The front cover picture shows the structure of the natural product FR258900, an inhibitor of glycogen phosphorylase (GP), which served as the lead compound for several series of synthetic analogues. Binding mode of the best inhibitor in the allosteric site of GP as revealed by molecular docking was also illustrated. It was shown by synthesis, enzyme kinetics, and computational methods that inhibitory compounds have two acyl side chains and tartaric acid can replace the pentanedioic acid core of the lead. Details of these studies including a quantitative structure–activity relationship suitable for further design of inhibitors are described in the Full Paper by L. Somsák et al. on
Invited for this month’s cover are a group of collaborators from the University of Debrecen (L. Somsák and P. Gergely) and the Institute of Chemistry of the Slovak Academy of Sciences (I. Tvaroška). The cover picture shows the natural product FR258900, some synthetic analogues, and the binding of the most active inhibitor to the allosteric site of the enzyme. Read the full text of the article at
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