experimental approach that combines electrochemical impedance spectroscopy and surface plasmon resonance measurements. In particular, we investigated the channel activity of wildtype PLN reconstituted in a tethered bilayer lipid membrane (tBLM) on a gold surface. Our results indicate that reconstituted PLN can generate ion-conducting channels in a tBLM. Experiments with a PLN monoclonal antibody support an oriented incorporation of PLN in the tBLM. We show that the binding of the antibody to the PLN cytoplasmic domain interferes with PLN channel activity. (literal)
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