CN106554388A - Polypeptide with ACE and DPP-IV inhibitory activity and its application - Google Patents
Polypeptide with ACE and DPP-IV inhibitory activity and its application Download PDFInfo
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- CN106554388A CN106554388A CN201510622792.0A CN201510622792A CN106554388A CN 106554388 A CN106554388 A CN 106554388A CN 201510622792 A CN201510622792 A CN 201510622792A CN 106554388 A CN106554388 A CN 106554388A
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Abstract
The present invention relates to one kind comes from the caseic polypeptide with Angiotensin-Converting (angiotensin-converting enzyme, ACE) and DPP-IV dual restraining activities.Its aminoacid sequence is Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe.Not only there is polypeptide FVAPFPEVF ACE inhibitory activity also to have DPP-IV inhibitory activity, and the health product and lead compound that can be used for the diseases such as blood pressure lowering, blood sugar lowering have a good application prospect.
Description
Technical field
The present invention relates to polypeptide FVAPFPEVF prepare suppress Angiotensin-Converting (ACE),
Answering in suppression dipeptidyl peptidase-IV (DPP-IV) or blood pressure lowering, hypoglycemic drug and health product
With.
Background technology
1. ACE inhibitory activity
Hypertension is a kind of common cardiovascular disease, and sickness rate is high, be cause the heart, brain, kidney and
The various complication such as blood vessel and cause apoplexy, promote atherosclerosiss, one of coronary heart disease it is important
Risk factor.The average attack rate of countries in the world is 10%-20%, and China hyperpietic exceedes
1.6 hundred million populations, it is the highly important problem of current social to treat and prevent hypertension.Peptide is a class weight
The Altace Ramipril wanted, the action target spot of peptides blood pressure lowering are to suppress angiotensin-converter
Activity (the document 1 of enzyme (angiotensin-converting enzyme, ACE)：Vanessa
Vermeirssen, John Van Camp, Willy Verstraete, British Journal of
Nutrition 2004,92：357-366).Angiotensin converting enzyme can not be had activity
It is octapeptide Angiotensin II vasoactive with strong contraction that decapeptide is angiotensin I converting,
So that blood pressure is raised, therefore suppression ACE activity can effective control hypertension.Polypeptide is a class weight
The ACE inhibitor wanted, the Peptides of native protein are the main source of ACE inhibitor peptide (texts
Offer 2：Lieselot Vercruysse,John Van Camp,Guy Smagghe,J.Agric.Food
Chem 2005,53:8106-8115).Angiotensin converting enzyme is for body blood pressure and cardiovascular
Function plays important adjustment effect, therefore suppresses the medicine of ACE activity in cardiovascular, heart failure
Play a significant role in the treatment of disease such as exhausting.The ACE inhibitor of polypeptide is while blood pressure lowering
The side effect such as the dry cough of common antihypertensive drugs will not be caused.
2. DPP-IV inhibitory activity
Dipeptidyl peptidase-IV (dipeptidyl peptidase-IV, DPP-IV) is (EC3.4.14.5) a kind of
Serine protease, is distributed widely in human body.DPP-IV inactivates which by the shearing to polypeptide,
So as to reach the effect of regulation of physiological functions.There is on the second of DPP-IV selective hydrolysis N- ends dried meat
The protein of propylhomoserin (Pro) or alanine (Ala).Its substrate specificity includes：Glucagon-like peptide
- 1 (GLP217-36), Gastric inhibitory polypeptide (GIP1-42), neuropeptide (NPY), YY peptides (PYY)
And pancreatic polypeptide family (PP-family) etc..The common feature of these materials is exactly N- ends second
Amino acid residue proline or alanine residue.DPP-IV is by acting on the above
Peptide substrate and in diabetes, glucose tolerance, obesity, appetite stimulator, hyperlipidemia, sclerotin
Play an important role in the relevant disease such as loose, neuropeptide metabolism and T- cell-stimulatings.Cause
This, gives the N- terminal degradations that DPP-IV inhibitor can prevent related substrates peptide, in vivo so as to protect
Barrier function of human body is normally run.
After DPP-IV is by complete GLP-1 and GIP reaction cut-out N- ends 2 amino acid residue,
Its inactivation is made so as to physiological reactions such as the blood glucose regulations that affects GLP-1 related to GIP.Give in vivo
DPP-IV inhibitor can prevent the N- terminal degradations of GLP-1 and GIP, increase insulin secretion
Plus so as to improve glucose tolerance.In view of the substantial connection of DPP-IV inhibitor and metabolism of blood glucose,
DPP-IV inhibitor has become the study hotspot of new type 2 diabetes mellitus medicine.
