Abstract:

Glycosylation is among the most common posttranslational
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.

Notes:

We report the accelerated, high-shear stirring-assisted synthesis of
multiply O-glycosylated peptides

 

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