Immobilization of α-Glucosidase on Polyethylene Glycol Diglycidyl Ether-Modified NH2-MIL-53(Al) for Inhibitory Activity Assay of Traditional Chinese Medicine DOI

Guang‐Zhen Wan,

Jia Liu, Juan Chen

и другие.

Langmuir, Год журнала: 2025, Номер unknown

Опубликована: Фев. 9, 2025

Enzyme inhibition-based drug screening is a critical strategy in development. However, significant limitations arise from the instability, limited reusability, and narrow applicability of traditional enzyme assays when for inhibitors complex matrices, such as extracts Chinese medicines (TCMs). A was developed that combines capillary electrophoresis (CE) with an enzymatic assay utilizing covalently immobilized α-glucosidase (α-Glu). NH2-MIL-53(Al) synthesized using hydrothermal method, serving robust support immobilization. By employing polyethylene glycol diglycidyl ether (PEGDGE) covalent linker, enhancements stability reusability α-Glu were achieved. The maintained 77.7% its initial activity over 10 cycles displayed Michaelis–Menten constant 1.25 mM. Moreover, inhibition IC50 values acarbose determined to be 17.41 μM 0.46 μM, respectively. Utilizing this system, 12 TCMs identified several potent inhibitors, including Chebulae Fructus Curcumae Longae Rhizoma. These results highlight successful integration PEGDGE creating stable reusable platform inhibitors. This approach not only advances field immobilization technology but also provides promising pathway discovering antidiabetic agents natural sources.

Язык: Английский

Immobilization of α-Glucosidase on Polyethylene Glycol Diglycidyl Ether-Modified NH2-MIL-53(Al) for Inhibitory Activity Assay of Traditional Chinese Medicine DOI

Guang‐Zhen Wan,

Jia Liu, Juan Chen

и другие.

Langmuir, Год журнала: 2025, Номер unknown

Опубликована: Фев. 9, 2025

Enzyme inhibition-based drug screening is a critical strategy in development. However, significant limitations arise from the instability, limited reusability, and narrow applicability of traditional enzyme assays when for inhibitors complex matrices, such as extracts Chinese medicines (TCMs). A was developed that combines capillary electrophoresis (CE) with an enzymatic assay utilizing covalently immobilized α-glucosidase (α-Glu). NH2-MIL-53(Al) synthesized using hydrothermal method, serving robust support immobilization. By employing polyethylene glycol diglycidyl ether (PEGDGE) covalent linker, enhancements stability reusability α-Glu were achieved. The maintained 77.7% its initial activity over 10 cycles displayed Michaelis–Menten constant 1.25 mM. Moreover, inhibition IC50 values acarbose determined to be 17.41 μM 0.46 μM, respectively. Utilizing this system, 12 TCMs identified several potent inhibitors, including Chebulae Fructus Curcumae Longae Rhizoma. These results highlight successful integration PEGDGE creating stable reusable platform inhibitors. This approach not only advances field immobilization technology but also provides promising pathway discovering antidiabetic agents natural sources.

Язык: Английский

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