Document Type
Article
Publication Date
10-12-2020
Department
Chemistry
Keywords
anions, peptides and proteins, monomers, free radicals, post-translational modification
Abstract
We report herein an efficient chemical synthesis of homogeneous human E-cadherin N-linked glycopeptides consisting of a heptapeptide sequence adjacent to the Asn-633 N-glycosylation site with representative N-glycan structures, including a conserved trisaccharide, a core-fucosylated tetrasaccharide, and a complex-type biantennary octasaccharide. The key steps are a chemoselective on-resin aspartylation using a pseudoproline-containing peptide and stereoselective glycosylation using glycosyl fluororide as a donor. This synthetic strategy demonstrates potential utility in accessing a wide range of homogeneous N-linked glycopeptides for the examination of their biological function.
Source Publication Title
Organic Letters
Publisher
American Chemical Society
Volume
22
Issue
21
First Page
8349
DOI
10.1021/acs.orglett.0c02971
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Recommended Citation
Zeng, C., Sun, B., Cao, X., Zhu, J., Oluwadahunsi, O. M., Liu, D., Zhu, H., Zhang, J., Zhang, Q., Zhang, G., Gibbons, C. A., Liu, Y., Zhou, J., & Wang, P. G. (2020). Chemical Synthesis of Homogeneous Human E-Cadherin N-Linked Glycopeptides: Stereoselective Convergent Glycosylation and Chemoselective Solid-Phase Aspartylation. Organic Letters, 22 (21), 8349. https://doi.org/10.1021/acs.orglett.0c02971
Comments
Online access: https://pubs.acs.org/doi/pdf/10.1021/acs.orglett.0c02971