Use of epi-equisetin for the preparation of a medicament for the prevention and treatment of lipodystrophy syndrome

Abstract

The application discloses an application of epi-Equisetin in preparation of a medicine for preventing and treating a fat metabolism syndrome, wherein the epi-Equisetin is produced by fermentation of a marine fungus Fusarium sp. SCSIO 152, is an isomer of equisetin, and can be used for preparing a medicine for reducing intracellular lipid accumulation, reducing expression of a fat differentiation marker gene, increasing Ucp1 protein expression and reducing a fat cell volume. The application provides a new alternative medicine for treatment of the fat metabolism syndrome.

Description

Technical Field

[0001] This invention belongs to the field of pharmaceutical science, specifically relating to the use of epi-Equisetin in the preparation of drugs for the prevention and treatment of lipid metabolism syndrome. Background Technology

[0002] Metabolic syndrome (MS) is a cluster of closely related cardiovascular disease risk factors, typically including central obesity, hypertension, hyperglycemia, and abnormal lipoproteinemia (usually manifested as high triglyceride and low high-density lipoprotein cholesterol levels). It signifies a significantly increased risk of cardiovascular disease and type 2 diabetes. Treatment for MS focuses primarily on lifestyle modifications, including a healthy diet, physical activity, weight management, and smoking cessation. Pharmacological treatments include antihypertensive drugs such as diuretics, ACE inhibitors, or calcium channel blockers to control hypertension; glucose-lowering drugs such as metformin or SGLT2 inhibitors to control blood sugar levels; and lipid-lowering drugs such as statins to control high cholesterol and high triglycerides. Although current treatment strategies include lifestyle modifications and a range of pharmacotherapy to manage various symptom-related factors, existing drugs do not fully meet patient needs, especially in addressing multiple aspects of the syndrome. Therefore, developing therapeutics for MS with novel targets is of paramount importance. The development of new drugs can not only target untapped biological pathways, but also explore different ways they interact with known pathways, thereby providing a more comprehensive and targeted treatment approach that can greatly improve patients’ prognosis and quality of life.

[0003] Equisetin is a natural product, a terpenoid compound isolated from sponge-derived fungi. Its unique structure and biological activities have attracted widespread interest from researchers. It exhibits various physiological functions in vivo, including antibacterial, antifungal, and antitumor effects. Due to its potential pharmacological value and biological activity, Equisetin has become an important research subject in the field of natural product drug research. In-depth studies of its chemical synthesis, biosynthetic pathways, and biological activities are expected to provide important clues for the development of new treatments and drugs. Diastereomers are isomers of molecules with the same structure but different stereoconfigurations. For Equisetin, different diastereomers can exist; these isomers have the same chemical formula but different stereoconfigurations in space. Because the molecular structure of Equisetin contains multiple stereocenters, it has multiple possible diastereomers. The existence of these diastereomers may affect their biological activities and interaction mechanisms. This study reveals a novel use of 2epi-Equisetin (2-epi epimer) in drugs for the prevention and treatment of metabolic syndrome. Summary of the Invention

[0004] In view of this, one of the objectives of the present invention is to provide the use of epi-Equisetin in the preparation of medicaments for the prevention and treatment of lipid metabolism syndrome.

[0005] To achieve the above objectives, the present invention provides the following technical solution:

[0006] The use of epi-Equisetin in the preparation of drugs for the prevention and treatment of lipid metabolism syndrome, wherein the structural formula of epi-Equisetin is as follows:

[0007]

[0008] The preferred application of the epi-Equisetin in the present invention is in the preparation of a medicament for reducing intracellular lipid accumulation.

[0009] The preferred embodiment of the present invention is the use of epi-Equisetin in the preparation of a drug for reducing the expression of adipogenic differentiation marker genes.

[0010] The preferred use of epi-Equisetin in the preparation of a drug that increases Ucp1 protein expression is preferred in this invention.

[0011] The present invention preferably relates to the use of epi-Equisetin in the preparation of a drug for reducing adipocyte volume.