The content of the invention
It is an object of the invention to provide polypeptide FVAPFPEVF is suppressing ACE activity, is suppressing
Application in DPP-IV activity and blood pressure lowering, blood sugar lowering；Polypeptide FVAPFPEVF has ACE
Suppress living, DPP-IV inhibitory activity and blood pressure lowering, hypoglycemic activity, as hypertension, heart
The health product and medicine of the disease such as disease and cardiovascular diseasess, diabetes, obesity, nephropathy, immunologic derangement
Thing lead compound has a good application prospect.
For achieving the above object, the present invention with the polypeptide FVAPFPEVF as ACE inhibitory activity,
DPP-IV inhibitory activity and blood pressure lowering, the active ingredient of hypoglycemic activity.
Which has sequence table SEQ ID NO：Aminoacid sequence in 1；Polypeptide FVAPFPEVF is
The work of ACE inhibitory activity, DPP-IV inhibitory activity and blood pressure lowering, hypoglycemic drug and health product
Property composition, wherein pharmaceutically acceptable carrier or adjuvant can be added.
Suppress living, DPP-IV inhibitory activity and blood pressure lowering, the polypeptide of hypoglycemic activity with ACE
FVAPFPEVF, aminoacid sequence are Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe, are single
Chain linear structure, white powder are soluble in water, and molecular weight is 1051.5Da；It is active to ACE
With acting on compared with high inhibition, IC50 is 35.76 μM；There is stronger suppression to DPP-IV activity
Effect, IC50 is 2.52mM.
Polypeptide FVAPFPEVF possesses the feature required by ACE inhibitor：
1. ACE inhibitory activity peptide depends primarily on C-terminal aminoacid, and C-terminal is aromatic amino acid
(Trp, Phe, Tyr), or hydrophobic amino acid；And N-terminal for hydrophobic amino acid peptide fragment with compared with
Strong ACE inhibitory activity.The C-terminal dipeptides of polypeptide FVAPFPEVF is above-mentioned aminoacid,
Respectively Val (hydrophobic) and Phe (aromatic series, hydrophobic), N-terminal is hydrophobic amino acid Phe,
Therefore fully meet requirement.
2. the hydrophobic amino acid content of peptide be affect its inhibitory activity major reason, inhibitory activity
High peptide all contains more hydrophobic amino acid.The hydrophobic amino acid difference of polypeptide FVAPFPEVF
There are Phe, Val, Ala, Pro, Phe, Pro, Val and Phe, containing more hydrophobic amino acid.
The present invention compared with prior art, has the advantages that：
The present invention is obtained from casein first and determines the structure of reactive compound, and compound has
Preferably suppress the activity of ACE and DPP-IV, therefore as cardiovascular disease such as treatment hypertension
And the health product and medicine of the disease such as diabetes, heart disease, obesity, nephropathy, immunologic derangement
Lead compound has good potentiality and application prospect.
Specific embodiment
The preparation of 1 polypeptide FVAPFPEVF of embodiment
The method combined with Shotgun proteomic techniques using LC-MS/MS.With milk
Yoghourt is raw material, Jing enzymolysis proteins, centrifugation, ultrafiltration and LC-MS/MS analyses, is closed with reference to structure effect
It is feature, screens the peptide fragment inhibited to ACE and DPP-IV.
Its concrete grammar is as follows：Yoghurt example and 35mM NaCl solutions are according to 1：1 volume ratio
Mixing, is 2.0 with 1M salt acid for adjusting pH, determines the protein content in Yoghourt, add stomach egg
White enzyme, addition is pepsin：Albumen quality ratio=1 in yoghurt example:100, digest in 37 DEG C
1h.PH to 7.0 is adjusted with 1M NaOH and terminates reaction.Enzymolysis solution in 4 DEG C,
40 minutes (3000～10000g) reactant liquors are centrifuged under 10000g (3000～10000g) rotating speed,
Supernatant molecular cut off is 10000 ultrafilter membrane (3000～10000) ultrafiltration, and filtrate is used
C18-SPE post desalinations.By enzymolysis sample lyophilizing after desalination, it is dissolved in 0.1% formic acid water of mass concentration,
LTQ Orbitrap XL (ion trap cyclotron resonance combines mass spectrograph) carry out mass spectral analyses to sample.
Peptide sequence searches storehouse：Sample is carried out into mass spectral analyses with LTQ Orbitrap XL, ion source is
ESI, the data for obtaining enter line retrieval in bovine.fasta storehouses, are screened with reference to structure activity relationship,
Obtain polypeptide of the sequence for FVAPFPEVF.
