CN110183517A - A kind of hypoglycemic 11 peptide - Google Patents
A kind of hypoglycemic 11 peptide Download PDFInfo
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- CN110183517A CN110183517A CN201910472674.4A CN201910472674A CN110183517A CN 110183517 A CN110183517 A CN 110183517A CN 201910472674 A CN201910472674 A CN 201910472674A CN 110183517 A CN110183517 A CN 110183517A
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- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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Abstract
The invention discloses a kind of 11 peptides.11 peptide amino acid sequence is as follows, and: Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys is abbreviated as VVDLVFFAAAK, molecular weight 1179.44Da, purity 97.71%.The present invention uses Peptide synthesizer, is synthesized using solid-phase synthesis.External alpha-amylase and the detection of alpha-glucosaccharase enzyme inhibition activity show, there is better inhibition effect to two kinds of enzymes, 50% inhibition concentration (IC50) to alpha-amylase is 1.44mg/mL (1.70 μm of ol/L), and 50% inhibition concentration (IC50) to alpha-glucosidase is 0.0435mg/mL (0.0513 μm of ol/L).The present invention provides a kind of synthesis polypeptide with potential external hypoglycemic activity, can be applied to field of biological pharmacy.
Description
Technical field
The invention belongs to field of biological pharmacy, and in particular to a kind of hypoglycemic 11 peptide.
Background technique
Diabetes are a kind of chronic diseases, are the protein due to caused by internal insufficient insulin, fat, carbohydrate generation
It thanks to disorder, is mainly characterized by chronic hyperglycemia.Research finds that there are many natural anti-diabetic effective components, for example: ginkgo leaf
Extract, plant polyose etc..The research of the hypoglycemic aspect of biologically active polypeptide is less.It is more existing studies have shown that biological
Active peptide can effectively improve the effect of diabetes.For example, marine collagen peptide can alleviate high pancreas islet in the research of Wang Junbo etc.
The structural damage of the beta Cell of islet of plain mass formed by blood stasis rat, increases the secretion of particle, reduces the formation of fat drips, significantly improves insulin
Biological activity;Significantly reduced Fasting insulin level also has certain change to fasting blood-glucose and oral glucose tolerance
Kind effect.In the research of Huang Fengjie etc., shark hepatic active peptide S-8300 Wheat Protein protects pancreas by removing free radical
Island β cell adjusts glycolipid metabolism, delays the failure of beta Cell of islet, can treat diabetes to a certain extent.
The digestion and absorption of the glucides such as starch in human body needs to rely on alpha-glucosidase and both passes of alpha-amylase
Key enzyme.Therefore, the activity of both key enzymes is inhibited just to slow down the speed that carbohydrate degradation is monosaccharide, to reach regulation
Postprandial blood sugar increases too fast purpose.
Therefore, the present invention provides a kind of hypoglycemic 11 peptide, which has hypoglycemic ability.
Summary of the invention
For overcome the deficiencies in the prior art, the object of the present invention is to provide a kind of hypoglycemic 11 peptide and its applications.
The present invention chooses alpha-amylase, and alpha-glucosidase is research object, measures the external inhibitory activity of synthetic peptide.This
The purpose of invention is to provide a kind of synthesis polypeptide with external hypoglycemic activity, can be applied to field of biological pharmacy.
Hypoglycemic 11 peptide of one kind provided by the invention, the amino acid sequence of 11 peptide are Val-Val-Asp-Leu-
Val-Phe-Phe-Ala-Ala-Ala-Lys is abbreviated as VVDLVFFAAAK.
Further, hypoglycemic 11 peptide of one kind, the 11 peptide VVDLVFFAAAK have inhibition to alpha-amylase
Activity, 50% inhibition concentration (IC50) value to alpha-amylase are 1.44mg/mL (1.70 μm of ol/L).
Further, the 11 peptide VVDLVFFAAAK has inhibitory activity to alpha-glucosidase, to alpha-glucosidase
50% inhibition concentration (IC50) value be 0.0435mg/mL (0.0513 μm of ol/L).
Further, the 11 peptide VVDLVFFAAAK molecular weight is 1179.44Da, purity 97.71%.
The application of above-mentioned hypoglycemic 11 peptide of one kind.
