A reliever for improving diabetes symptoms

Abstract

The present invention provides a mitigating agent for improving the symptoms of diabetes, and belongs to the field of medical technology. The mitigating agent is composed of a polypeptide extracted from algae hook shrimp and a pharmaceutically acceptable carrier, wherein the polypeptide is a 200Da-500Da algae hook shrimp polypeptide. The extraction method of the algae hook shrimp polypeptide comprises: mixing the algae hook shrimp powder with distilled water, adjusting the pH to 8, adding pancreatic enzymes for enzymolysis at 37°C for 3 hours; then adjusting the pH to 7, adding papain for enzymolysis at 55°C for 5 hours; heating to 95°C, inactivating the enzyme, and centrifuging the supernatant; after pretreatment with a 0.45 micron filter membrane, separating by 500Da and 200Da nanofiltration membranes, obtaining a 200Da-500Da polypeptide solution, and performing vacuum freeze drying. The polypeptide of the present invention can improve the proliferation of pancreatic islet cells and the ability to secrete insulin, effectively reduce the blood sugar level of diabetic rats, and improve the symptoms of diabetes.

Description

Technical Field

[0001] The invention belongs to the field of medical technology, and in particular relates to a mitigating agent for improving diabetes symptoms. Background Art

[0002] Diabetes is one of the most common endocrine and metabolic disorders, with a very high prevalence worldwide. The metabolic state of pancreatic islet cells is crucial to the glucose metabolism in diabetic patients, and the damage and destruction of pancreatic islet cells is one of the main pathogenesis of diabetes. Therefore, controlling and regulating the proliferation, insulin secretion and apoptosis of pancreatic islet cells has become one of the key strategies for the treatment of diabetes. This not only helps maintain normal blood sugar levels, but also effectively slows down the progression of the disease and reduces the occurrence of complications.

[0003] Currently, the treatment of diabetes mainly includes insulin injection, oral hypoglycemic drugs and lifestyle intervention. However, these treatments have some shortcomings, such as strong drug dependence, possible side effects with long-term use, and poor drug response in some patients. Therefore, it is urgent to develop new, safe and effective diabetes treatment drugs.

[0004] Marine biological resources are rich and diverse, with unique bioactive ingredients, including peptides, proteins, polysaccharides, lipids, etc., which have multiple biological activities such as antibacterial, antiviral, anti-inflammatory, antioxidant, and anti-tumor. Due to their unique structure and diverse biological activities, marine biological drugs have gradually attracted widespread attention from the scientific and medical communities, and have become an important source of new drug development in recent years.

[0005] Algae hook shrimp is a kind of crustacean widely distributed in freshwater and marine environments, belonging to the order Amphipoda. Algae hook shrimp is rich in various biochemical components, such as proteins, peptides, fatty acids, minerals and vitamins. Current research mainly focuses on its application as marine feed. These studies usually focus on the role of algae hook shrimp in aquaculture, such as as a high-quality feed for fish and other aquatic animals, providing rich nutrition to promote growth and enhance immunity. However, there are relatively few studies on the medicinal use of algae hook shrimp. In particular, in the field of diabetes treatment, no relevant research reports on algae hook shrimp have been seen. Summary of the invention

[0006] The present invention provides a mitigating agent for improving the symptoms of diabetes, thereby achieving safe and effective treatment of diabetes.

[0007] To achieve the above object, the present invention provides the following technical solutions:

[0008] Firstly, the present invention provides a mitigating agent for improving the symptoms of diabetes, wherein the mitigating agent is composed of a polypeptide extracted from the algae hook shrimp and a pharmaceutically acceptable carrier, wherein the polypeptide is an algae hook shrimp polypeptide of 200Da-500Da.

