CN118047839A - Blood glucose reducing functional polypeptide and application thereof - Google Patents
Blood glucose reducing functional polypeptide and application thereof Download PDFInfo
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- CN118047839A CN118047839A CN202410227596.2A CN202410227596A CN118047839A CN 118047839 A CN118047839 A CN 118047839A CN 202410227596 A CN202410227596 A CN 202410227596A CN 118047839 A CN118047839 A CN 118047839A
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 61
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 52
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 title claims abstract description 51
- 239000008103 glucose Substances 0.000 title claims abstract description 51
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 50
- 239000008280 blood Substances 0.000 title claims abstract description 33
- 210000004369 blood Anatomy 0.000 title claims abstract description 33
- 230000001603 reducing effect Effects 0.000 title claims abstract description 23
- 230000000694 effects Effects 0.000 claims abstract description 24
- 102100025012 Dipeptidyl peptidase 4 Human genes 0.000 claims abstract description 20
- 108010067722 Dipeptidyl Peptidase 4 Proteins 0.000 claims abstract description 19
- 241000699670 Mus sp. Species 0.000 claims abstract description 15
- 239000003814 drug Substances 0.000 claims abstract description 13
- 210000004185 liver Anatomy 0.000 claims abstract description 9
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 16
- 230000002218 hypoglycaemic effect Effects 0.000 claims description 8
- 206010012601 diabetes mellitus Diseases 0.000 claims description 5
- 238000003786 synthesis reaction Methods 0.000 claims description 4
- 239000003112 inhibitor Substances 0.000 claims description 3
- 208000017169 kidney disease Diseases 0.000 claims description 3
- 208000019423 liver disease Diseases 0.000 claims description 3
- 238000000034 method Methods 0.000 claims description 3
- FIYMBBHGYNQFOP-IUCAKERBSA-N Leu-Gly-Gln Chemical compound CC(C)C[C@@H](C(=O)NCC(=O)N[C@@H](CCC(=O)N)C(=O)O)N FIYMBBHGYNQFOP-IUCAKERBSA-N 0.000 claims description 2
- DPURXCQCHSQPAN-AVGNSLFASA-N Leu-Pro-Pro Chemical compound CC(C)C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 DPURXCQCHSQPAN-AVGNSLFASA-N 0.000 claims description 2
- 235000013305 food Nutrition 0.000 claims description 2
- 108010073472 leucyl-prolyl-proline Proteins 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 claims 4
- 230000002265 prevention Effects 0.000 claims 2
- 208000001072 type 2 diabetes mellitus Diseases 0.000 abstract description 4
- 231100000957 no side effect Toxicity 0.000 abstract description 2
- 230000002401 inhibitory effect Effects 0.000 description 7
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 239000002609 medium Substances 0.000 description 5
- 230000037396 body weight Effects 0.000 description 4
- 102100036475 Alanine aminotransferase 1 Human genes 0.000 description 3
- 108010082126 Alanine transaminase Proteins 0.000 description 3
- 108010003415 Aspartate Aminotransferases Proteins 0.000 description 3
- 102000004625 Aspartate Aminotransferases Human genes 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- PNNCWTXUWKENPE-UHFFFAOYSA-N [N].NC(N)=O Chemical compound [N].NC(N)=O PNNCWTXUWKENPE-UHFFFAOYSA-N 0.000 description 3
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- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
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- 239000000859 incretin Substances 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 150000003628 tricarboxylic acids Chemical class 0.000 description 2
- VBBFIBMVFSUUBP-MERQFXBCSA-N (2S)-1-(2-aminoacetyl)-N-(4-nitrophenyl)pyrrolidine-2-carboxamide hydrochloride Chemical compound Cl.NCC(=O)N1CCC[C@H]1C(=O)NC1=CC=C([N+]([O-])=O)C=C1 VBBFIBMVFSUUBP-MERQFXBCSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
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- 208000013016 Hypoglycemia Diseases 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 206010067125 Liver injury Diseases 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 206010061481 Renal injury Diseases 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
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- 230000004110 gluconeogenesis Effects 0.000 description 1
- 230000004153 glucose metabolism Effects 0.000 description 1
- 230000004190 glucose uptake Effects 0.000 description 1
- 229940096919 glycogen Drugs 0.000 description 1
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- 230000002443 hepatoprotective effect Effects 0.000 description 1
- 201000001421 hyperglycemia Diseases 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003914 insulin secretion Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
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- 230000007774 longterm Effects 0.000 description 1
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- 238000012544 monitoring process Methods 0.000 description 1
- 230000001607 nephroprotective effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000007410 oral glucose tolerance test Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
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- 108010005636 polypeptide C Proteins 0.000 description 1
- 230000008569 process Effects 0.000 description 1
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- 239000003531 protein hydrolysate Substances 0.000 description 1
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Landscapes
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a blood glucose reducing functional polypeptide and application thereof. The pentapeptide with the blood glucose reducing function provided by the invention can inhibit DPP-IV activity, promote liver glucose consumption and improve glucose tolerance activity of mice; can achieve the effect of reducing blood sugar from a plurality of targets, is safe and easy to absorb, has no side effect, and can be applied to preparing the medicine for preventing and treating the type II diabetes.