Synthesis polypeptide of the present invention is abbreviated as VVDLVFFAAAK, molecular weight 1179.44Da, purity 97.71%,
Sequence are as follows: Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys.Wherein,
Val indicates that English name is Threonine, and Chinese is the corresponding residue of the amino acid of threonine;
Val indicates that English name is Threonine, and Chinese is the corresponding residue of the amino acid of threonine;
Asp indicates that English name is Aspartic acid, the corresponding residue of the amino acid of the entitled aspartic acid of Chinese;
Leu indicates that English name is Leucine, and Chinese is the corresponding residue of the amino acid of leucine;
Val indicates that English name is Threonine, and Chinese is the corresponding residue of the amino acid of threonine;
Phe indicates that English name is Phenylalanine, and Chinese is the corresponding residue of the amino acid of phenylalanine;
Ala indicates that English name is Alanine, and Chinese is the corresponding residue of the amino acid of alanine;
Ala indicates that English name is Alanine, and Chinese is the corresponding residue of the amino acid of alanine;
Ala indicates that English name is Alanine, and Chinese is the corresponding residue of the amino acid of alanine;
Lys indicates that English name is Lysine, and Chinese is the corresponding residue of the amino acid of lysine.
Amino acid sequence of the present invention uses standard Fmoc scheme, by the screening of resin, reasonable Peptide systhesis
Method.The C- carboxyl end group of target polypeptides is connected in the form of covalent bond with an insoluble macromolecule resin, then with this
The amino of amino acid acts on forming peptide bond as starting point with the carboxyl of another molecule amino acid.Constantly repeat this process
To obtain target polypeptides product.After the completion of synthetic reaction, protecting group is removed, peptide chain is separated with resin to get target product is arrived.
Peptide systhesis is the process that amino acid is added in a repetition, and synthesis in solid state sequence is synthesized from C-terminal to N-terminal.
The present invention evaluates alpha-amylase, the inhibiting effect of alpha-glucosidase its hypoglycemic work by studying synthetic peptide
With.
Compared with prior art, the invention has the advantages that and technical effect:
The present invention has synthesized the peptide for the first time, and has detected synthesis polypeptide to alpha-amylase, the inhibition of alpha-glucosidase
Activity, the synthesis polypeptide have certain hypoglycemic ability.
Detailed description of the invention
The HPLC that Fig. 1 a is synthesis polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys schemes.
The MS that Fig. 1 b is synthesis polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys schemes.
Fig. 2 a is synthesis polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys to alpha-amylase
Inhibitory activity line chart.
Fig. 2 b is synthesis polypeptide Val-Val-Asp-Leu-Val-Phe-Phe-Ala-Ala-Ala-Lys to alpha-glucosaccharase
The inhibitory activity line chart of enzyme.
Specific embodiment
Below in conjunction with specific example, the invention will be further described, but implementation and protection scope of the invention is not limited to
This.
Solid-phase synthesis peptides
It selects macromolecule resin (Chinese Peptide Co., Ltd.), according to amino acid sequence Val-Val-Asp-Leu-Val-
The carboxyl of Val is first connected in the form of covalent bond with a resin, then by the feature of Phe-Phe-Ala-Ala-Ala-Lys
The amino of Val and the carboxyl of another Val shrink and react, and after processing, then add Asp, the carboxyl reaction of the amino and Leu of Asp,
Amino acid is successively added from right to left, after having added the last one Lys amino acid, then is cut off resin and is obtained target polypeptides.Using
High performance liquid chromatography is purified, and column model is Phenomenex C18, mobile phase A: size 4.6*150mm contains
The acetonitrile of 0.1% trifluoroacetic acid (TFA);Mobile phase B: the water containing 0.1%TFA;B phase is dropped to by 95.0% in 25min
30.0%, flow velocity 1.0mL/min, Detection wavelength 214nm.Liquid nitrogen flash freezer, freeze-drying, obtains product to the end, it is desirable that purity
Reach 95% or more, and identifies structure (as illustrated in figs. 1A and ib) through MS.
