Dror Ben Abba Amiel, Hen Okshtein, Israel Alshanski, Zvi Hayouka, Shlomo Yitzchaik, Mattan Hurevich
Abstract Glycosylation is among the most common post-translational modifications of proteins. There is a great synthetic and practical difficulty in the assembly and deprotection of glycopeptides. State-of-the-art methods for glycopeptide synthesis are wasteful of glycosylated amino acids, are slow, and suffer from low yields. These shortcomings hamper accessibility to multiply glycosylated peptides. We report the accelerated, high-shear stirring-assisted synthesis of multiply O-glycosylated peptides. The equimolar assembly was streamlined with deacetylation to provide multiglycosylated peptides at high purity. Cadherin-derived multiglycosylated peptides synthesized in large quantities provided selective Listeria monocytogenes electrochemical biosensing.