CN110183517B - Blood sugar reducing undecapeptide - Google Patents
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Abstract
The invention discloses an undecapeptide. The undecapeptide amino acid sequence is shown below: Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys, abbreviated VVDLVFFAAAK, molecular weight 1179.44Da, purity 97.71%. The invention uses a polypeptide synthesizer and adopts a solid phase synthesis method for synthesis. The in vitro alpha-amylase and alpha-glucosidase inhibition activity test shows that the alpha-amylase inhibitor has a good inhibition effect on both enzymes, the 50% inhibition concentration (IC50) on the alpha-amylase is 1.44mg/mL (1.70 mu mol/L), and the 50% inhibition concentration (IC50) on the alpha-glucosidase is 0.0435mg/mL (0.0513 mu mol/L). The invention provides a synthetic polypeptide with potential in-vitro hypoglycemic activity, which can be applied to the field of biological pharmacy.
Description
Technical Field
The invention belongs to the field of biological pharmacy, and particularly relates to blood sugar reducing undecapeptide.
Background
Diabetes is a chronic disease, is a metabolic disorder of protein, fat and carbohydrate caused by insufficient insulin in vivo, and is mainly characterized by chronic hyperglycemia. Many natural antidiabetic active ingredients have been found, such as: ginkgo leaf extract, plant polysaccharide, etc. The hypoglycemic aspect of bioactive polypeptides is less studied. Several studies have shown that bioactive peptides are effective in ameliorating the effects of diabetes. For example, in the research of the Wangweibo and the like, the marine collagen peptide can relieve the structural damage of islet beta cells of a rat with hyperinsulinemia, increase the secretion of particles, reduce the formation of lipid droplets and obviously improve the biological activity of insulin; obviously reduces the fasting insulin level, and has certain improvement effect on fasting blood glucose and oral glucose tolerance. In the research of Huangfengjie and the like, shark liver active peptide S-8300 has the antioxidation effect, protects pancreatic beta cells by removing free radicals, regulates glycolipid metabolism, delays the failure of the pancreatic beta cells, and can treat diabetes to a certain extent.
The digestion and absorption of carbohydrates such as starch in human bodies need to depend on two key enzymes, namely alpha-glucosidase and alpha-amylase. Therefore, inhibiting the activities of the two key enzymes can slow down the degradation speed of carbohydrates into monosaccharides so as to achieve the purpose of regulating and controlling the excessive rise of blood sugar after meals.
Therefore, the invention provides a hypoglycemic undecapeptide, and the synthetic polypeptide has hypoglycemic capacity.
Disclosure of Invention
In order to overcome the defects of the prior art, the invention aims to provide the blood sugar-reducing undecapeptide and the application thereof.
The invention selects alpha-amylase and alpha-glucosidase as research objects to determine the in vitro inhibitory activity of synthetic peptide. The invention aims to provide a synthetic polypeptide with in-vitro hypoglycemic activity, which can be applied to the field of biological pharmacy.
The amino acid sequence of the undecapeptide is Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys, which is abbreviated as VVDLVFFAAAK.
Further, the undecapeptide VVDLVFFAAAK has inhibitory activity on alpha-amylase, and the 50% inhibitory concentration (IC50) value of the undecapeptide on the alpha-amylase is 1.44mg/mL (1.70 mu mol/L).
Further, the undecapeptide VVDLVFFAAAK has inhibitory activity on alpha-glucosidase, and the 50% inhibitory concentration (IC50) value on alpha-glucosidase is 0.0435mg/mL (0.0513. mu. mol/L).
Further, the undecapeptide VVDLVFFAAAK has a molecular weight of 1179.44Da and a purity of 97.71%.
The application of the blood sugar-reducing undecapeptide is provided.