[0009] Preferably, the Gnaphalium polypeptide is extracted according to the following extraction method:

[0010] (1) Grind the dried algae shrimp into algae shrimp powder, mix with 10 times the mass of distilled water, and stir thoroughly until evenly dispersed;

[0011] (2) adjusting the pH value to 8, placing in a constant temperature water bath at 37°C, adding pancreatic enzyme at a concentration of 2% by weight of the algae hook shrimp powder, and performing a primary enzymatic hydrolysis at 37°C for 3 hours;

[0012] (3) adjusting the pH value to 7, raising the temperature to 55°C, adding 2% papain by weight of the algae hook shrimp powder, and performing secondary enzymolysis at 55°C for 5 hours;

[0013] (4) heating the solution after the secondary enzymatic hydrolysis to 95° C., maintaining it for 20 minutes to inactivate the enzyme, and centrifuging the supernatant to obtain the enzymatic hydrolyzate of the algae hook shrimp;

[0014] (5) Pre-treating the enzymatic hydrolysate of the algae hook shrimp using a 0.45 μm filter membrane;

[0015] (6) fractionating the pretreated algae hook shrimp enzymatic hydrolysate using a nanofiltration membrane with a cutoff range of 500Da and 200Da to obtain an algae hook shrimp polypeptide solution of 200Da-500Da;

[0016] (7) The 200Da-500Da algae hook shrimp polypeptide solution is vacuum freeze-dried to obtain the 200Da-500Da algae hook shrimp polypeptide.

[0017] Preferably, the pharmaceutically acceptable carrier is physiological saline.

[0018] Preferably, the concentration of the Gnatia sphaeroides polypeptide is 5-50 μg / mL.

[0019] Preferably, the concentration of the Gnatia spp polypeptide is 25 μg / mL.

[0020] Preferably, the diabetes is type 1 diabetes.

[0021] In addition, the present invention provides an application of a polypeptide in the preparation of a drug for treating diabetes, wherein the polypeptide is a 200Da-500Da Gammaridae polypeptide.

[0022] Preferably, the Gnatia sphaeroides polypeptide is extracted by the extraction method described in claim 2.

[0023] Preferably, the Gnaphalium polypeptide achieves the effect of treating diabetes by improving the proliferation ability and insulin secretion ability of pancreatic islet cells.

[0024] In addition, the present invention provides an application of a polypeptide in the preparation of a drug for improving the proliferation ability of pancreatic islet cells, wherein the polypeptide is a 200Da-500Da Gammaridae polypeptide, and the Gammaridae polypeptide is extracted by the extraction method described in claim 2.

[0025] Preferably, the polypeptide is a 200Da-500Da Gammaridae polypeptide, and the Gammaridae polypeptide is extracted by the extraction method described in claim 2.

[0026] In addition, the present invention provides an application of a polypeptide in the preparation of a drug for treating elevated blood sugar caused by streptozotocin, characterized in that the polypeptide is a 200Da-500Da algae hook shrimp polypeptide, and the algae hook shrimp polypeptide is extracted by the extraction method described in claim 2.

[0027] The beneficial effects of the present invention are:

[0028] The present invention provides a polypeptide extracted from the algae hook shrimp, which is used to improve the symptoms of diabetes and has the following beneficial effects:

[0029] 1. The present invention verifies through experiments that the extracted polypeptide C of the present invention can significantly reduce the blood sugar level of diabetic rats, thereby effectively improving the symptoms of diabetes.

[0030] 2. Algae hook shrimp polypeptide C can significantly promote the proliferation of pancreatic islet cells, increase the number and function of pancreatic islet cells, and help maintain normal blood sugar levels. This is of great significance for the treatment of diabetes and the repair of pancreatic islet cells.

[0031] 3. The polypeptide C of the present invention can significantly increase the insulin secretion of pancreatic islet cells, thereby further controlling blood sugar levels.

[0032] 4. The polypeptide C extracted from the marine organism Gammarus gammarus of the present invention is natural, safe, and has no obvious side effects. Compared with traditional chemical drug treatments, it has higher biocompatibility and safety. BRIEF DESCRIPTION OF THE DRAWINGS

[0033] Figure 1 The effects of different Gnaphalium peptides (polypeptide A, polypeptide B, polypeptide C and polypeptide D) on pancreatic islet cell proliferation are demonstrated.

[0034] Figure 2 The effects of different concentrations of Gnaphalium polypeptide C on pancreatic islet cell proliferation are shown.

[0035] Figure 3The effects of different Gammaridae polypeptides (polypeptide A, polypeptide B, polypeptide C and polypeptide D) on insulin secretion in pancreatic islet cells are shown.

[0036] Figure 4 This study demonstrates the effect of Ganoderma lucidum polypeptide C on blood glucose in diabetic rats. DETAILED DESCRIPTION

[0037] The present invention is further described below by means of specific implementation methods. The following examples are specific implementation methods of the present invention, but the implementation methods of the present invention are not limited to the following examples.

