D‐enantiomer peptide of the TCRa transmembrane domain inhibits T‐cell activation in vitro and in vivo

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Abstract
SPECIFIC AIMSIntermolecular 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.PRINCIPAL FINDINGS1. D-CP is a structural mirror image of L-CPTo 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 performed to ensure that the secondary structure of the D-CP was indeed a mirror image of the L-CP. Experiments were performed in a zwitterio...