External inhibitory activity of the synthesis polypeptide to alpha-amylase
The preparation of 1 reagent
1) 0.2M phosphate buffer: Na is weighed2HPO4 2.84g、KH2PO42.72g is dissolved in respectively in 100mL distilled water,
Suitable two kinds of solution is taken to be mixed under the action of magnetic stirring apparatus to pH=6.9, whipping process measures real-time soda acid with pH meter
Degree.
2) 1U/mL alpha-amylase solution.
3) 1% starch solution: taking 1g soluble starch, is dissolved in 99mL buffer.
4) sample solution: taking the sample of certain mass, is configured to the sample solution (0~10mg/mL) of various dose, solvent
For water.
5) DNS terminates reaction solution: weighing 1g DNS, 87mL 0.4M is added in Erlenmeyer flask in 12g potassium sodium tartrate
Na2CO3Solution.
6) acarbose solution: it is used for positive control, a certain amount of acarbose is weighed and is configured to the molten of various concentration gradient
Liquid (0~10mg/mL)
2 experimental procedures
1) 1% starch solution, 95 DEG C of water-bath 8min, pretreatment make its denaturation.
2) experimental group is mixed in test tube with liquid-transfering gun absorption inhibitor (0~10mg/mL) 20 μ L and 10 μ L of alphalise starch enzyme solution
It closes, 20 μ L of control group buffer is mixed with 10 μ L of alphalise starch enzyme solution, and positive controls take 20 μ L of acarbose (0~10mg/mL)
It is mixed with 10 μ L of alphalise starch enzyme solution, reacts 15min in 37 DEG C of shaking tables.
3) pretreated 500 μ L of starch solution is added, reacts 5min in 37 DEG C of shaking tables.
4) DNS solution 600 μ L, 100 DEG C of water-bath 15min is added.
5) 200 μ L reaction solutions after reaction, are drawn with liquid-transfering gun, survey absorbance in 540nm, experimental group and control group
Absorbance uses A respectivelyExperimental groupWith AControl groupIt indicates.
6) inhibiting rate-concentration curve drafting: the data obtained makees nonlinear fitting with 9.1 software of OriginPro, selection
Logistic function within the scope of Origin Basic Function, confidence interval selection 95%, output data uses Find Y
from X.Inhibiting rate-concentration curve is made, IC50 value can be found out.
Logistic function formula is as follows:
A1 is the minimum value of y, and A2 is the maximum value of y, and P=3, X0 are the value of x at y=50%.
External inhibitory activity of the synthesis polypeptide to alpha-glucosidase
The preparation of 1 reagent
1) 0.2M phosphate buffer: Na is weighed2HPO4 2.84g、KH2PO42.72g is dissolved in respectively in 100mL distilled water,
Suitable two kinds of solution is taken to be mixed under the action of magnetic stirring apparatus to pH=6.9, whipping process measures real-time soda acid with pH meter
Degree.
2) P-NPG solution: substrate solution weighs 0.03765g p-NPG, is dissolved in 25mL distilled water.
3) 0.2U/mL α glucoside enzyme solution: the 5 μ L of alpha-glucosaccharase enzyme solution (200U/ml) dispensed is drawn, with distillation
Water is made into 5mL.
4) sample solution: taking the sample of certain mass, is configured to the sample solution (0~10mg/mL) of various concentration, solvent
For water.
5)0.2M Na2CO3: weigh 0.848g Na2CO3, it is dissolved in 40mL distilled water.
2 experimental procedures
1) it being reacted in 96 orifice plates, experimental group, background group, control group, positive controls addition reagent are as shown in table 1, in
37 DEG C of shaking tables react 20min.
The additive amount of 1 sample of table
2) 50 μ L of buffer, 40 μ L of substrate solution are added in each hole, is removed after 37 DEG C of shaking tables react 20min, is added 140
μL Na2CO3Solution terminates reaction.
3) absorbance is surveyed in 405nm, the absorbance of experimental group and control group uses A respectivelyExperimental groupWith AControl groupIt indicates.
4) inhibiting rate-concentration curve drafting: the data obtained makees nonlinear fitting with 9.1 software of OriginPro, selection
Logistic function within the scope of Origin Basic Function, confidence interval selection 95%, output data uses Find Y
from X.Inhibiting rate-concentration curve is made, IC50 value can be found out.