[0038] Example 1: Obtaining Gammaridae polypeptides

[0039] 1. Crushing and dissolving:

[0040] Grind the dried robust algae gammarus into a fine powder, ensuring the powder is fine and uniform.

[0041] The algae gammarus powder was mixed with 10 times the mass of distilled water, and stirred thoroughly until uniformly dispersed to obtain an algae gammarus solution.

[0042] 2. pH adjustment and temperature control:

[0043] The pH value of the algal gammarus solution was adjusted to 8 using NaOH solution and HCl solution.

[0044] The solution was placed in a thermostatic water bath and the temperature was controlled at 37°C.

[0045] 3. One-time pancreatic enzymatic hydrolysis:

[0046] Add 2% pancreatic enzyme of the mass of the algae hook shrimp powder, and carry out the enzymatic hydrolysis process for 3 hours, stirring every 30 minutes.

[0047] 4. Secondary enzymatic hydrolysis:

[0048] The pH value of the solution after enzymatic hydrolysis was adjusted to 7 using HCl solution and NaOH.

[0049] The solution temperature was raised to 55°C and continued to be heated in a constant temperature water bath.

[0050] Papain at 2% by weight of the algae hook shrimp powder was added and the enzymatic hydrolysis process was carried out for 5 hours, during which the mixture was stirred every 30 minutes.

[0051] 5. Enzyme inactivation and centrifugation:

[0052] Enzyme inactivation: Heat the enzymatic solution to 95°C and keep it for 20 minutes to inactivate the enzyme.

[0053] Centrifugal separation: Place the enzymatic hydrolysate in a centrifuge tube and centrifuge at 4500r / min for 15 minutes.

[0054] After centrifugation, carefully remove the supernatant, retain the supernatant as the algae hook shrimp enzymatic hydrolysate, and discard the precipitate.

[0055] 6. Nanofiltration membrane initial separation:

[0056] The enzymatic hydrolysate of the algae hook shrimp was pre-treated by filtering with a 0.45 micron filter membrane to remove large particles and impurities.

[0057] Ultrasonic degassing was performed to remove bubbles in the solution to avoid affecting the nanofiltration process.

[0058] A nanofiltration membrane with a molecular weight cutoff range of 1000 Da was selected, and the pretreated algae hook shrimp enzymatic hydrolysate was initially separated through the nanofiltration membrane system to collect the permeate (containing polypeptides less than 1000 Da) and the concentrate (containing polypeptides greater than 1000 Da).

[0059] The concentrate with a mass greater than 1000 Da was collected separately and labeled as polypeptide solution A.

[0060] 7. Further classification of peptides of different molecular sizes:

[0061] 500-1000 Da peptide separation:

[0062] The initially separated permeate was filtered again using a nanofiltration membrane with a molecular weight cutoff range of 500 Da, and the concentrate (containing polypeptides of 500-1000 Da) and the permeate were collected.

[0063] The 500-1000 Da concentrate was collected separately and labeled as peptide solution B.

[0064] 200-500 Da peptide separation:

[0065] The permeate from the previous step was filtered again using a nanofiltration membrane with a molecular weight cutoff range of 200 Da.

[0066] The concentrate (containing peptides of 200-500 Da) and the permeate were collected.

[0067] The 200-500 Da concentrate was collected separately and labeled as peptide solution C.

[0068] Separation of peptides smaller than 200 Da:

[0069] The permeate is a peptide solution with a size less than 200 Da, which is collected separately and labeled as peptide solution D.

[0070] 8. Vacuum freeze drying:

[0071] Freeze drying:

[0072] Peptide solutions A, B, C and D with different molecular weight ranges were placed in freeze-drying bottles respectively.

[0073] A vacuum freeze dryer was used with the freezing temperature set to -50°C and the vacuum degree maintained below 0.1 mbar for 48 hours of freeze drying until the sample was completely dry to obtain polypeptide A, polypeptide B, polypeptide C and polypeptide D.