Description
Technical Field
The invention relates to the field of bioactive peptides, in particular to a polypeptide with a blood glucose reducing function and application thereof.
Background
The incidence of diabetes rises year by year, and has become the third chronic disease that seriously threatens human health. Clinical medicines often have side effects such as weight gain, hypoglycemia, gastrointestinal adverse reactions and the like, and the safety of the medicines for long-term administration is still to be further verified. The active peptide is safe, easy to absorb and free of side effects, and is an excellent candidate substance for developing products with the function of reducing blood sugar.
Dipeptidyl peptidase-IV (DIPEPTIDYL PEPTIDASE IV, DPP-IV) inhibitors are one of the new targets for the treatment of type II diabetes. Endogenous incretins can promote insulin secretion and thereby lower blood glucose. However, endogenous incretins are degraded by DPP-IV and lose their physiological activity. Thus, inhibiting DPP-IV activity can promote insulin production and reduce hyperglycemia in diabetes. The structure activity research of the DPP-IV inhibitory peptide shows that: DPP-IV inhibitory peptides typically contain branched amino acids (Ile, leu and Val) at the N-terminus and a Pro residue at the P2 position.
The liver is one of the important organs for maintaining blood glucose balance in the body. The liver can inhibit gluconeogenesis, promote glucose uptake and glycogen synthesis, increase glucose consumption, and reduce glucose content in blood. The prior researches show that the bioactive peptide not only serves as an important provider of a cell nitrogen source, but also serves as a provider of key intermediate metabolites in tricarboxylic acid circulation, so that the normal operation of tricarboxylic acid circulation is ensured, the mitochondrial energy metabolism of cells is promoted, and power is provided for glucose metabolism.
Disclosure of Invention
The invention aims to overcome the defects and shortcomings of the prior art and provide a polypeptide with a blood glucose reducing function.
Another object of the present invention is to provide the use of the polypeptide having blood glucose reducing function.
The aim of the invention is achieved by the following technical scheme:
Compared with the prior art, the invention has the following advantages and effects:
A polypeptide with blood glucose reducing function, which is at least one of the following polypeptides:
QPEVM whose amino acid sequence is Gln-Pro-Glu-Val-Met;
LPLLQ, the amino acid sequence of which is Leu-Pro-Leu-Leu-Gln;
VPQLE whose amino acid sequence is Val-Pro-Gln-Leu-Glu;
LPVPQ, the amino acid sequence of which is Leu-Pro-Val-Pro-Gln;
LPQYL, the amino acid sequence of which is Leu-Pro-Gln-Tyr-Leu;
IPIQY, the amino acid sequence of which is Ile-Pro-Ile-Gln-Tyr;
LGQ, the amino acid sequence of which is Leu-Gly-Gln;
LPP, the amino acid sequence of which is Leu-Pro-Pro.
The polypeptide with the blood glucose reducing function is prepared by a chemical synthesis method.
The polypeptide with the blood glucose reducing function can inhibit DPP-IV activity, promote liver glucose consumption and improve glucose tolerance activity of mice.
The application of the polypeptide with the blood glucose reducing function in preparing a DPP-IV inhibitor.
The application of the polypeptide with the function of reducing blood glucose in preparing medicines for preventing and/or treating type II diabetes.
The application of the polypeptide with the blood glucose reducing function in preparing foods or medicines with the blood glucose reducing effect.
The application of the polypeptide with the function of reducing blood glucose in preparing medicines for preventing and/or treating liver diseases.
The application of the polypeptide with the blood glucose reducing function in preparing medicines for preventing and/or treating kidney diseases.