The synthesized polypeptide is abbreviated as VVDLVFFAAAK, has the molecular weight of 1179.44Da, the purity of 97.71 percent and the sequence as follows: Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys. Wherein the content of the first and second substances,
val represents the corresponding residue of the amino acid with the english name Threonine and the chinese name Threonine;
val represents the corresponding residue of the amino acid with the english name Threonine and the chinese name Threonine;
asp represents the corresponding residue of an amino acid having the English name Aspartic acid and the Chinese name Aspartic acid;
leu represents the corresponding residue of the amino acid named Leucine in England and Leucine in Chinese;
val represents the corresponding residue of the amino acid with the english name Threonine and the chinese name Threonine;
phe represents the corresponding residue of an amino acid with the english name Phenylalanine and the chinese name Phenylalanine;
ala represents the corresponding residue of the amino acid with the English name Alanine and the Chinese name Alanine;
ala represents the corresponding residue of the amino acid with the English name Alanine and the Chinese name Alanine;
ala represents the corresponding residue of the amino acid with the English name Alanine and the Chinese name Alanine;
lys represents the corresponding residue of an amino acid with the English name Lysine and the Chinese name Lysine.
The amino acid sequence of the invention adopts a standard Fmoc scheme, and a reasonable polypeptide synthesis method is realized by screening resin. The C-terminal carboxyl group of the target polypeptide is covalently linked to an insoluble polymeric resin, and then the amino group of the amino acid is used as a starting point to react with the carboxyl group of another molecule of amino acid to form a peptide bond. The process is repeated continuously to obtain the target polypeptide product. And after the synthesis reaction is finished, removing the protecting group, and separating the peptide chain from the resin to obtain the target product. Polypeptide synthesis is a process of repeated addition of amino acids, and the solid phase synthesis sequence is synthesized from the C-terminus to the N-terminus.
The hypoglycemic effect of the synthetic peptide is evaluated by researching the inhibition effect of the synthetic peptide on alpha-amylase and alpha-glucosidase.
Compared with the prior art, the invention has the following advantages and technical effects:
the peptide is synthesized for the first time, the inhibitory activity of the synthesized polypeptide on alpha-amylase and alpha-glucosidase is detected, and the synthesized polypeptide has a certain blood sugar reducing capability.
Drawings
FIG. 1a is an HPLC picture of the synthetic polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys.
FIG. 1b is a MS picture of the synthetic polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys.
FIG. 2a is a line graph of the inhibitory activity of the synthetic polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys on alpha-amylase.
FIG. 2b is a line graph showing the inhibitory activity of the synthetic polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys on α -glucosidase.
Detailed Description
The present invention is further illustrated by the following specific examples, but the scope of the invention is not limited thereto.
Solid phase synthesis of polypeptides
Selecting high molecular resin (Zhongtai Biochemical Co., Ltd.), connecting the carboxyl of Val with a resin in a covalent bond form according to the characteristics of an amino acid sequence Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys, then carrying out a shrinkage reaction on the amino of Val and the carboxyl of another Val, adding Asp after treatment, carrying out a reaction on the amino of Asp and the carboxyl of Leu, sequentially adding amino acid from right to left, adding the last Lys amino acid, and then cutting off the resin to obtain the target polypeptide. Purifying by high performance liquid chromatography, with column model of Phenomenex C18 and size of 4.6 x 150mm, mobile phase A of acetonitrile containing 0.1% trifluoroacetic acid (TFA); mobile phase B, water containing 0.1% TFA; the B phase is reduced from 95.0% to 30.0% in 25min, the flow rate is 1.0mL/min, and the detection wavelength is 214 nm. Quick freezing with liquid nitrogen, freeze drying to obtain final product with purity of above 95%, and identifying structure by MS (shown in FIG. 1a and FIG. 1 b).
In vitro inhibitory Activity of synthetic Polypeptides on alpha-Amylase
1 preparation of reagent
1)0.2M phosphate buffer: weighing Na2HPO4 2.84g、KH2PO42.72g of the two solutions are respectively dissolved in 100mL of distilled water, an appropriate amount of the two solutions are mixed under the action of a magnetic stirrer until the pH value is 6.9, and the pH value is measured by a pH meter in real time during stirring.
2)1U/mL alpha-amylase solution.
3) 1% starch solution: 1g of soluble starch was dissolved in 99mL of buffer.
4) Sample solution: taking a certain mass of sample, and preparing sample solutions (0-10 mg/mL) with different dosages, wherein the solvent is water.
5) DNS termination reaction solution: 1g of DNS and 12g of potassium sodium tartrate are weighed into a conical flask, and 87mL of 0.4M Na is added2CO3And (3) solution.