[0074] Example 2: Detection of the effects of polypeptide A, polypeptide B, polypeptide C and polypeptide D on pancreatic islet cell proliferation

[0075] (1) INS-1 cells were cultured in RPMI-1640 complete medium (containing 10% fetal bovine serum, 1% penicillin and streptomycin, 50 μmol / L β-mercaptoethanol, 1 mmol / L pyruvate, and 10 mmol / L HEPES) at 37°C in a 5% CO2 incubator until the logarithmic growth phase;

[0076] (2) INS-1 cells in the logarithmic growth phase were digested and centrifuged and inoculated into a 96-well plate, with approximately 5 × 10 cells per well. 3 The peripheral wells of the 96-well plate were not inoculated with cells, and PBS solution was added to them to prevent edge effect;

[0077] (3) After the cells are completely attached, add serum-free RPMI-1640 medium and perform synchronization treatment for 24 hours;

[0078] (4) After synchronization, peptide treatment was performed. The control group was added with RPMI-1640 complete medium, and the drug intervention groups A, B, C, and D were added with RPMI-1640 complete medium containing 5 μg / mL peptide A, peptide B, peptide C, and peptide D, respectively. Three replicate wells were set for each group, and a zeroing well was also set.

[0079] (5) After 48 h of treatment, the culture medium was removed, the cells were washed twice with PBS, and 90 µL of serum-free culture medium and 10 µL of CCK-8 solution were added and incubated for 3 h.

[0080] (6) After incubation, use an ELISA reader to measure the absorbance of each well at 450 nm.

[0081] The results obtained in Example 2 are shown in Table 1 and Figure 1 As shown:

[0082] Table 1 Effects of polypeptide A, polypeptide B, polypeptide C and polypeptide D on pancreatic islet cell proliferation

[0083]

[0084] According to Table 1 and Figure 1The data showed that compared with the control group, the OD 450 Compared with the OD value (0.6506±0.0382) of the drug intervention group C 450 The OD value (0.8629±0.0399) was significantly increased, and the difference met the statistical requirement (P=0.0184). However, the OD values ​​of the other drug intervention groups A (0.6517±0.0388), B (0.6557±0.0361) and D (0.665±0.0381) were significantly higher than those of the control groups A (0.6517±0.0388), B (0.6557±0.0361) and D (0.665±0.0381). 450 The values ​​were not significantly different from those of the control group. This indicates that among the four Gammaridae polypeptides prepared by the present invention, only polypeptide C has a significant effect of promoting the proliferation of pancreatic islet cells.

[0085] This finding suggests that polypeptide C has potential biological activity and can be used as an effective ingredient to promote pancreatic cell proliferation.

[0086] Example 3: In Example 2, the present invention found that polypeptide C can promote the proliferation of pancreatic islet cells. In order to determine the optimal concentration of polypeptide C, in this example, the present invention tested different concentrations of polypeptide C to determine its optimal concentration.

[0087] (1) INS-1 cells were cultured in RPMI-1640 complete medium in a 37°C, 5% CO2 incubator until the logarithmic growth phase;

[0088] (2) INS-1 cells in the logarithmic growth phase were digested and centrifuged and inoculated into a 96-well plate, with approximately 5 × 10 cells per well. 3 The peripheral wells of the 96-well plate were not inoculated with cells, and PBS solution was added to them at the same time to prevent edge effect;

[0089] (3) After the cells are completely attached, add serum-free RPMI-1640 medium and perform synchronization treatment for 24 hours;

[0090] (4) After the synchronization treatment technique, peptide treatment was performed. The control group was added with RPMI-1640 complete medium, and the drug intervention groups C-1, C-2, C-3 and C-4 were added with RPMI-1640 complete medium containing 1 μg / mL peptide C, 5 μg / mL peptide C, 25 μg / mL peptide C and 50 μg / mL peptide C, respectively. Three replicate wells were set for each group, and a zeroing well was also set;

[0091] (5) After 48 h of treatment, the culture medium was removed, the cells were washed twice with PBS, and 90 µL of serum-free culture medium and 10 µL of CCK-8 solution were added and incubated for 3 h.

[0092] (6) After incubation, use an ELISA reader to measure the absorbance of each well at 450 nm.

[0093] The results obtained in Example 3 are shown in Table 2 and Figure 2 shown.

[0094] Table 2 Effects of different concentrations of polypeptide C on pancreatic islet cell proliferation

[0095]

[0096] From Table 2 and Figure 2 It can be seen that polypeptide C significantly promotes the proliferation of pancreatic islet cells within a certain concentration range. 450 The values ​​were higher than those of the control group, indicating that polypeptide C has significant biological activity;

[0097] Specific analysis shows that compared with the control group, the OD of the 1μg / mL peptide C group 450 The value was slightly increased, indicating that 1 μg / mL polypeptide C had a slight promoting effect on pancreatic islet cell proliferation, but the difference was not significant.