Logistic function formula is as follows:
A1 is the minimum value of y, and A2 is the maximum value of y, and P=3, X0 are the value of x at y=50%.
Application Example 1
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.1% starch solution, 95 DEG C of water-bath 8min are taken, pretreatment makes its denaturation.Experimental group draws 11 peptides (10 mg/ with liquid-transfering gun
ML) 20 μ L are mixed in test tube with 10 μ L of alpha-amylase enzyme solution, and 20 μ L of control group buffer is mixed with 10 μ L of alpha-amylase enzyme solution,
Positive controls take 20 μ L of acarbose (10mg/mL) to mix with 10 μ L of alpha-amylase enzyme solution, react 15min in 37 DEG C of shaking tables.
Above-mentioned 500 μ L of pretreated starch solution is added, reacts 5min in 37 DEG C of shaking tables.600 μ L of DNS solution, 100 DEG C of water-baths are added
15min.After reaction, 200 μ L reaction solutions are drawn with liquid-transfering gun, surveys absorbance in 540nm, calculates inhibiting rate.It can by Fig. 2 a
Know, 11 peptides are 84.75% to the inhibiting rate of alpha-amylase, slightly above the inhibiting rate (81.87%) of acarbose.
Application Example 2
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.1% starch solution, 95 DEG C of water-bath 8min are taken, pretreatment makes its denaturation.Experimental group draws 11 peptides (4 mg/mL) with liquid-transfering gun
20 μ L are mixed in test tube with 10 μ L of alpha-amylase enzyme solution, and 20 μ L of control group buffer is mixed with 10 μ L of alpha-amylase enzyme solution, sun
Property control group take 20 μ L of acarbose (4mg/mL) to mix with 10 μ L of alpha-amylase enzyme solution, react 15min in 37 DEG C of shaking tables.It is added
Pretreated 500 μ L of starch solution reacts 5min in 37 DEG C of shaking tables.DNS solution 600 μ L, 100 DEG C of water-bath 15min is added.Instead
After answering, 200 μ L reaction solutions are drawn with liquid-transfering gun, absorbance is surveyed in 540nm, calculates inhibiting rate.By Fig. 2 a it is found that 11 peptides
Inhibiting rate to alpha-amylase is 65.97%, and the inhibiting rate of acarbose is 77.15% under comparable sodium.
Application Example 3
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.1% starch solution, 95 DEG C of water-bath 8min are taken, pretreatment makes its denaturation.Experimental group draws 11 peptide (1.5mg/ with liquid-transfering gun
ML) 20 μ L are mixed in test tube with 10 μ L of alpha-amylase enzyme solution, and 20 μ L of control group buffer is mixed with 10 μ L of alpha-amylase enzyme solution,
Positive controls take 20 μ L of acarbose (1.5mg/mL) to mix with 10 μ L of alpha-amylase enzyme solution, react 15min in 37 DEG C of shaking tables.
Pretreated 500 μ L of starch solution is added, reacts 5min in 37 DEG C of shaking tables.600 μ L of DNS solution, 100 DEG C of water-baths are added
15min.After reaction, 200 μ L reaction solutions are drawn with liquid-transfering gun, surveys absorbance in 540nm, calculates inhibiting rate.It can by Fig. 2 a
Know, 11 peptides are 51.12% to the inhibiting rate of alpha-amylase, and under concentration, acarbose inhibiting rate is 68.14%.
Application Example 4
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.Experimental group (11 peptides (4mg/mL), 20 μ L and 10 μ L of alpha-glucosidase enzyme solution), background group (11 are added in 96 orifice plates
20 μ L of peptide (4mg/mL) and 10 μ L of buffer), control group (10 μ L of 10 μ L of buffer and alpha-glucosidase enzyme solution), positive control
Group (20 μ L of acarbose solution (4mg/mL) and 10 μ L of alpha-glucosidase enzyme solution), reacts 20min in 37 DEG C of shaking tables.In each hole
50 μ L of buffer, 40 μ L of substrate solution is added, is removed after 37 DEG C of shaking tables react 20min, 140 μ L Na is added2CO3Solution terminates
Reaction.Absorbance is surveyed in 405nm and calculates inhibiting rate.By Fig. 2 b it is found that 11 peptides are to the inhibiting rate of alpha-glucosidase
98.26%, close to acarbose inhibiting rate (99.5%).