The ACE inhibitory activity detection of 2 polypeptide FVAPFPEVF of embodiment
Principle
The simulation substrate of ACE catalytic decomposition angiotensin Is under conditions of 37 DEG C, PH8.3
Hippuryl-L-Histidyl-L-Leucine (HHL) produces hippuric acid, and the material has spy at 228nm
Levy ultraviolet absorption peak.When ACE mortifiers are added, catalytic action of the ACE to HHL is pressed down
System, the growing amount of hippuric acid can be reduced.The ultraviolet suction of hippuric acid before and after inhibitor is added by measure
Receipts value can calculate the size of inhibitory activity.
Reaction system
Buffer is 0.05M, PH8.3 borate buffer solutions；Substrate is
Hippuryl-L-Histidyl-L-Leucine (HHL), MW 429.47, are made into above-mentioned buffer
5mM；ACE (angiotensin-converting enzyme) is made into 0.1U/ml with above-mentioned buffer.
ODA(matched group is light absorption value when there is no inhibitor but there is enzyme)：50 μ l are buffered
Liquid+50ulHHL+50 μ l buffer is subsequently adding 50 μ lACE in 37 DEG C of water-bath 5min, 37 °
C water-bath 30min, add 200 μ l, the HCl terminating reactions of 1M to add 1ml ethyl acetate
Extraction product hippuric acid, vibrates 15S, 3500r/min centrifugation 5min, takes 0.8ml supernatants, 90 °
C drying with water bath 15min, are dissolved in 0.8ml distilled water again, detect that light absorption value is OD at 228nmA。
ODB(sample sets are light absorption value when there is inhibitor and enzyme):+ 50 μ of 50 μ l samples
LHHL+50 μ l buffer is subsequently adding 50 μ lACE, 37 DEG C of water in 37 DEG C of water-bath 5min
Bath 30min, adds 200 μ l, the HCl terminating reactions of 1M to add the extraction of 1ml ethyl acetate
Production of hippuric acid, vibrates 15S, 3500r/min centrifugation 5min, takes 0.8ml supernatants, 90 DEG C of water
Bath is dried 15min, is dissolved in 0.8ml distilled water again, detects that light absorption value is OD at 228nmB。
The polypeptide FVAPFPEVF obtained using embodiment 1 is operated as sample.
ODC(blank group is light absorption value when there is no inhibitor and enzyme)：50 μ l buffer+50
μ lHHL+50 μ l buffer is subsequently adding 50 μ l buffer in 37 DEG C of water-bath 5min, 37 °
C water-bath 30min, add 200 μ l, the HCl terminating reactions of 1M to add 1ml ethyl acetate
Extraction product hippuric acid, vibrates 15S, 3500r/min centrifugation 5min, takes 0.8ml supernatants, 90 °
C drying with water bath 15min, are dissolved in 0.8ml distilled water again, detect that light absorption value is OD at 228nmC。
ACE suppression ratio (%)=(ODA-ODB)/(ODA-ODC) × 100%
Respectively with different concentration, ACE suppression is carried out to polypeptide FVAPFPEVF as stated above
Activity determination.As a result it is as follows：
The DPP-IV inhibitory activity detection of 3 polypeptide FVAPFPEVF of embodiment
Principle
Adopt the Chromogenic assay with glycyl proline paranitroanilinum (Gly-Pro-PNA) as substrate
Screening DPP-IV inhibitor, the Cleaning Principle of the method is the catalysis of DPP-IV in the basic conditions bottom
Thing Gly-Pro-p-nitroanilide is hydrolyzed, and generates the paranitroanilinum of yellow, and the latter is in wavelength 405nm
There is characteristic absorption peak at place, reflects enzyme activity by the absorbance size that microplate reader is measured at 405nm
Property height.
Method
Sample：Sample is dissolved in into the Tris-HCl buffer (pH=8.0) of 100mM, 40mg/mL is made into
Storing solution, then storing solution is diluted to into different concentration, as sample solution.
Substrate：Gly-pro-p-nitroanilide solution, with the Tris-HCl buffer (pH=8.0) of 100mM
Gly-pro-p-nitroanilide is configured to into the Gly-pro-p-nitroanilide solution of 1.59mM.
Positive drug：Diprotin solution As, Tris-HCl buffer of the Diprotin A with 100mM
(pH=8.0) 2mM storing solutions are configured to, using being front diluted to 800uM.Remaining storing solution point
If dressing up main, -20 DEG C of preservations.
Enzyme：DPP-IV solution, is configured to 0.01U/mL with the Tris-HCl buffer (pH=8.0) of 100mM
DPP-IV solution.