[0098] 5μg / mL polypeptide C significantly increased the proliferation rate of pancreatic islet cells, OD 450 The value was significantly higher than that of the control group, indicating that this concentration of polypeptide C has a strong promoting effect on pancreatic islet cell proliferation.

[0099] 25μg / mL polypeptide C can make the proliferation of pancreatic islet cells reach the maximum value, OD 450 The value was the highest, significantly higher than the control group and other drug intervention groups. This shows that 25μg / mL is the most effective concentration, which significantly promotes pancreatic islet cell proliferation.

[0100] OD of 50μg / mL peptide C 450 The value was slightly lower than that of the C-3 group, but still significantly higher than that of the control group. This indicates that although high concentrations of polypeptide C (50 μg / mL) can still promote pancreatic cell proliferation, its effect is slightly lower than that of 25 μg / mL, which may be due to saturation effects, negative feedback, and other reasons.

[0101] Therefore, the present invention determines that 25 μg / mL is the optimal concentration of polypeptide C.

[0102] Example 4: Insulin secretion is also the key to treating diabetes, so in this example, the present invention tests the effects of different polypeptides on insulin secretion. Since 25 μg / mL was determined to be the optimal concentration of polypeptide C in Example 3, the polypeptide concentration was selected to be 25 μg / mL in this example.

[0103] (1) INS-1 cells were cultured in RPMI-1640 complete medium in a 37°C, 5% CO2 incubator until the logarithmic growth phase.

[0104] (2) Digest and centrifuge INS-1 cells in the logarithmic growth phase and adjust the cell concentration to 10 6 / ml, and 500ul was inoculated into each well of a 24-well plate.

[0105] (3) After the cells were completely attached to the wall, peptide treatment was performed. The control group was added with RPMI-1640 complete medium, and the drug intervention groups A, B, C and D were added with RPMI-1640 complete medium containing 5 μg / mL peptide A, peptide B, peptide C and peptide D, respectively. Three replicate wells were set up for each group.

[0106] (4) After 24 h of treatment, discard the supernatant, gently wash the cells three times with preheated PBS, add preheated KRBH buffer containing 3.3 mM glucose, and equilibrate for 1 h.

[0107] (5) Add KRBH buffer containing 16.7 mM glucose and incubate at 37°C for 2 hours to stimulate pancreatic islet cells to secrete insulin.

[0108] (6) After the culture is completed, the supernatant was collected and centrifuged at 1000 rpm for 5 minutes at 4°C. The supernatant was then tested for insulin using radioimmunoassay (RIA).

[0109] The results are shown in Table 3 and Figure 3 As shown:

[0110] Table 3 Effects of polypeptide A, polypeptide B, polypeptide C and polypeptide D on insulin secretion

[0111]

[0112] From Table 3 and Figure 3 The results show that there are significant differences in the effects of different peptide treatments on insulin secretion. The specific analysis is as follows:

[0113] Drug intervention group A:

[0114] The insulin secretion was 0.87±0.037 mU / L, which had no significant difference compared with the control group, indicating that polypeptide A had no significant effect on insulin secretion.

[0115] Drug intervention group B:

[0116] The insulin secretion was 0.90±0.038 mU / L, slightly higher than that of the control group but the difference was not significant, indicating that polypeptide B had no significant effect on insulin secretion.

[0117] Drug intervention group C:

[0118] The insulin secretion was 1.23±0.032 mU / L, which was significantly higher than that of the control group (P<0.05), indicating that polypeptide C can significantly promote insulin secretion (P=0.0014). Compared with the control group, the insulin secretion increased by about 42.9%, showing the significant effect of polypeptide C.

[0119] Drug intervention group D:

[0120] The insulin secretion was 0.89±0.033 mU / L, slightly higher than that of the control group but the difference was not significant, indicating that the promoting effect of polypeptide D on insulin secretion was limited.

[0121] In summary, compared with the control group, only polypeptide C significantly promoted insulin secretion in pancreatic islet cells, while other polypeptides (A, B, D) had no significant effect on insulin secretion. This result shows that polypeptide C has obvious biological activity in promoting insulin secretion.