6) Acarbose solution: for positive control, a certain amount of acarbose is weighed to prepare solutions (0-10 mg/mL) with different concentration gradients
2 Experimental procedures
1) 1% starch solution in water bath at 95 deg.C for 8min, and pre-treating to denature.
2) 20 mu L of inhibitor (0-10 mg/mL) and 10 mu L of alpha-amylase solution are sucked by a pipette gun and mixed in a test tube, 20 mu L of buffer solution of a control group and 10 mu L of alpha-amylase solution are mixed, 20 mu L of acarbose (0-10 mg/mL) and 10 mu L of alpha-amylase solution are mixed in a positive control group, and the mixture is subjected to shaking table reaction at 37 ℃ for 15 min.
3) Adding 500 μ L of the pretreated starch solution, and reacting in a shaker at 37 deg.C for 5 min.
4) Adding DNS solution 600. mu.L, and water bath at 100 deg.C for 15 min.
5) After the reaction, 200. mu.L of the reaction solution was aspirated by pipette gun, absorbance was measured at 540nm, and absorbance of the experimental group and the control group was measured by AExperimental groupAnd AControl groupAnd (4) showing.
6) Drawing an inhibition rate-concentration curve: the obtained data is subjected to nonlinear fitting by using originPro 9.1 software, a Logistic Function within the range of Origin Basic Function is selected, the confidence interval is selected to be 95%, and Find Y from X is adopted as output data. The IC50 value was determined by plotting the inhibition rate versus concentration.
The Logistic function formula is as follows:
a1 is the minimum value of y, a2 is the maximum value of y, P is 3, and X0 is the value of X at 50%.
In vitro inhibitory Activity of synthetic Polypeptides on alpha-glucosidase
1 preparation of reagent
1)0.2M phosphate buffer: weighing Na2HPO4 2.84g、KH2PO42.72g of the two solutions are respectively dissolved in 100mL of distilled water, an appropriate amount of the two solutions are mixed under the action of a magnetic stirrer until the pH value is 6.9, and the pH value is measured by a pH meter in real time during stirring.
2) P-NPG solution: the substrate solution, 0.03765g p-NPG, was weighed and dissolved in 25mL of distilled water.
3)0.2U/mL α glucosidase solution: 5. mu.L of the dispensed alpha-glucosidase solution (200U/mL) was aspirated and made up to 5mL with distilled water.
4) Sample solution: taking a certain mass of sample, and preparing sample solutions (0-10 mg/mL) with different concentrations, wherein the solvent is water.
5)0.2M Na2CO3: 0.848g of Na was weighed2CO3Dissolved in 40mL of distilled water.
2 Experimental procedures
1) The reaction was carried out in a 96-well plate, and the reagents were added to the experimental group, the background group, the control group, and the positive control group as shown in Table 1, followed by shaking reaction at 37 ℃ for 20 min.
TABLE 1 amount of sample added
2) Adding buffer solution 50 μ L and substrate solution 40 μ L into each well, shaking at 37 deg.C for 20min, removing, adding Na 140 μ L2CO3The solution stops the reaction.
3) Measuring absorbance at 405nm, and respectively using A as absorbance of experimental group and control groupExperimental groupAnd AControl groupAnd (4) showing. .
4) Drawing an inhibition rate-concentration curve: the obtained data is subjected to nonlinear fitting by using originPro 9.1 software, a Logistic Function within the range of Origin Basic Function is selected, the confidence interval is selected to be 95%, and Find Y from X is adopted as output data. The IC50 value was determined by plotting the inhibition rate versus concentration.
The Logistic function formula is as follows:
a1 is the minimum value of y, a2 is the maximum value of y, P is 3, and X0 is the value of X at 50%.
Application example 1
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. Taking 1% starch solution, and performing water bath at 95 deg.C for 8min, and pretreating to denature. 20 mu L of undecapeptide (10mg/mL) and 10 mu L of alpha-amylase solution are sucked by a pipette and mixed in a test tube, 20 mu L of buffer solution of a control group is mixed with 10 mu L of alpha-amylase solution, 20 mu L of acarbose (10mg/mL) and 10 mu L of alpha-amylase solution are mixed in a positive control group, and the mixture is subjected to shake reaction at 37 ℃ for 15 min. Adding 500 μ L of the above pretreated starch solution, and reacting at 37 deg.C for 5min by shaking table. Adding DNS solution 600. mu.L, and water bath at 100 deg.C for 15 min. After the reaction, 200. mu.L of the reaction solution was aspirated by a pipette gun, and the absorbance at 540nm was measured to calculate the inhibition rate. As shown in FIG. 2a, the inhibition rate of alpha-amylase by undecapeptide is 84.75%, which is slightly higher than the inhibition rate of acarbose (81.87%).