[0012] The beneficial effects of this invention are as follows: This invention provides the use of epi-Equisetin in the preparation of drugs for the prevention and treatment of lipid metabolism syndrome. Epi-Equisetin is produced by fermentation of the marine fungus Fusarium sp. SCSIO 152 and is an isomer of equisetin. It can reduce intracellular lipid accumulation, reduce the expression of adipocyte differentiation marker genes, increase Ucp1 protein expression, and reduce adipocyte volume, thus providing a new drug candidate for the treatment of lipid metabolism syndrome. Attached Figure Description

[0013] To make the objectives, technical solutions, and beneficial effects of this invention clearer, the following figures are provided for illustration:

[0014] Figure 1Results of the effects of epi-Equisetin on lipid metabolism (A: Effect of epi-Equisetin on neutral lipid accumulation in 3T3-L1 cells, epi-Equisetin (0.25 μM, 0.5 μM, 1 μM) and Equisetin (1 μM); B: Cells were fixed, stained with Oil Red O, and then treated with isopropanol for 30 min. The supernatant was collected, and the absorbance at 510 nm was measured (n=3); *P<0.05; **P<0.01; C: Effect of epi-Equisetin on the pyroptosis differentiation marker gene GS) D: DMD expression; D: epi-Equisetin expression of adipogenic differentiation marker gene C / EBPα; E: epi-Equisetin expression of adipogenic differentiation marker gene Fabp4; F: epi-Equisetin expression of adipogenic differentiation marker gene Pparγ; G: Protein expression; H: Quantitative statistics of Ucp1 protein; I: Quantitative statistics of Fabp4 protein; J: Quantitative statistics of Pparγ protein; K: High-fat diet feeding with epi-Equisetin (40 mg / kg) via gavage, Equis Body shape comparison of mice after 6 weeks of gavage administration of etin as a positive control (40 mg / kg); L: Body weight change graph after 45 days of gavage administration; M: Insulin tolerance test of control, epi-Equisetin (40 mg / kg), and Equisetin (40 mg / kg) mice after 6 weeks of high-fat feeding; N: Glucose tolerance test of control, epi-Equisetin (40 mg / kg), and Equisetin (40 mg / kg) mice after 6 weeks of high-fat feeding; O: Morphological comparison of mouse liver, iWAT, and BAT. Weight and morphological comparison of various mouse tissues; P: Morphological comparison and weight of mouse liver, iWAT and BAT, and weight statistics of various mouse tissues; Q: Effect of epi-Equisetin and EQST on the survival rate of LO2 cells at different concentrations; R: H&E stained sections of control group, epi-Equisetin (40 mg / kg), Equisetin (40 mg / kg) and BAT under high-fat feeding conditions; All values ​​are expressed as mean ± standard deviation; n = 3; *P < 0.05; **P < 0.01). Detailed Implementation

[0015] The present invention will be further described below with reference to the accompanying drawings and specific embodiments, so that those skilled in the art can better understand and implement the present invention. However, the embodiments described are not intended to limit the present invention.

[0016] Example 1: Obtaining epi-Equisetin

[0017] The marine fungus SCSIO 152 was isolated and purified from deep-sea sediments in the northern South China Sea and the strain is preserved at the Marine Microbiology Research Center of the Chinese Academy of Sciences.

[0018] Marine fungus SCSIO 152 was fermented, and the fermentation product was extracted with ethyl acetate. The ethyl acetate was concentrated by distillation to obtain a total extract. The total extract was subjected to silica gel column chromatography using normal phase column chromatography: a gradient of petroleum ether-chloroform (100:0, 80:20, 70:30, 50:50, 0:100 v / v), followed by a gradient of chloroform-methanol (98:2, 95:5, 90:10; 50:50 v / v), yielding nine fractions, Fr.1–9. Antimicrobial activity tracking using Bacillus subtilis showed that Fr.7–8 were the active fractions. Fr.7–8 were combined and subjected to medium-pressure reversed-phase MPLC chromatography (acetonitrile-water gradient elution 0–20 min, 50%–100%, flow rate 20 mL / min) to obtain the fraction Fr.(7-8)-1–Fr.(7-8)-5. HPLC-DAD and activity tracking showed that Fr.(7-8)-3 was the active target product. Finally, the product was purified by preparative high-performance liquid chromatography (CH3CN horizontal gradient elution for 20 min, flow rate 10 mL / min), yielding compounds equisetin(1) (2.2 g) and epi-equisetin(2) (2.0 g) at 16.2 and 17.3 min, respectively. The structures of the compounds are shown below:

[0019]

[0020] Example 2: Evaluation of the lipid-lowering activity of epi-Equisetin

[0021] Tests showed that epi-Equisetin purity was >99%, as indicated by Oil Red O, qPCR, and WB.