[0122] Example 5: Detection of the effect of polypeptide C on blood glucose in diabetic rats using an animal model

[0123] (1) Twenty-four male SPF SD rats weighing 250-270 g were cultured for one week.

[0124] (2) Dissolve STZ (streptozotocin) in 0.1% citric acid buffer (pH 4.5) to prepare a 5 mg / ml solution. Dissolve polypeptide C in physiological saline to prepare a 25 μg / mL solution and set aside.

[0125] (3) The rats were randomly divided into three groups: control group, model group and treatment group. The rats in the model group and treatment group were intraperitoneally injected with 2.5 mL of STZ solution.

[0126] (4) Blood glucose monitoring began 72 hours after injection. Modeling was considered successful when fasting blood glucose was ≥11.1 mmol / L.

[0127] (5) After successful modeling, the treatment group was gavaged with 2.5 mL of polypeptide C solution, and the control group and model group were gavaged with 2.5 mL of normal saline. After 7 consecutive days of treatment, the fasting blood glucose levels of the different treatment groups were monitored.

[0128] The results are shown in Table 4 and Figure 4 shown.

[0129] Table 4 Effects of polypeptide C on blood glucose in diabetic rats

[0130]

[0131] From Table 4 and Figure 4The results showed that compared with the control group, the fasting blood glucose concentration of the STZ-induced diabetic rat model group increased significantly, from 3.62±0.08 mmol / L to 17.43±0.16 mmol / L. This result showed that the diabetic rat model was successfully established by STZ induction, which was consistent with the characteristics of diabetic hyperglycemia and verified the success of the model construction.

[0132] Compared with the model group, the fasting blood glucose concentration of the polypeptide C treatment group decreased significantly from 17.43±0.16 mmol / L to 7.76±0.15 mmol / L. This result shows that polypeptide C has a significant hypoglycemic effect and can effectively reduce the blood glucose level of diabetic rats. Therefore, the polypeptide C prepared by the present invention can be used for the treatment of diabetes.

Claims

1. A mitigating agent for improving symptoms of type I diabetes, characterized in that: The mitigating agent is composed of a polypeptide extracted from the algae hook shrimp and a pharmaceutically acceptable carrier, wherein the polypeptide is an algae hook shrimp polypeptide of 200Da-500Da; The algae hook shrimp polypeptide is extracted according to the following extraction method: (1) Grind the dried algae shrimp into algae shrimp powder, mix with 10 times the mass of distilled water, and stir thoroughly until evenly dispersed; (2) adjusting the pH value to 8, placing in a constant temperature water bath at 37°C, adding pancreatic enzyme at a concentration of 2% by weight of the algae hook shrimp powder, and performing a primary enzymatic hydrolysis at 37°C for 3 hours; (3) adjusting the pH value to 7, raising the temperature to 55°C, adding 2% papain by weight of the algae hook shrimp powder, and performing secondary enzymolysis at 55°C for 5 hours; (4) heating the solution after the secondary enzymatic hydrolysis to 95° C., maintaining it for 20 minutes to inactivate the enzyme, and centrifuging the supernatant to obtain the enzymatic hydrolyzate of the algae hook shrimp; (5) Pre-treating the enzymatic hydrolysate of the algae hook shrimp using a 0.45 μm filter membrane; (6) fractionating the pretreated algae hook shrimp enzymatic hydrolysate using a nanofiltration membrane with a cutoff range of 500Da and 200Da to obtain an algae hook shrimp polypeptide solution of 200Da-500Da; (7) vacuum freeze-drying the 200Da-500Da algae hook shrimp polypeptide solution to obtain 200Da-500Da algae hook shrimp polypeptide; The concentration of the algae hook shrimp polypeptide is 5-50 μg / mL; The algae hook shrimp is a strong algae hook shrimp.

2. A mitigating agent for improving symptoms of type I diabetes according to claim 1, characterized in that: The pharmaceutically acceptable carrier is physiological saline.

3. Use of a polypeptide in the preparation of a drug for treating type I diabetes, characterized in that: The polypeptide is a 200Da-500Da algae hook shrimp polypeptide; The algae hook shrimp polypeptide is extracted by the extraction method described in claim 1; The algae hook shrimp polypeptide achieves the effect of treating type I diabetes by improving the proliferation ability and insulin secretion ability of pancreatic islet cells; The algae hook shrimp is a strong algae hook shrimp.

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