CN113943346A - Spirulina antihypertensive peptide and application thereof - Google Patents
Spirulina antihypertensive peptide and application thereof Download PDFInfo
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- CN113943346A CN113943346A CN202111200168.3A CN202111200168A CN113943346A CN 113943346 A CN113943346 A CN 113943346A CN 202111200168 A CN202111200168 A CN 202111200168A CN 113943346 A CN113943346 A CN 113943346A
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- spirulina
- antihypertensive
- polypeptide
- ace
- hypertension
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Images
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Cardiology (AREA)
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- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
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- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biochemistry (AREA)
- Heart & Thoracic Surgery (AREA)
- Genetics & Genomics (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention belongs to the technical field of biology, and relates to a preparation method of spirulina antihypertensive active peptide and application of the spirulina antihypertensive active peptide in functional foods, health-care products or medicines. The invention takes spirulina as raw material, uses proteinase K to carry out enzymolysis to spirulina protein, and obtains spirulina oligopeptide with sequences of TVFNHEGR and LQAGGLF through gel chromatography and reversed phase chromatography separation of polypeptide after enzymolysis. Experiments show that the separated polypeptide has remarkable Angiotensin Converting Enzyme (ACE) inhibitory activity, and the IC50 is 198 mu M and 60.01 mu M respectively. The invention provides a method for preparing spirulina antihypertensive peptides, successfully identifies two spirulina oligopeptides with better antihypertensive activity and novel sequence, provides reference for fully utilizing spirulina protein resources, and has good development and utilization prospects.
Description
Technical Field
The invention belongs to the technical field of bioactive peptides, and relates to application of spirulina polypeptides in research and development of Angiotensin Converting Enzyme (ACE) inhibitors or foods, medicines or health-care products related to hypertension treatment.
Background
Bioactive peptides (Bioactive peptides) are peptide fragments with certain bioactivity consisting of 2-20 amino acid units. The polypeptide with the activities of resisting tumor, resisting bacteria, resisting inflammation, reducing blood sugar, resisting virus, reducing blood pressure and the like is separated from soybean, gluten, casein and aquatic product protein. By 9 months 2021, the BIOPEP database contains up to 4300 or more polypeptides with various biological activities, 1046 polypeptides with ACE inhibitory activity, and the number of the polypeptides is the largest. Compared with macromolecular protein, the bioactive peptide has the characteristics of small molecular weight, easy absorption, low antigenicity and the like, and is widely applied to the fields of food, health-care products, cosmetics, medicines and the like.
Hypertension refers to Systolic Blood Pressure (SBP) >140mmHg and/or Diastolic Blood Pressure (DBP) >90mmHg without the use of a hypotensive agent, and is classified into 1 grade, 2 grades, and 3 grades according to the level of elevation of blood pressure. As a chronic multiple disease, the health and daily life of a large number of patients are disturbed, and researches prove that the blood pressure level and the cardiovascular disease risk present a direct relationship. In addition, long-term hypertension can also cause damage to target organs such as the heart, large blood vessels, kidneys, eyes, and brain. The prevalence rate of hypertension of adults in China is 23.2 percent and still shows an ascending trend, so that effective hypertension treatment medicines and health-care foods have very high research values.
In the regulation of blood pressure, the Renin-Angiotensin System (RAS) and the Kinin-Bradykinin System (KKS) play a crucial role. In the RAS system, angiotensinogen is hydrolyzed by renin to produce angiotensin I, and further, after hydrolysis catalyzed by Angiotensin Converting Enzyme (ACE), angiotensin II is produced, which acts on the corresponding receptor to cause vasoconstriction and thus blood pressure rise. In addition, ACE may also catalyze the degradation of bradykinin and decrease the secretion of NO and prostaglandins through a cascade of reactions, thereby mitigating the effects of nitric oxide and prostaglandin-induced blood pressure elevation. In conclusion, ACE plays a crucial role in the regulation of blood pressure, and the regulation of its activity is crucial for the control of blood pressure. The development of ACE inhibitors has therefore played a major role in the prevention and treatment of hypertension.
The existing blood pressure regulating medicines comprise diuretics, prils, terraces and sartans. These antihypertensive drugs, while regulating blood pressure, reduce the patient's body compliance with the drugs and thus increase the cost of treatment and the difficulty of blood pressure control. There is therefore a need to find more diverse ACE inhibitors. In the past decades, natural polypeptides with the activities of reducing blood pressure and blood sugar, resisting bacteria, regulating immunity and the like are separated from zymolytes of milk, soybeans and fish proteins. The naturally derived ACE inhibitory peptides have higher safety compared with chemical synthesis drugs while effectively generating a regulating effect on the activity of ACE, and although some ACE inhibitory peptides derived from spirulina are reported at present, polypeptides with better activity and higher safety are still to be discovered.