[0022] Cell line: 3T3-L1 (mouse embryonic fibroblasts)

[0023] Test method:

[0024] Logarithmic growth phase mouse SVF cells were harvested, digested, counted, and seeded at appropriate concentrations into 6-well plates. Cells were cultured for 24 hours until complete adherence. After cell growth contact inhibition, a lipid accumulation model was established. The drug treatment groups were simultaneously administered epi-Equisetin at concentrations of 0.25 μM, 0.5 μM, and 1 μM; the positive control group was administered Equisetin (1 μM). After 24 hours, the culture medium was discarded, the cells were washed twice with PBS, and fixed with 4% paraformaldehyde at 4°C for 1 hour. The paraformaldehyde was then discarded. Each well was stained with 200 μL of Oil Red O working solution at room temperature for 30 minutes. The results are shown below. Figure 1As shown, epi-Equisetin can significantly reduce lipid droplet formation during preadipocyte differentiation. Oil Red working solution was washed with PBS, and 300 μL of isopropanol was added to each well to dissolve the dye adhering to the lipids. OD values ​​were measured at 510 nm using a microplate reader. Results are shown below. Figure 1 As shown in B.

[0025] The results showed that epi-Equisetin at a concentration of 1 μM could inhibit the formation of lipid droplets in cells, and its efficacy was comparable to that of the positive control drug Equisetin.

[0026] Example 3: Evaluation of epi-Equisetin's RNA Level Expression

[0027] Cell culture: When seeding differentiated cells, use 3T3-L1 cells or mouse SVF cells in logarithmic growth phase, at a density of 10 × 10⁶ cells per well. 4 One cell was seeded in a 6-well plate and cultured until cell contact inhibition was achieved. 1.5 mL of drug-treated adipogenic differentiation induction medium was added to each well.

[0028] After 48 hours, the medium was changed to one containing insulin, IBMX, and dexamethasone. Two days later, it was changed to a medium containing only insulin. The medium was changed every two days until obvious lipid droplets appeared after 4-6 days. When seeding proliferating cells, 5 × 10⁶ 3T3-L1 cells were used per well. 4 Cells were seeded in 6-well plates and treated with drugs the following day.

[0029] RNA extraction: Mature adipocytes after induced differentiation or cells treated with proliferative drugs 24 hours prior were gently rinsed twice with PBS. 1 mL of Trizol was added to each well of a six-well plate, and cells were pipetted from top to bottom. The cell suspension was collected into a 1.5 mL sterile, enzyme-free centrifuge tube and lysed on ice for 30 min. 200 μL of chloroform solution was added to each tube, and the mixture was vortexed and incubated on ice for 10 min. After clear natural stratification, the mixture was centrifuged at 12000 rpm for 15 min at 4°C. The centrifuge tube was carefully removed from the centrifuge. The homogenate was now divided into three layers. The supernatant was carefully transferred to a new centrifuge tube, being careful not to aspirate the white intermediate layer. The upper aqueous phase was transferred to a new, pre-chilled, enzyme-free sterile tube. An equal volume of isopropanol was added, and the mixture was vortexed and incubated on ice for 20 min. The tube was then centrifuged at 12000 rpm for 15 min at 4°C. Discard the supernatant, add pre-cooled 75% ethanol and wash thoroughly, centrifuge at 12000 rpm for 10 min at 4°C; discard the ethanol solution, invert the centrifuge tube and let it air dry. Add 20 μL of DEPC water to dissolve the RNA precipitate, mix well by pipetting, and determine the RNA concentration using Nanodrop 2000.

[0030] Reverse transcription: Prepare a 20 μL reverse transcription system according to the SweScript All-in-One RT SuperMix for qPCR (One-Step gDNA Remover) instructions. Take 0.2 mL centrifuge tubes and add 4 μL of 5×SweScriptAll-in-One SuperMix for qPCR and 4 μL of gDNA Remover to each tube. Calculate the corresponding volume based on the measured RNA concentration. Make up the remaining volume with DEPC water. The reverse transcription reaction program is set as follows: 25℃, 5 min; 42℃, 30 min; 85℃, 5 s; 4℃, incubate. After the reaction, add 180 μL of sterile, enzyme-free water to each tube to obtain cDNA product.

