Biophysical studies of a transmembrane peptide derived from the T cell antigen receptor
Ali, M, de Planque, M R R, Huynh, N T, Manolios, N and Separovic, F (2002) Biophysical studies of a transmembrane peptide derived from the T cell antigen receptor. International Journal of Peptide Research and Therapeutics, 8, (3-5), 227-233.
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Core peptide (CP) is a unique peptide derived from the transmembrane sequence of T cell antigen receptor (TCR)-alpha chain and is capable of inhibiting the immune response both invitro and in animal models of T cell mediated inflammation. The structure of CP, with sequence GLRILLLKV, is similar to the amphipathic region of many peptides. Unlike antimicrobial peptides, however, which damage cell membranes, electron microscopy and propidium iodide exclusion assays on cell membranes suggest that CP does not create pores and may act by interfering with signal transduction at the membrane level. To investigate this effect further we report the results of31P and2H solid-state NMR spectroscopy of CP on model membranes. As predicted, even at high concentrations of CP, the structure of model membranes was not significantly perturbed. Only at the very high peptide-to-lipid molar ratio of 1∶10 significant effects on the model membranes were observed. We conclude that CP does not destroy the integrity of the lipid bilayer.
|Keywords:||2H NMR - 31P NMR - T cell antigen receptor - CD - lipid bilayer|
|Divisions:||Faculty of Physical Sciences and Engineering > Electronics and Computer Science > NANO
|Date Deposited:||17 Oct 2007|
|Last Modified:||16 Aug 2012 03:49|
|Further Information:||Google Scholar|
|ISI Citation Count:||1|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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