Stop bath：Acetic acid-the sodium-acetate buffer (pH=4.0) of 1M.
Experiment is carried out in 96 orifice plates, detects absorbance in 405nm using microplate reader.First by enzyme, delay
Rush liquid and medicine and water-bath 30min is distinguished at a temperature of 37 DEG C, then by sample (or buffer), bottom
Thing sequentially adds in 96 orifice plates 37 DEG C and is incubated 10 minutes, adds DPP-IV enzymatic solution, mixes
Incubate 60 minutes after 37 DEG C, add the Acetic acid-sodium acetate buffer (pH 4.0) of 100 μ L 1M
Make reaction terminating.405nm absorbances are determined with microplate reader.Reaction cumulative volume is 100 μ l.Experiment point
For 4 groups, 3 multiple holes are set per group.Each group is respectively：
Sample sets (S groups)：Sample+enzyme+substrate.
Sample blank group (SB groups)：Sample+substrate.
Negative control group (C groups)：Enzyme+substrate.
Blank group (B groups)：Substrate.
Concrete each group sample-adding product are shown in Table 1.
1 DPP-VI inhibitory activity experiment packet of table and sample-adding amount
Note：(1) in table, the unit of numeral is μ l.
(2) it is 100 μ l to react cumulative volume, and each group will with buffer after reactant according to listed addition in table
Final volume is mended to 100 μ l.
(3) calculating of suppression ratio
S group suppression ratio=(1-) × 100%
(4) testing result
Respectively with 300 μ g/ml, 600 μ g/ml, the peptide concentration of 1200 μ g/ml enter as stated above
Row DPP-IV inhibitory activity is detected.As a result such as following table：
Jing IC50Computer calculates the IC of the sequence50For 2.65mg/mL, i.e. 2.52mM.
Claims (4)
1. a kind of polypeptide with ACE and DPP-IV inhibitory activity, it is characterised in that：The polypeptide
For FVAPFPEVF, with sequence table SEQ ID NO：Aminoacid sequence in 1；The polypeptide
Aminoacid sequence is specially Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe.
2. polypeptide described in a kind of claim 1 is preparing ACE inhibitor, DPP-IV inhibitor or drop
Application in blood pressure medication, hypoglycemic drug during one or two or more kinds.
3. according to the application described in claim 2, it is characterised in that：The ACE inhibitor, DPP-IV
In inhibitor and blood pressure lowering, hypoglycemic drug, one or two or more kinds is with polypeptide FVAPFPEVF
For active ingredient.
4. according to the application described in Claims 2 or 3, it is characterised in that：The ACE inhibitor,
Medicine can be added in one or two or more kinds in DPP-IV inhibitor and blood pressure lowering, hypoglycemic drug
Acceptable carrier or adjuvant on.
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| CN201510622792.0A CN106554388B (en) | 2015-09-25 | 2015-09-25 | Polypeptide with ACE and DPP-IV inhibitory activity and application thereof |
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Cited By (3)
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|---|---|---|---|---|
| CN110511274A (en) * | 2019-07-18 | 2019-11-29 | 华南理工大学 | A kind of casein blood sugar reducing peptide and preparation method thereof |
| CN112442108A (en) * | 2019-08-29 | 2021-03-05 | 中国科学院大连化学物理研究所 | ACE and DPP-IV inhibitory peptide of medlar, derivative polypeptide, application and mixture |
| CN113801192A (en) * | 2021-08-31 | 2021-12-17 | 华南理工大学 | Tetrapeptide for inhibiting dipeptidyl peptidase IV and application thereof |
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Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110511274A (en) * | 2019-07-18 | 2019-11-29 | 华南理工大学 | A kind of casein blood sugar reducing peptide and preparation method thereof |
| CN110511274B (en) * | 2019-07-18 | 2022-01-11 | 华南理工大学 | Casein hypoglycemic peptide and preparation method thereof |
| CN112442108A (en) * | 2019-08-29 | 2021-03-05 | 中国科学院大连化学物理研究所 | ACE and DPP-IV inhibitory peptide of medlar, derivative polypeptide, application and mixture |
| CN112442108B (en) * | 2019-08-29 | 2021-11-30 | 中国科学院大连化学物理研究所 | ACE and DPP-IV inhibitory peptide of medlar, derivative polypeptide, application and mixture |
| CN113801192A (en) * | 2021-08-31 | 2021-12-17 | 华南理工大学 | Tetrapeptide for inhibiting dipeptidyl peptidase IV and application thereof |
| CN113801192B (en) * | 2021-08-31 | 2023-06-20 | 华南理工大学 | Tetrapeptides for inhibiting dipeptidyl peptidase IV and application thereof |
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