Compared with the prior art, the invention has the following advantages and beneficial effects:
The pentapeptide with the blood glucose reducing function provided by the invention can inhibit DPP-IV activity, promote liver glucose consumption and improve glucose tolerance activity of mice; can achieve the effect of reducing blood sugar from a plurality of targets, is safe and easy to absorb, has no side effect, and can be applied to preparing the medicine for preventing and treating the type II diabetes and the liver or kidney diseases.
Drawings
FIG. 1 is a schematic diagram of a glucose consumption activity assay;
FIG. 2 is a graph showing comparison of DPP-IV inhibitory activity of polypeptides;
FIG. 3 is a graph comparing the activity of the polypeptides in promoting glucose consumption of HepG2 cells;
FIG. 4 is an in vivo improvement of glucose tolerance activity of a polypeptide in mice.
Fig. 5 shows the hepatoprotective and nephroprotective effects of the polypeptides.
Detailed Description
The present invention will be described in further detail with reference to examples and drawings, but embodiments of the present invention are not limited thereto.
The following examples are presented to further illustrate the practice of the invention, but are not intended to limit the practice and protection of the invention. It should be noted that the following processes, if not specifically described in detail, can be realized or understood by those skilled in the art with reference to the prior art. The reagents or apparatus used were not manufacturer-specific and were considered conventional products commercially available.
Example 1
In the previous experiments, the subject group found a series of polypeptides with DPP-IV inhibitory activity in protein hydrolysates, and in order to further study their properties, the gill biochemical limited was commissioned to perform artificial synthesis samples for subsequent experiments, respectively:
Polypeptide a: QPEVM;
Polypeptide B: LPLLQ;
Polypeptide C: VPQLE;
Polypeptide D: LPVPQ;
polypeptide E: LPQYL;
polypeptide F: IPIQY;
Polypeptide G: LGQ;
Polypeptide H: LPP.
EXAMPLE 2 determination of DPP-IV inhibitory Activity
The DPP-IV inhibition activity is determined as follows: in a 96-well plate, 80. Mu.L of a sample and 80. Mu.L of 0.5mM substrate Gly-Pro-pNA were added, mixed well, incubated in a microplate reader at 37℃for 10min, 40. Mu.L of DPP-IV enzyme solution (preheated at 37℃for 3 min) at a concentration of 12.5mU/mL was added, shaken for 30s, and read at 405nm once every 2min for 120min, thereby monitoring the release of pNA. An equivalent volume of 100mM pH 8.0Tris-HCl buffer was used as a control. The reagent or sample is prepared or diluted by the Tris-HCl buffer solution. The absorbance values (as ordinate) were plotted against time (as abscissa) and the slope of the curve was obtained over a linear range (R 2 > 0.995), and then the DPP-IV inhibitory activity of the samples was calculated according to the following formula. The peptide was tested at a concentration of 800. Mu.M.
DPP-IV inhibition (%) = (1-Slope sample/Slopecontrol) ×100%;
Where Slope sample represents the Slope of the sample group and Slope control represents the Slope of the control group.
The experimental results are shown in figure 2, and the experimental results show that the polypeptides A-F have stronger DPP-IV inhibition activity; whereas polypeptides G and H have poor activity.
Example 3
0.5ML of Caco-2-containing cell suspension was inoculated into a cell (cell diameter: 12 mm) of a 12-well Transwell plate (cell diameter: 0.4 μm) (inoculation density: 4X 10 5 cells/mL). Culturing in an incubator with 5% CO2 at 37deg.C. The medium was changed every 2 days. Culturing for 21 days. Monolayer integrity was monitored by measuring transepithelial resistance (TEER) using a trans-membrane resistance meter, when TEER values should be above 400 Ω cm2 at the start of the simulated absorption experiment. At 20 days of culture, hepG2 cells in logarithmic growth phase were inoculated at 4X 10 6 cells/well into the lower chamber of a 12-well plate and cultured in an incubator at 37℃with 5% CO 2 for 24 hours.
The cells were washed twice with MEM medium to remove residual medium. 0.5mL of peptide (1 mM) dissolved in the basal medium MEM (containing 5mM glucose) was added to the chamber, 1.5mL of basal medium MEM (containing 5mM glucose) was added to the lower chamber, and the Transwell plate was incubated at 37℃with 5% CO 2 for 24 hours. Subsequently, the glucose content of the medium in the lower chamber was determined. Glucose consumption was calculated by subtracting the glucose concentration in the cell culture medium in the lower chamber after incubation 24 from the glucose concentration in the original medium.
As shown in fig. 3, the experimental results show that the glucose consumption of the polypeptides a to G is significantly increased compared with the blank group, and the increase effect is higher than that of the polypeptide H, which proves that the polypeptides can effectively help the body to increase the glucose consumption.