Application Example 5
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.Experimental group (11 peptides (1mg/mL), 20 μ L and 10 μ L of alpha-glucosidase enzyme solution), background group (11 are added in 96 orifice plates
20 μ L of peptide (1mg/mL) and 10 μ L of buffer), control group (10 μ L of 10 μ L of buffer and alpha-glucosidase enzyme solution), positive control
Group (20 μ L of acarbose solution (1mg/mL) and 10 μ L of alpha-glucosidase enzyme solution), reacts 20min in 37 DEG C of shaking tables.In each hole
50 μ L of buffer, 40 μ L of substrate solution is added, is removed after 37 DEG C of shaking tables react 20min, 140 μ L Na is added2CO3Solution terminates
Reaction.Absorbance is surveyed in 405nm and calculates inhibiting rate.By Fig. 2 b it is found that 11 peptides are to the inhibiting rate of alpha-glucosidase
95.16%, it is 2.4 times of acarbose inhibiting rate (40.22%).
Application Example 6
By Fig. 1 a peak area percent shown it is found that the purity of 11 peptides is 97.71%, the purity for meeting synthetic peptide is wanted
It asks.Experimental group (11 peptides (0.5mg/mL), 20 μ L and 10 μ L of alpha-glucosidase enzyme solution), background group (ten are added in 96 orifice plates
One peptide (0.5mg/mL), 20 μ L and 10 μ L of buffer), control group (10 μ L of 10 μ L of buffer and alpha-glucosidase enzyme solution), the positive
Control group (20 μ L of acarbose solution (0.5mg/mL) and 10 μ L of alpha-glucosidase enzyme solution), reacts 20min in 37 DEG C of shaking tables.
50 μ L of buffer, 40 μ L of substrate solution are added in each hole, is removed after 37 DEG C of shaking tables react 20min, 140 μ L Na is added2CO3It is molten
Liquid terminates reaction.Absorbance is surveyed in 405nm and calculates inhibiting rate.By Fig. 2 b it is found that inhibition of 11 peptides to alpha-glucosidase
Rate is 94.26%, is 4.7 times of acarbose inhibiting rate (20.19%).
Above embodiments are only preferrred embodiment of the present invention, for explaining only the invention, are not intended to limit the present invention, this
Field technical staff should belong to guarantor of the invention without departing from change made under spirit of the invention, replacement, modification etc.
Protect range.
Sequence table
<110>South China Science & Engineering University
<120>a kind of hypoglycemic 11 peptide
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 11
<212> PRT
<213>artificial sequence (artificial synthesized)
<400> 1
Val Val Asp Leu Val Phe Phe Ala Ala Ala Lys
1 5 10
Claims (4)
1. a kind of hypoglycemic 11 peptide, which is characterized in that the amino acid sequence of 11 peptide is Val-Val-Asp-Leu-Val-
Phe-Phe-Ala-Ala-Ala-Lys is abbreviated as VVDLVFFAAAK.
2. hypoglycemic 11 peptide of one kind according to claim 1, which is characterized in that described VVDLVFFAAAK pairs of 11 peptide
Alpha-amylase has inhibitory activity, and IC50 value is 1.44mg/mL.
3. hypoglycemic 11 peptide of one kind according to claim 1, which is characterized in that described VVDLVFFAAAK pairs of 11 peptide
Alpha-glucosidase has inhibitory activity, and IC50 value is 0.0435mg/mL.
4. hypoglycemic 11 peptide of one kind according to claim 1, which is characterized in that the 11 peptide VVDLVFFAAAK points
Son amount is 1179.44Da, purity 97.71%.
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Cited By (1)
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CN114716524A (en) * | 2022-04-15 | 2022-07-08 | 中国农业大学 | Cooked millet prolamin peptide for inhibiting alpha-amylase and alpha-glucosidase |
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CN114716524B (en) * | 2022-04-15 | 2023-05-23 | 中国农业大学 | Cooked millet prolamin peptides inhibiting alpha-amylase and alpha-glucosidase |
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