[0031] Real-time quantitative PCR: Prepare a 10 μL PCR reaction mixture, including 5 μL of SYBR qPCR Master Mix (2×), 0.3 μL of upstream primer (10 μmol / L), 0.3 μL of downstream primer (10 μmol / L), 1 μL of cDNA template, and 3.4 μL of ddH2O. After adding the mixture, shake well in the dark and centrifuge for 2 seconds before transferring to the PCR machine. A three-step PCR reaction program was used: 95℃ pre-denaturation for 10 min, 95℃ denaturation for 10 s, 60℃ annealing for 30 s, and 72℃ extension for 30 s, for a total of 40 cycles.

[0032] Primers for quantitative fluorescence detection:

[0033] GSDMD F: 5'-CCATCGGCCTTTGAGAAAGTG-3' (SEQ ID NO. 1);

[0034] R: 5'-ACACATGAATAACGGGGTTTCC-3' (SEQ ID NO. 2);

[0035] CEBP / αF: 5'-CAAGAACAGCAACGAGTACCG-3' (SEQ ID NO. 3);

[0036] R: 5'-GTCACTGGTCAACTCCAGCAC-3' (SEQ ID NO.4);

[0037] FABP4 F: 5'-AAGGTGAAGAGCATCATAACCCT-3' (SEQ ID NO.5);

[0038] R: 5'-TCACGCCTTTCATAACACATTCC-3'SEQ ID NO.6);

[0039] PPARγF: 5'-TCGCTGATGCACTGCCTATG-3' (SEQ ID NO.7);

[0040] R: 5'-GAGAGGTCCACAGAGCTGATT-3' (SEQ ID NO. 8);

[0041] β-actin F: 5'-GTCCCTGACCCTCCCAAAAG-3' (SEQ ID NO.9);

[0042] R: 5'-GCTGCCTCAACACCTCAACCC-3' (SEQ ID NO. 10);

[0043] Data processing: Using β-actin as an internal reference gene, the expression levels of the target gene and the internal reference gene were detected, and 2... -△△Ct The relative expression levels of the two were calculated using the method, and the results are as follows: Figure 1 As shown in the CF diagram. The results indicate that epi-Equisetin significantly reduced the expression of all adipogenic differentiation marker genes.

[0044] Example 4: Evaluation of epi-Equisetin on protein expression

[0045] Cell culture: When seeding differentiated cells, take 3T3-L1 or iWAT cells in logarithmic growth phase and plant them at 10 × 10⁶ cells per well. 4 Cells were seeded into 6-well plates and cultured until cell contact inhibition was observed. 1.5 mL of drug-treated adipogenic differentiation induction medium was added to each well. After 48 hours, the medium was replaced with insulin-only medium, and the medium was gently changed daily for 4-6 days until visible lipid droplets were observed under a microscope. When seeding proliferating cells, 5 × 10⁶ 3T3-L1 cells were used per well. 4 Cells were seeded in 6-well plates and treated with drugs the following day.

[0046] Extraction of total cellular protein: Discard the culture medium in the culture dish, gently wash the cells of each treatment group three times with pre-chilled PBS, add 120 μL of RIPA solution containing 1% each of PMSF, protease inhibitor and phosphatase inhibitor to each well of a 6-well plate, scrape the cells from the culture dish with the tip of a yellow pipette, and collect the cell solution in a 1.5 mL pre-chilled centrifuge tube, incubate on ice for 30 minutes to fully lyse, centrifuge at 12000 rpm for 10 minutes at 4°C, and transfer the supernatant to a new 1.5 mL centrifuge tube.

[0047] Protein concentration determination using the BCA method: Dilute the BSA standard with RIPA. Mix reagent A thoroughly by shaking. Prepare an appropriate amount of BCA working solution by mixing A:B at a volume ratio of 50:1. Add 25 μL of freshly prepared BCA standard solution and the sample to be tested to a 96-well plate. Add 200 μL of BCA working solution to each well of the BSA standard solution and sample, and mix thoroughly. Incubate the 96-well plate at 37°C for 30 minutes until the lowest concentration of BSA standard solution turns purple. Measure the protein concentration using a microplate reader at 560 nm. Establish a standard curve using the BSA standard solution and calculate the protein concentration for each sample based on the standard curve.

[0048] Sample preparation: Mix the supernatant with 5× loading buffer at a ratio of 4:1, heat in a 95°C metal bath for 10 minutes, then cool and aliquot, and finally store at -80°C. Ensure that the protein concentration of each sample is consistent.