Example 4
Male normal C57BL (body weight: 20.+ -.2 g) mice (6-8 weeks old, purchased from Yaokang biological medicine technologies Co., ltd.) were adapted for one week. Mice were divided into 9 groups of 6 mice each, including a control group (physiological saline) and a polypeptide group (300. Mu. Mol/kg), based on blood glucose level and body weight. Mice were fasted for 12H (no water forbidden during fasting) before OGTT, then were perfused with polypeptides a-H or physiological saline, and were perfused with 50% glucose solution (2.5 g/kg of lavage dose) after 30 min. Blood glucose levels were measured using an Omron glucometer tail vein, including-30, 0, 30, 60 and 120min (0 min at the time of glucose lavage). The area under the curve AUC 0-120 min of each group of samples within 120min is calculated.
The results are shown in FIG. 4, and the experimental results show that the mice with the gastric lavage polypeptides A-F have lower elevation of blood glucose level than the mice with the gastric lavage polypeptides G and H, which proves the effect of improving glucose tolerance.
Example 5
Male C57BL/BSK-db/db (body weight: 41.+ -.2 g) and C57BL/BSK-db/m (body weight: 23.+ -.2 g) mice (6-8 weeks old, available from Yaokang biological medicine Co., ltd.) were fed adaptively for one week. Db/db mice were randomly divided into 3 groups (8 each) DC groups (db/db control group, treated with physiological saline); P-L (low dose peptide treatment group: 50 mg/(kg d)); P-H (high dose peptide treatment group: 300 mg/(kg d)); NC group (db/m mice 8 as normal control, normal saline treatment), wherein the peptide used in the low and high dose peptide groups was polypeptide F (IPIQY). Fasting blood glucose was measured using blood glucose at 1 week of the intragastric interval. After the fourth week, the mice were dissected, plasma was collected, and the content of glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, creatinine, and urea nitrogen in the plasma was measured
The experimental results are shown in fig. 5, and the results show that the polypeptide F has the effect of reducing blood glucose in vivo. Meanwhile, compared with a normal mouse, the diabetic mouse increases the contents of glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, creatinine and urea nitrogen in blood, which indicates liver and kidney injury. The polypeptide F obviously reduces the contents of glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, creatinine and urea nitrogen in blood of a diabetic mouse, which indicates that the polypeptide F also has liver and kidney protecting effects.
The above examples are preferred embodiments of the present invention, but the embodiments of the present invention are not limited to the above examples, and any other changes, modifications, substitutions, combinations, and simplifications that do not depart from the spirit and principle of the present invention should be made in the equivalent manner, and the embodiments are included in the protection scope of the present invention.
Claims (7)
1. A hypoglycemic functional polypeptide, characterized by being at least one of the following polypeptides:
QPEVM whose amino acid sequence is Gln-Pro-Glu-Val-Met;
LPLLQ, the amino acid sequence of which is Leu-Pro-Leu-Leu-Gln;
VPQLE whose amino acid sequence is Val-Pro-Gln-Leu-Glu;
LPVPQ, the amino acid sequence of which is Leu-Pro-Val-Pro-Gln;
LPQYL, the amino acid sequence of which is Leu-Pro-Gln-Tyr-Leu;
IPIQY, the amino acid sequence of which is Ile-Pro-Ile-Gln-Tyr;
LGQ, the amino acid sequence of which is Leu-Gly-Gln;
LPP, the amino acid sequence of which is Leu-Pro-Pro.
2. The polypeptide of claim 1, wherein:
The blood glucose reducing functional polypeptide is prepared by a chemical synthesis method;
The polypeptide with the blood glucose reducing function can inhibit DPP-IV activity, promote liver glucose consumption and improve glucose tolerance activity of mice.
3. Use of a hypoglycemic functional polypeptide according to claim 1 or 2 for the preparation of DPP-IV inhibitors.
4. Use of the hypoglycemic functional polypeptide as claimed in claim 1 or 2 for the preparation of a medicament for preventing and/or treating type two diabetes.
5. Use of the hypoglycemic functional polypeptide as claimed in claim 1 or 2 for preparing food or medicament with hypoglycemic effect.
6. Use of a hypoglycemic polypeptide according to claim 1 or 2 for the preparation of a medicament for the prevention and/or treatment of liver diseases.
7. Use of a hypoglycemic polypeptide according to claim 1 or 2 for the preparation of a medicament for the prevention and/or treatment of kidney diseases.
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