Application example 2
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. Taking 1% starch solution, and performing water bath at 95 deg.C for 8min, and pretreating to denature. 20 mu L of undecapeptide (4mg/mL) and 10 mu L of alpha-amylase solution are sucked by a pipette and mixed in a test tube, 20 mu L of buffer solution of a control group is mixed with 10 mu L of alpha-amylase solution, 20 mu L of acarbose (4mg/mL) and 10 mu L of alpha-amylase solution are mixed in a positive control group, and the mixture is subjected to shake reaction at 37 ℃ for 15 min. Adding 500 μ L of the pretreated starch solution, and reacting in a shaker at 37 deg.C for 5 min. Adding DNS solution 600. mu.L, and water bath at 100 deg.C for 15 min. After the reaction, 200. mu.L of the reaction solution was aspirated by a pipette gun, and the absorbance at 540nm was measured to calculate the inhibition rate. As shown in FIG. 2a, the alpha-amylase inhibition ratio of undecapeptide was 65.97%, and the acarbose inhibition ratio at the same concentration was 77.15%.
Application example 3
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. Taking 1% starch solution, and performing water bath at 95 deg.C for 8min, and pretreating to denature. 20 mu L of undecapeptide (1.5mg/mL) and 10 mu L of alpha-amylase solution are sucked by a pipette and mixed in a test tube, 20 mu L of buffer solution of a control group is mixed with 10 mu L of alpha-amylase solution, 20 mu L of acarbose (1.5mg/mL) and 10 mu L of alpha-amylase solution are mixed in a positive control group, and then the mixture is subjected to shaking table reaction at 37 ℃ for 15 min. Adding 500 μ L of the pretreated starch solution, and reacting in a shaker at 37 deg.C for 5 min. Adding DNS solution 600. mu.L, and water bath at 100 deg.C for 15 min. After the reaction, 200. mu.L of the reaction solution was aspirated by a pipette gun, and the absorbance at 540nm was measured to calculate the inhibition rate. As shown in FIG. 2a, the alpha-amylase inhibition ratio of undecapeptide is 51.12%, and the acarbose inhibition ratio of undecapeptide is 68.14% at the same concentration.
Application example 4
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. To a 96-well plate, an experimental group (20. mu.L of undecapeptide (4mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution), a background group (20. mu.L of undecapeptide (4mg/mL) and 10. mu.L of buffer), a control group (10. mu.L of buffer and 10. mu.L of alpha-glucosidase enzyme solution), and a positive control group (20. mu.L of acarbose solution (4mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution) were added, and the mixture was subjected to shake reaction at 37 ℃ for 20 min. Adding buffer solution 50 μ L and substrate solution 40 μ L into each well, shaking at 37 deg.C for 20min, removing, adding Na 140 μ L2CO3The solution stops the reaction. Absorbance was measured at 405nm and inhibition was calculated. As shown in FIG. 2b, the inhibition rate of α -glucosidase by undecapeptide was 98.26%, which is close to the acarbose inhibition rate (99.5%).
Application example 5
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. To a 96-well plate, an experimental group (20. mu.L of undecapeptide (1mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution), a background group (20. mu.L of undecapeptide (1mg/mL) and 10. mu.L of buffer), a control group (10. mu.L of buffer and 10. mu.L of alpha-glucosidase enzyme solution), and a positive control group (20. mu.L of acarbose solution (1mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution) were added, and the mixture was subjected to shake reaction at 37 ℃ for 20 min. Adding buffer solution 50 μ L and substrate solution 40 μ L into each well, shaking at 37 deg.C for 20min, removing, adding Na 140 μ L2CO3The solution stops the reaction. Absorbance was measured at 405nm and inhibition was calculated. As is clear from FIG. 2b, the inhibition ratio of the undecapeptide to the alpha-glucosidase was 95.16%, which is 2.4 times the inhibition ratio of acarbose (40.22%).
