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Chemical synthesis of mirror-image D-version of the immunoglobulin-like domain of TrkA (^DlgC^TrkA), a protein molecule needed for mirror-image screening of D-peptide ligands targeting TrkA, was found to be difficult due to the poor efficiency of intermediate synthesis and final protein folding. To solve this problem, the strategy of removable glycosylation modification was used and found to effectively improve the yield of peptide segment synthesis and ligation. Interestingly, it is important to note that temporary glycosylation at distinct sites of ^DlgC^TrkA led to significant differences in the process of protein folding. More details are discussed in the article by Li et al. on pages 2316—2322.