A set of conformationally well-defined L/D-peptide epitopes provides a serological bar code for autoantibody subtypes.

ABSTRACT: Which conformational parameters lead to an antibody-affine peptide antigen? And in how many different conformations can we actually present the respective conformational epitope? To provide answers from a chemical point of view, we direct the bending and tethering of peptide backbones by the utilisation of a hydrophobic cluster, disulfides, and d-amino acids. Each mutation is employed pairwise on directly opposite sides of a β-hairpin. In combination, these synthetic modules guide the formation of complementary β-sheet-like structures, whereby the oppositely configured (l/d-)bi-disulfide pairs form with high regioselectivity. The conformational properties of the peptides are assessed by NMR spectroscopy and correlated with their antibody affinity in ELISA. From a pool of thus designed pept

SUBMITTER: Schrimpf A 

PROVIDER: S-EPMC6075753 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature