Spatial Screening of Cyclic Neoglycopeptides: Identification of Polyvalent Wheat‐Germ Agglutinin Ligands

Abstract

Affinities enhanced by up to 619-fold were found for new ligands of the plant lectin wheat-germ agglutinin (compared to the binding of N-acetylglucosamine (GlcNAc)). These polyvalent neoglycopeptides were identified from screening of a spatially diverse library of type 1. Binding affinity is determined not only by the number of GlcNAc residues but also by the ligand architecture.