Biophysical studies of a transmembrane peptide derived from the T cell antigen receptor |
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Authors: | Ali M De Planque MRR Huynh NT Manolios N Separovic F |
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Institution: | (1) Department of Rheumatology, Wesimead Hospital, Westmead, 2145 Sydney, NSW, Australia;(2) School of Chemistry, University of Melbourne, 3010 Melbourne, VIC, Australia;(3) Department of Rheumatology, Westmead Hospital, Westmead, 2145 Sydney, NSW, Australia |
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Abstract: | Summary 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. |
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Keywords: | 2H NMR 31P NMR T cell antigen receptor CD lipid bilayer |
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