Effect of Noncanonical Amino Acids on Protein−Carbohydrate-Interactions

Under the title : "Effect of Noncanonical Amino Acids on Protein−Carbohydrate Interactions" the article describes how the incorporation of a non canonical amino acids, eg. fluorinated tryptophan analogs is modulating the structure, dynamics and the affinity of protein-carbohydrate interactions. The authors used a synthetic biology approach to incorporate these noncanonical amino acids into the bacterial lectin (Ralstonia solanacearum).

Throughout a series of highly accurate measurements complemented by computational modeling studies, the authors observed differences in stability and affinity toward fucosylated glycans. While fluorination decreases the aromaticity of the indole ring and, therefore, the strength of carbohydrate−aromatic interactions, additional weak hydrogen bonds are formed between fluorine and the ligand.