Expeditious Synthesis of a Glycopeptide Library

Abstract

Short proteoglycan fragments are of great importance for biochemical research. The solid‐phase synthesis of such glycopeptides relies on excessive use of glycosylated amino acids, extended reaction times, and additional post‐assembly deprotection protocols. We employed high‐shear mixing for expedient and equimolar O‐glycopeptide assembly. We further developed a stirring‐based deprotection on the solid support, thus completing the synthesis of a glycopeptide library in a minimal amount of time and purification hurdles.

Accelerated solid-phase synthesis of glycopeptides containing multipleN-glycosylated sites

“…The synthetic method used for the synthesis of glycopeptides GP-n follows the protocols set up for other post-translationally modified peptides by HTFS-PS. 21,22 All syntheses were carried out in the same reactor, using 100 mg of solid support. All the steps in the process were performed at 90 °C with a stirring of 1200 rounds per minute (rpm).…”

“…The strategy proved extremely useful for the synthesis of PTM-peptides, such as a set of O-glycopeptides that were assembled in minutes using equimolar amounts of Gbb. 21 The strategy was also utilized for the synthesis of a set of multi-phosphorylated peptides in which the difficulty of the synthesis increased with the number and the proximity of the phosphorylation sites. 22 For each PTM (e.g., phosphorylation), the same reactor was used but the chemistry was tailored to match the specific characteristics of the peptides.…”