@article {3221697, title = {Expeditious Synthesis of Multiglycopeptides with Heterogeneous Glycan Cores Derived from a-Dystroglycan Mucin-Like Domain}, journal = {Organic \& Biomolecular Chemistry}, volume = {24}, year = {2026}, note = {An accelerated stirring-based solid-phase process for the equimolar synthesis of heteroglycosylated peptides bearing both Man and α-GalNAc glycan cores was optimized and organized by distinguishing between diffusion-dependent and -independent steps.}, pages = {1889-1898}, abstract = {

Glycosylation is a post-translational modification prevalent in the majority of proteins. Many glycoproteins contain several glycosylation sites, often bearing different glycan moieties. The inherent difficulties of glycopeptide synthesis worsen for heterogeneously glycosylated peptides, as each glycan introduces unique synthetic hurdles. Stirring-assisted solid-phase synthesis proved extremely valuable in accessing post-translational modified peptides. We present the stirring-assisted synthesis of a heterogeneous glycopeptide library, derived from α-Dystroglycan, bearing a variety of glycosylation patterns combining both mannose and GalNAc cores. The developed strategy streamlined the expeditious assembly with the post-assembly manipulation, enabling the procurement of heterogeneously glycosylated peptides in high purity.


\ }, url = {DOI: 10.1039/D6OB00013D}, author = {Dror Ben Abba Amiel and Mattan Hurevich} }