Application example 6
As can be seen from the percentage peak areas shown in FIG. 1a, the purity of the undecapeptide is 97.71%, which meets the purity requirements of the synthetic peptide. To a 96-well plate, an experimental group (20. mu.L of undecapeptide (0.5mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution), a background group (20. mu.L of undecapeptide (0.5mg/mL) and 10. mu.L of buffer solution), a control group (10. mu.L of buffer solution and 10. mu.L of alpha-glucosidase enzyme solution), and a positive control group (20. mu.L of acarbose solution (0.5mg/mL) and 10. mu.L of alpha-glucosidase enzyme solution) were added, and the mixture was subjected to shake reaction at 37 ℃ for 20 min. Adding buffer solution 50 μ L and substrate solution 40 μ L into each well, shaking at 37 deg.C for 20min, removing, adding Na 140 μ L2CO3The solution stops the reaction. Absorbance was measured at 405nm and inhibition was calculated. As is clear from FIG. 2b, the inhibition ratio of α -glucosidase by undecapeptide was 94.26%, which is 4.7 times the inhibition ratio of acarbose (20.19%).
The above examples are only preferred embodiments of the present invention, which are intended to be illustrative and not limiting, and those skilled in the art should understand that they can make various changes, substitutions and alterations without departing from the spirit and scope of the invention.
Sequence listing
<110> university of southern China's science
<120> hypoglycemic undecapeptide
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 11
<212> PRT
<213> Artificial sequence (Artificial Synthesis)
<400> 1
Val Val Asp Leu Val Phe Phe Ala Ala Ala Lys
1 5 10
Claims (4)
1. An undecapeptide for lowering blood sugar, characterized in that the amino acid sequence of the undecapeptide is Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys, abbreviated as VVDLVFFAAAK.
2. The use of a hypoglycemic undecapeptide in the preparation of a biopharmaceutical having hypoglycemic activity in vitro of claim 1, wherein said undecapeptide VVDLVFFAAAK has inhibitory activity on α -amylase and an IC50 value of 1.44 mg/mL.
3. The use of a hypoglycemic undecapeptide in the preparation of a biopharmaceutical for its in vitro hypoglycemic activity of claim 1, wherein said undecapeptide VVDLVFFAAAK has inhibitory activity on α -glucosidase with an IC50 value of 0.0435 mg/mL.
4. Use of a hypoglycemic undecapeptide in the preparation of biopharmaceuticals having hypoglycemic activity in vitro according to claim 1, wherein said undecapeptide VVDLVFFAAAK has a molecular weight of 1179.44Da and a purity of 97.71%.
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| WO2006126695A1 (en) * | 2005-05-23 | 2006-11-30 | Japan Tobacco Inc. | Pyrazole compound and therapeutic agent for diabetes comprising the same |
| CN104497105A (en) * | 2014-11-20 | 2015-04-08 | 渤海大学 | Pentapeptide KLPGF with auxiliary hyperglycemic function |
| CN105237624A (en) * | 2015-09-28 | 2016-01-13 | 华南理工大学 | Heptapeptide EMLQPPL and applications thereof |
| CN106699846A (en) * | 2016-12-05 | 2017-05-24 | 华南理工大学 | Anti-obesity undecapeptide NALKCCHSCPA |
| CN109021079A (en) * | 2018-08-31 | 2018-12-18 | 华南理工大学 | A kind of hypoglycemic ten hexapeptide |
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2019
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|---|---|---|---|---|
| WO2006126695A1 (en) * | 2005-05-23 | 2006-11-30 | Japan Tobacco Inc. | Pyrazole compound and therapeutic agent for diabetes comprising the same |
| CN104497105A (en) * | 2014-11-20 | 2015-04-08 | 渤海大学 | Pentapeptide KLPGF with auxiliary hyperglycemic function |
| CN105237624A (en) * | 2015-09-28 | 2016-01-13 | 华南理工大学 | Heptapeptide EMLQPPL and applications thereof |
| CN106699846A (en) * | 2016-12-05 | 2017-05-24 | 华南理工大学 | Anti-obesity undecapeptide NALKCCHSCPA |
| CN109021079A (en) * | 2018-08-31 | 2018-12-18 | 华南理工大学 | A kind of hypoglycemic ten hexapeptide |
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