T-Cell Antigen Receptor-alpha Chain Transmembrane Peptides: Correlation between Structure and Function |
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Authors: | Marina Ali Noeris K Salam Michael Amon Veronika Bender David E Hibbs Nicholas Manolios |
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Institution: | (1) Department of Rheumatology, Westmead Hospital, Westmead, 2145 Sydney, NSW, Australia;(2) Faculty of Pharmacy, University of Sydney, 2006 Sydney, NSW, Australia |
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Abstract: | Core peptide (CP) is a unique peptide derived from the transmembrane sequence of T cell antigen receptor (TCR)-alpha chain that is capable of inhibiting the immune response both in vitro and in animal models of T cell mediated inflammation. CP contains two basic amino acids (lysine and arginine) in its sequence. The presence of these charged residues interspersed between hydrophobic amino acids is important for function. Here in an attempt to understand CP’s biophysical properties leading to activity we have synthesized a number of CP analogues and correlated their model structure with their biological activity. It became apparent that it is not only the charge of the amino acids but also the nature of the polar amino acids themselves and the topography and spacing between them by hydrophobic amino acids, creating a hydrophobic face, that are critical for CP function.Australian Peptide Conference Issue. |
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Keywords: | Molecular modelling peptides T-cell antigen receptor membranes |
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