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  • Title: Synthesis and antibody recognition of cyclic epitope peptides, together with their dimer and conjugated derivatives based on residues 9-22 of herpes simplex virus type 1 glycoprotein D.
    Author: Jakab A, Schlosser G, Feijlbrief M, Welling-Wester S, Manea M, Vila-Perello M, Andreu D, Hudecz F, Mezo G.
    Journal: Bioconjug Chem; 2009 Apr; 20(4):683-92. PubMed ID: 19271736.
    Abstract:
    The synthesis of new cyclic peptides comprising the 9-22 epitope (9)LKMADPNRFRGKDL(22) sequence derived from HSV gD-1 is reported. In addition, we describe procedures for the preparation of cyclic peptide dimers and conjugates with an oligotuftsin derivative carrier. The binding of a monoclonal antibody, Mab A16, to the synthesized compounds was determined by enzyme-linked immunosorbent assay. It was demonstrated that cyclization decreased the binding activity of the antibody to the epitope. However, dimerization and conjugation could significantly increase the binding capacity of the cyclic epitope peptides. The attachment site in dimers and conjugates, as well as the topology of the construct, had a significant influence on the antibody recognition, while replacement of Met in position 11 by Nle had no marked effect.
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