Recent advances on discovery of enzyme inhibitors from natural products using bioactivity screening

Yan, Tian‐Ci; Cao, Jun; Ye, Li‐Hong

doi:10.1002/jssc.202200084

Cited by 11 publications

(12 citation statements)

References 104 publications

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“…Enzymes are a type of biological substance that maintain the homeostasis and balance of the human body by catalyzing metabolic responses and modulating cells. Enzyme inhibitors can slow the progression of many diseases [ 1 ]. α-Glucosidase (α-GLU) is one of the important targets of diabetes, and acarbose, a α-GLU inhibitor, has been widely used to treat diabetes.…”

Section: Introductionmentioning

confidence: 99%

“…Xanthine oxidase (XOD) is the key enzyme of gout, and its inhibitor (allopurinol) is a commonly used gout treatment drug. Tyrosinase (TYR) is related to pigmented skin diseases such as chloasma and senile plaques, and acetylcholinesterase (ACHE) is related to Alzheimer’s disease [ 1 , 2 , 3 ]. Currently, the enzyme inhibitors majorly originate from chemical synthetic, and natural products [ 1 ].…”

Section: Introductionmentioning

confidence: 99%

“…Tyrosinase (TYR) is related to pigmented skin diseases such as chloasma and senile plaques, and acetylcholinesterase (ACHE) is related to Alzheimer’s disease [ 1 , 2 , 3 ]. Currently, the enzyme inhibitors majorly originate from chemical synthetic, and natural products [ 1 ]. Chemical synthetic enzyme inhibitors usually have some side effects; for example, acarbose carries the risk of skin allergy and liver damage, while allopurinol carries the risk of liver and kidney damage [ 3 , 4 , 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

“…Chemical synthetic enzyme inhibitors usually have some side effects; for example, acarbose carries the risk of skin allergy and liver damage, while allopurinol carries the risk of liver and kidney damage [ 3 , 4 , 5 , 6 ]. To find safer enzyme inhibitors, screening enzyme inhibitors from natural products has become a research hotspot, and many natural inhibitors, such as huperzine-A, ursolic acid, and resveratrol, have been discovered [ 1 , 7 ]. However, due to the complex composition of natural products, screening enzyme inhibitors from them is extremely difficult [ 1 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

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Screening of Tyrosinase, Xanthine Oxidase, and α-Glucosidase Inhibitors from Polygoni Cuspidati Rhizoma et Radix by Ultrafiltration and HPLC Analysis

Chen

Huang

et al. 2023

Molecules

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Polygoni Cuspidati Rhizoma et Radix (PCR), the rhizome and root of Polygonum cuspidatum Sieb. et Zucc., has been used as an herbal medicine for a long time. In this study, the ultrafiltration combined with high performance liquid chromatography (UF-HPLC) method was developed to screen tyrosinase (TYR), α-glucosidase (α-GLU), and xanthine oxidase (XOD) inhibitors from PCR. Firstly, the inhibitory activity of 50% methanol PCR extract on TYR, α-GLU, XOD, and acetylcholinesterase (ACHE) was tested. The extract showed a good inhibition on the enzymes, except for ACHE. Therefore, UF-HPLC experiments were carried out to screen TYR, α-GLU, and XOD inhibitors from PCR extract. Seven potential bioactive components were discovered, including methylgallate (1), 1,6-di-O-galloyl-D-glucose (2), polydatin-4′-O-D-glucoside (3), resveratrol-4′-O-D-glucoside (4), polydatin (5), malonyl glucoside resveratrol (6), and resveratrol-5-O-D-glucoside (7). Most of them were found as enzyme inhibitors from PCR for the first time, except polydatin (5), which had been reported as an α-GLUI in PCR in the literature. Finally, molecular docking analysis was applied to validate the interactions of these seven potential active components with the enzymes. Compounds 1–7 were proven as TYR inhibitors, compounds 2, 4–7 were identified as XOD inhibitors, and compounds 4–6 were confirmed as α-GLU inhibitors. In short, the current study provides a good reference for the screening of enzyme inhibitors through UF-HPLC, and provides scientific data for future studies of PCR.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Screening of Tyrosinase, Xanthine Oxidase, and α-Glucosidase Inhibitors from Polygoni Cuspidati Rhizoma et Radix by Ultrafiltration and HPLC Analysis

