131287-39-3Relevant articles and documents
Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy
Li, Yulei,Zhang, Yihan,Wu, Minghao,Chang, Qi,Hu, Honggang,Zhao, Xia
, p. 516 - 525 (2019)
As a host defense peptide, hymenochirin-1B has attracted increasing attention for its strong cytotoxic activities. However, its poor selectivity and proteolytic stability remain major obstacles for clinical application. To solve these problems, we designed and synthesized a series of peptide analogues of hymenochirin-1B based on cationic residue substitution and stapling combined with a glycosylation strategy. Some analogues showed improvement not only in selectivity and proteolytic stability but also in antitumor activity. Among them, the glycosylated stapled peptide H-58 was identified as the most potential antitumor peptide. Flow cytometry and a competitive binding assay revealed that H-58 displayed significant antitumor selectivity. Confocal microscopy and nuclear staining with Hoechst dye demonstrated that H-58 entered the nucleus and caused DNA damage. In summary, the strategy of glycosylated stapled peptides is a promising approach for improving the antitumor selectivity, proteolytic stability, and antitumor activity of hymenochirin-1B, which can be used for other bioactive peptide modifications.
Synthesis of PNGase-resistant N-glycopeptide containing an α-anomeric glycosidic linkage
Dao, Yuankun,Dong, Suwei,Dong, Weidong,Zhang, Jun
, (2022/03/01)
N-glycans in eukaryotic proteins are commonly attached to asparagine residues via β-N-glycosidic linkages, which are susceptible to glycosidases, such as PNGase. Here we report the preparation of α-N-glycosylated peptides based on the solid-phase peptide synthesis strategy using an α-N-GlcNAc-containing asparagine building block, and a transglycosylation reaction of oligosaccharide oxazoline promoted by endoglycosidases CCN180H. The resultant glycopeptide, bearing the complex-type α-N-sialyl undecasaccharide, exhibits resistance against PNGase F, which may be of potential use in studying the catabolism of N-glycans and glycoengineering those peptide-based therapeutics.
Total Synthesis of Glycosylated Human Interferon-γ
Ashhurst, Anneliese S.,Dowman, Luke J.,Fairbanks, Antony J.,Kwan, Ann,Larance, Mark,Li, Henry Y.,Payne, Richard J.,Wang, Xiaoyi,Watson, Emma E.
, p. 6863 - 6867 (2020/09/15)
Interferon-γ(IFN-γ) is a glycoprotein that is responsible for orchestrating numerous critical immune induction and modulation processes and is used clinically for the treatment of a number of diseases. Herein, we describe the total chemical synthesis of homogeneously glycosylated variants of human IFN-γusing a tandem diselenide-selenoester ligation-deselenization strategy in the C- to N-terminal direction. The synthetic glycoproteins were successfully folded, and the structures and antiviral functions were assessed.
