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- W3048809541 abstract "Glycosylation is a promising strategy for modulating the physicochemical properties of peptides. However, the influence of glycosylation on the biological activities of peptides remains unknown. Here, we chose the bee venom peptide HYL as a model peptide and 12 different monosaccharides as model sugars to study the effects of glycosylation site, number, and monosaccharide structure on the biochemical properties, activities, and cellular selectivities of HYL derivatives. Some analogues of HYL showed improvement not only in cell selectivity and proteolytic stability but also in antitumor and antimicrobial activity. Moreover, we found that the helicity of glycopeptides can affect its antitumor activity and proteolytic stability, and the α-linked d-monosaccharides can effectively improve the antitumor activity of HYL. Therefore, it is possible to design peptides with improved properties by varying the number, structure, and position of monosaccharides. What’s more, the glycopeptides HYL-31 and HYL-33 show a promising prospect for antitumor and antimicrobial drugs development, respectively. In addition, we found that the d-lysine substitution strategy can significantly improve the proteolytic stability of HYL. Our new approach provides a reference or guidance for the research of novel antitumor and antimicrobial peptide drugs." @default.
- W3048809541 created "2020-08-18" @default.
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- W3048809541 date "2020-08-10" @default.
- W3048809541 modified "2023-10-14" @default.
- W3048809541 title "Effects of Glycosylation and <scp>d</scp>-Amino Acid Substitution on the Antitumor and Antibacterial Activities of Bee Venom Peptide HYL" @default.
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- W3048809541 doi "https://doi.org/10.1021/acs.bioconjchem.0c00355" @default.
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