Selection of Galectin-Binding Ligands from Synthetic Glycopeptide Libraries

Galectins, a class of carbohydrate-binding proteins, play a crucial role in various physiological and disease processes. Therefore, the identification of ligands that efficiently bind these proteins could potentially lead to the development of new therapeutic compounds. In this study, we present a method that involves screening synthetic click glycopeptide libraries to identify lectin-binding ligands with low micromolar affinity. Our methodology, initially optimized using Concanavalin A, was subsequently applied to identify binders for the therapeutically relevant galectin 1. Binding affinities were assessed using various methods and showed that the selected glycopeptides exhibited enhanced binding potency to the target lectins compared to the starting sugar moieties. This approach offers an alternative means of discovering galectin-binding ligands as well as other carbohydrate-binding proteins, which are considered important therapeutic targets. Lectin ligands: A methodology enabling the identification of lectin-binding ligands with enhanced affinities to Concanavalin A and Galectin 1 selected from click glycopeptide libraries is described. The obtained results indicate that this method provides a promising approach to identify ligands for galectins and other therapeutically-interesting carbohydrate-binding proteins.image