Chen

Huang

et al. 2023

Molecules

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“…Hydrodynamic and/or electroosmotic flows, upon application of pressurization and/or high voltage, respectively, are used in this case as driving forces to introduce samples and reagents and trigger mixing inside the capillary. Two main strategies were accordingly developed for this purpose, including transverse diffusion of laminar flow profiles (TDLFP), where a hydrodynamic flow is created to deform the boundaries of reagent and analyte plugs to facilitate diffusion and thus mixing [26, 27], and electrophoretically mediated microanalysis (EMMA), in which compounds are mixed via the difference in their electrophoretic mobilities under an electric field [28–30]. The application of EMMA is limited when some reactants are sensitive to the electric field when the electrophoretic mobilities of several reactants are similar or the reaction requires too many reaction components.…”

Section: Introductionmentioning

confidence: 99%

In capillary labeling and online electrophoretic separation of N‐glycans from glycoproteins

Yang

Duc

Tran

et al. 2022

J of Separation Science

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In this study, we present a new approach for in-capillary fluorescent labeling of N-glycans prior to their analysis with CE coupled with laser-induced fluorescent detection. This integrated approach allows using a CE capillary as a microreactor to perform several steps required for labeling glycans with 8aminopyrene-1,3,6 trisulfonic acid and at the same time as a separation channel for CE of fluorescently labeled glycans. This could be achieved through careful optimization of all different steps, including sequential injections of fluorescent dye and glycan plugs, mixing by transverse diffusion of laminar flow profiles, incubation in a thermostatic zone, and finally separation and detection with CE. Such a complex sample treatment protocol for glycan labeling that is feasible thus far only in batchwise mode can now be converted into an automated and integrated protocol. Our approach was applied successfully to analyze fluorescently labeled N-linked oligosaccharides released from human immunoglobulin G and rituximab, a monoclonal antibody used for cancer treatment. We demonstrated the superiority of this in-capillary approach over the conventional in-tube protocol, with fourfold less reagent consumption and full automation without remarkable degradation of the glycan separation profile obtained by capillary electrophoresis.

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Screening of inhibitors on successful covalent tyrosinase coupling with help from SpyBank

Yi,

Gong,

Cui

et al. 2024

Biomedical Chromatography

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Microbial metabolites are an important source of tyrosinase (TYR) inhibitors because of their rich chemical diversity. However, because of the complex metabolic environment of microbial products, it is difficult to rapidly locate and identify natural TYR inhibitors. Affinity‐based ligand screening is an important method for capturing active ingredients in complex samples, but ligand immobilization is an important factor affecting the screening process. In this paper, TYR was used as ligand, and the SpyTag/SpyCatcher coupling system was used to rapidly construct affinity chromatography vectors for screening TYR inhibitors and separating active components from complex samples. We successfully expressed SpyTag–TYR fusion protein and SpyCatcher protein, and incubated SpyCatcher protein with epoxy‐activated agarose. The SpyTag–TYR protein was spontaneously coupled with SpyCatcher to obtain an affinity chromatography filler for immobilization of TYR, and the performance of the packaging material was characterized. Finally, compound 1 with enzyme inhibitory activity was successfully obtained from the fermentation product of marine microorganism C. Through HPLC, MS, 1H NMR and 13C NMR analyses, its structure was deduced as azelaic acid, and its activity was analyzed. The results showed that this is a feasible method for screening TYR inhibitors in complex systems.

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Recent advances on discovery of enzyme inhibitors from natural products using bioactivity screening

Cited by 11 publications

References 104 publications

Screening of Tyrosinase, Xanthine Oxidase, and α-Glucosidase Inhibitors from Polygoni Cuspidati Rhizoma et Radix by Ultrafiltration and HPLC Analysis

Screening of Tyrosinase, Xanthine Oxidase, and α-Glucosidase Inhibitors from Polygoni Cuspidati Rhizoma et Radix by Ultrafiltration and HPLC Analysis

In capillary labeling and online electrophoretic separation of N‐glycans from glycoproteins

Screening of inhibitors on successful covalent tyrosinase coupling with help from SpyBank

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