AI Article Synopsis
- - The text discusses the importance of peptide fragments of glycoproteins with multiple -glycosylated sites for studying protein interactions and developing new diagnostics and immunotherapies.
- - Challenges in solid-phase synthesis of these glycopeptides stem from difficult couplings, leading to low yields and requiring more reagents and time.
- - The proposed solution is a method called High-Temperature Fast Stirring Peptide Synthesis (HTFS-PS), which uses heating and stirring with low-loading solid supports to improve the efficiency and yield of glycopeptide synthesis.
Article Abstract
Peptide fragments of glycoproteins containing multiple -glycosylated sites are essential biochemical tools not only to investigate protein-protein interactions but also to develop glycopeptide-based diagnostics and immunotherapy. However, solid-phase synthesis of glycopeptides containing multiple -glycosylated sites is hampered by difficult couplings, which results in a substantial drop in yield. To increase the final yield, large amounts of reagents but also time-consuming steps are required. Therefore, we propose herein to utilize heating and stirring in combination with low-loading solid supports to set up an accelerated route to obtain, by an efficient High-Temperature Fast Stirring Peptide Synthesis (HTFS-PS), glycopeptides containing multiple -glycosylated sites using equimolar excess of the precious glycosylated building blocks.
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| http://dx.doi.org/10.1039/d2ob01886a | DOI Listing |
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