D-enantiomer peptide of the TCRα transmembrane domain inhibits T-cell activation in vitro and in vivo Doron Gerber * , 1 , Francisco J. Quintana † , 1 , Itai Bloch * , Irun R. Cohen † and Yechiel Shai * ,2 * Department of Biological Chemistry and † Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel 2 Correspondence: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. E-mail: Yechiel.Shai@weizmann.ac.il <h3>SPECIFIC AIMS</h3> Intermolecular interactions are sterically constrained. Accordingly, sequence-specific interactions between D and L-stereoisomers were ruled out. This teaching was challenged recently in studies of intramembrane protein assembly. Here, we studied the ability of a TCR transmembrane domain (TMD) D-stereoisomer peptide (D-CP), compared with the L-stereoisomer peptide (L-CP), to interact with native intramembrane protein domains and inhibit T-cell activation. <h3>PRINCIPAL FINDINGS</h3> <h3>1. D-CP is a structural mirror image of L-CP</h3> To test the role of chirality in the recognition process of the TCRα transmembrane domain (TMD), we chemically synthesized three CP peptides: wild-type L-CP, which has been shown to inhibit antigen-specific T cell activation; D-CP, which is a mirror image of the first; and 2G CP, an inactive mutated peptide. Circular dichroism experiments were
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D-enantiomer peptide of the TCRα transmembrane domain inhibits T-cell activation in vitro and in vivo
Gerber, Doron; Quintana, Francisco J.; Bloch, Itai; Cohen, Irun R.; Shai, Yechiel
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, Volume 19 (9): 1190
Fed of American Socs for Experimental Biology – Jul 1, 2005
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