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- W4323031673 abstract "Glycosidases are a type of enzyme that hydrolytically cleave carbohydrates and form glycans for biologically important processes. The inadequacies of glycosidases or their genetic abnormalities are responsible for various diseases. Thus, the development of glycosidase mimetics is of great importance. We have designed and synthesized an enzyme mimetic containing l-phenylalanine, α-aminoisobutyric acid (Aib), l-leucine, and m-Nifedipine. From X-ray crystallography, the foldamer adopts a β-hairpin conformation stabilized by two 10-member and one 18-member NH⋅⋅⋅O=C hydrogen bonds. Moreover, the foldamer was found to be highly efficient in hydrolysing ethers and glycosides in the presence of iodine at room temperature. Further, X-ray analysis shows the backbone conformation of the enzyme mimetic to be almost unchanged after the glycosidase reaction. This is the first example of iodine-supported artificial glycosidase activity with an enzyme mimic at ambient conditions." @default.
- W4323031673 created "2023-03-04" @default.
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- W4323031673 date "2023-05-04" @default.
- W4323031673 modified "2023-10-12" @default.
- W4323031673 title "Synthesis and Structural Investigation of Foldamer‐Based Iodine‐Supported Artificial Glycosidases" @default.
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- W4323031673 doi "https://doi.org/10.1002/cbic.202200758" @default.
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