[0049] Prepare 10 mL of separating gel (12%): 3.3 mL deionized water, 4.0 mL 30% acrylamide mixture, 2.5 mL 1.5 M Tris-Cl buffer, 100 μL 10% APS, 100 μL 10% SDS, and 4 μL TEMED. Add isopropanol and press the gel onto a flat surface. Let it stand for 30 min, then pour off the isopropanol and rinse thoroughly with double-distilled water.

[0050] Prepare 4 mL of stacking gel (5%): Mix 2.2 mL of deionized water, 0.67 mL of 30% acrylamide mixture, 1 mL of 0.5 M Tris-Cl buffer, 40 μL of 10% APS and 4 μL of TEMED, and add until overflowing. Insert a comb (1.5 mm) and let it air dry for 40 minutes.

[0051] Sample loading: Immerse the polyacrylamide gel in the electrophoresis buffer, remove the comb, and add about 20 μL of protein sample to each lane, or add 5-10 μL of pre-stained protein standard molecular weight marker.

[0052] Solution preparation:

[0053] Electrophoresis buffer: Weigh and add 3.02g Tris, 18.8g glycine and 1g SDS, and bring the volume to 1L with double-distilled water. The components are Tris (25mM), glycine (250mM) and 0.1% SDS.

[0054] Electroporation buffer: Weigh and add 5.82 g Tris, 2.93 g Glycine and 3.75 mL SDS, and bring the volume to 850 mL with double-distilled water. The buffer contains Tris (48 mM), glycine (39 mM) and 10% SDS. Add 150 mL of methanol and mix well before use.

[0055] TBST solution: Weigh and add 12.1g Tris-HCl, 9g sodium chloride, and 1mL Tween 20. Add double-distilled water to a final volume of 1L. The solution contains Tris-HCl (100mM), 0.9% NaCl, and 0.1% Tween. Adjust the pH to 7.6. Blocking solution: Weigh 2.5g of skim goat milk powder and dissolve it thoroughly in 50mL of TBST. Prepare fresh before use.

[0056] 10% APS: Dissolve 1g of APS in 10mL of purified water, then dispense and store at -80℃ for an extended period.

[0057] Electrophoresis: Electrophoresis begins at a constant voltage of 80V for approximately 0.5 hours. Once the bromophenol blue has completely passed through the stacking gel, the voltage is increased to 120V, and protein separation proceeds in the separating gel for approximately 3 hours. Electrophoresis is stopped once the target protein has been completely separated, based on the marker's electrophoretic performance.

[0058] Transfer: Using a Bio-Rad transfer apparatus, the PVDF membrane was soaked in methanol for 3 minutes to activate the membrane surface. The filter paper and PVDF membrane were layered in the following order: sponge → 3 layers of filter paper moistened with transfer buffer → polyacrylamide gel → PVDF membrane → 3 layers of filter paper moistened with transfer buffer → sponge. Air bubbles were removed between the sponge and filter paper using a glass spreader, ensuring no air bubbles were present between each layer. After assembling the transfer apparatus, the protein was transferred onto the PVDF membrane at a constant current of 200 mA for approximately 2.5 hours.

[0059] Blocking: Immediately after the transfer is complete, mark both sides of the PVDF membrane and perform TBST cleaning for 10 minutes. Then, transfer the membrane to a blocking solution containing 5% skim milk powder and slowly shake it on a shaker at room temperature for 2 hours for blocking.

[0060] Primary antibody incubation: Wash the membrane three times in TBST, each time for 10 minutes. Dilute the primary antibody solution appropriately according to the instructions. Then immerse the membrane in the primary antibody solution, gently shake on a shaker, and incubate at room temperature for 2 hours, or overnight at 4°C. Detailed information on the primary antibody can be found in Table 2.

[0061] Secondary antibody incubation: Wash the membrane three times with TBST for 10 min each time. Dilute the secondary antibody at a ratio of 1:3000. Incubate the membrane with the secondary antibody for 1.5 h. Secondary antibody information is shown in Table 3.

[0062] Imaging analysis: The membrane was washed three times with TBST for 10 min each time. The target protein was detected using the Bio-Rad ChemiDoc™ XRS+ imaging system, and its expression level was analyzed. The results are as follows: Figure 1 As shown in G~J. The results showed that epi-Equisetin treatment increased Ucp1 protein expression and decreased Fap4 and Pparγ expression.

[0063] Table 1. Primary Antibody Information

[0064]

[0065] Table 2. Secondary antibodies used in the experiment

[0066]

[0067] Example 5: Evaluation of epi-Equisetin expression in mouse body weight

[0068] Nine male C57BL / 6J mice (Changzhou Cavens Laboratory Animal Co., Ltd.) were purchased and acclimatized to their environment for three weeks. They were then divided into three equal groups based on body weight: a control group (saline), a drug treatment group (epi-Equisetin), and a positive control group (Equisetin). Body weight changes were measured after 45 days of gavage administration. Results are as follows: Figure 1 As shown in K and L. The results indicate that epi-Equisetin gavage significantly prevented phenotypic obesity in mice from week 2 onwards.

[0069] Example 6: Evaluation of epi-Equisetin on glucose tolerance and insulin tolerance in mice

[0070] Mouse preparation: The bedding of each group of mice was changed before the experiment. GTT mice were fasted for one night, and ITT mice were fasted for 4 hours. During the fasting period, the mice were allowed to drink water normally. The weight of each mouse was recorded, and a serial number was marked on the base of the mouse's tail with a marker pen so that the mice being tested could be quickly identified during the experiment.

[0071] Cut off about 2mm from the end of the mouse's tail with scissors, gently squeeze the tail to collect a drop of blood, measure the blood glucose with a blood glucose meter, and recognize the measured value as the blood glucose value at 0 min. The operation should be as gentle as possible so as not to frighten the mouse excessively. After the mouse has adapted for 30 minutes, prepare to inject insulin solution into the peritoneum.

[0072] The mice were gently picked up and injected with insulin solution using a 1 mL syringe according to standard intraperitoneal injection procedures. The injection volume was determined based on the mouse's weight, and the injection dose was 0.01 mL / g. Blood glucose levels were measured at 15 min, 30 min, 45 min, and 60 min, following step (3). After the experiment, each cage of mice was fed. The blood glucose results are shown below. Figure 1 As shown in M ​​and N, the results indicate that epi-Equisetin had no significant effect on insulin sensitivity in mice.

[0073] Example 7

[0074] After the above experiments were completed, the mice were euthanized humanely. Their abdomens were wiped with alcohol, and the abdominal cavities were opened. Morphological comparisons of various mouse tissues, including iWAT, Ewat, BAT, and liver, were collected. The weights of each tissue were also tallied. The results are as follows: Figure 1 As shown in O and P. The results showed that epi-Equisetin treatment significantly reduced the weight of iWAT and BAT. Furthermore, HE staining clearly revealed that BAT and iWAT adipocytes were smaller, such as... Figure 1 As shown in R.

[0075] Example 8

[0076] Dilute the stock solutions of EQST and epi-EQST into the culture medium. The diluted media contain drug concentrations of 1 μM, 10 μM, 20 μM, 40 μM, 60 μM, 80 μM, 100 μM, 120 μM, and 140 μM. Add 100 μL of drug solution to each well (three wells per concentration). MTT assay: Observe LO2 cells 24 hours after drug treatment. Prepare a 5 mg / mL MTT solution from thiazolyl blue powder; any unused solution can be stored at -20°C protected from light. Add 20 μL of MTT solution to each well to a final concentration of 0.5 mg / mL. Incubate at 37°C, 5% CO2, and 90% humidity for 4 hours. Gently aspirate all supernatant from the wells to prevent monolayer cell rupture, and add 200 mL of DMSO solution to each well. Place the well plate in the dark on a shaker and shake for 10 minutes to completely dissolve the formazan. Measure the absorbance at 490 nm using a microplate reader. Process and analyze the results using Excel and Graphpad Prism. Results are as follows: Figure 1 As shown in Figure Q, the survival rate of LO2 cells treated with epi-Equisetin was significantly higher than that treated with EQST at 100 μM.

[0077] The above-described embodiments are merely preferred embodiments provided to fully illustrate the present invention, and the scope of protection of the present invention is not limited thereto. Equivalent substitutions or modifications made by those skilled in the art based on the present invention are all within the scope of protection of the present invention. The scope of protection of the present invention is defined by the claims.

Claims

1. The use of epi-Equisetin in the preparation of drugs for the prevention and treatment of lipid metabolism syndrome, characterized in that: The structural formula of epi-Equisetin is as follows: 。

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