The spirulina has a long history of utilization as a nutrient-rich alga, is rich in nutrients and contains various nutrient substances such as protein, vitamins, trace elements necessary for human bodies and the like. Research shows that the spirulina has the functions of resisting fatigue, lowering blood pressure, resisting bacteria, resisting virus, resisting oxidation and the like. The spirulina protein is possible to release small molecule active peptide with better activity and easier absorption through enzymolysis. Some patents related to spirulina active peptides exist at present, and most of the patents are preparation methods of the active peptides, such as patents with publication numbers of CN111154824A, CN107502641A, CN107674905A, CN103981245A, CN107446977A, CN101906135A, CN10126546 and CN 112646856A. The activity of the polypeptides reported in the patents is focused on the aspects of antioxidation, antibiosis, fatigue resistance and the like, and except that the spirulina antihypertensive peptide with the sequence of IQP is reported in the patent with the publication number of CN101906135A by Lujun, the spirulina antihypertensive peptide with clear sequence is not needed. Therefore, the spirulina antihypertensive peptide still needs to be further developed and researched.
In the area of antihypertensive peptides, patents and polypeptide sequences with exact sequence information have been published as shown in table 1, and both polypeptides claimed in this patent are different from these polypeptides.
Table 1 shows published patents and polypeptide sequences relating to antihypertensive peptides.
Disclosure of Invention
The invention aims to provide a spirulina antihypertensive peptide and application thereof in foods, medicines or health-care products.
In order to achieve the purpose, the invention adopts the technical scheme that:
the antihypertensive peptide is obtained by carrying out enzymolysis and further separation on Spirulina platensis or Spirulina maxima serving as raw materials, wherein the Spirulina polypeptide has an amino acid sequence shown in a sequence table SEQ ID NO. 1; the specific sequence is Thr-Val-Phe-Asn-His-Glu-Gly-Arg (abbreviated as TVFNHEGR).
The spirulina polypeptide is an amino acid sequence in a sequence table SEQ ID NO. 2; the specific sequence is Leu-Gln-Ala-Gly-Gly-Leu-Phe ((LQAGGLF for short).
Wherein the sequences are Thr-Val-Phe-Asn-His-Glu-Gly-Arg (TVFNHEGR), Leu-Gln-Ala-Gly-Gly-Leu-Phe (LQAGGLF) and the molecular weights are 959.03Da and 704.82Da respectively. The polypeptide obtained by an enzymolysis and separation method or a chemical synthesis method can be applied to the preparation of antihypertensive drugs, pharmaceutical compositions or health products.
The spirulina antihypertensive peptide can obviously inhibit Angiotensin Converting Enzyme (ACE) under the in-vitro experiment condition that the malonyl-histidine-leucine is used as a substrate, and the half inhibition rate (IC50) is 190.3 mu M and 60.01 mu M.
The preparation method of the spirulina antihypertensive peptide comprises the following steps: the feed liquid (g: mL) ratio of the spirulina dry powder to water is 1: 10-1: 20, the suspension is frozen at the temperature of-20 ℃, then unfrozen at the temperature of 20-50 ℃, then the feed liquid is treated by using an ultrasonic cell disruption instrument at the power of 200-800w, after circulation (freeze thawing and ultrasonic cell disruption) is carried out for three times, the supernatant is centrifugally taken, protease K is added according to the enzyme substrate ratio of 1-10%, and the enzymolysis conditions are as follows: performing enzymolysis at pH 8-12 and 25-65 deg.C for 1-12 hr, and heating at 95 deg.C for 15min to inactivate enzyme. And (3) using a Sephadex G-15 gel column, using deionized water as a mobile phase, collecting an elution peak by using an automatic fraction collector at the flow rate of 1mL/min, and freeze-drying to obtain the spirulina antihypertensive peptide.
The spirulina polypeptide is used as an active ingredient, and is mixed with auxiliary materials meeting the production requirements of medicines or foods, and the medicines, health products or foods obtained by the conventional preparation method can realize the treatment, alleviation or prevention of hypertension.
The spirulina polypeptide is prepared by one or two of spirulina antihypertensive peptides or spirulina antihypertensive peptide extracts in a sequence table SEQ ID NO.1 or SEQ ID NO.2 and adding any carrier or auxiliary material which is allowed by food or medicine production.
The invention has the advantages that:
the polypeptide obtained by the invention has excellent in-vitro ACE inhibitory activity and has no obvious cytotoxicity in a cell level experiment. The polypeptide is hexapeptide, the molecular weight is 959.03Da and 704.82Da respectively, and the molecular weight is small and easy to absorb. The polypeptide has good application prospect in the fields of foods, health-care products, medicines and the like with blood pressure regulating activity.
Drawings
FIG. 1 shows TVFNHEGR and LQAGGLF mass spectra.
FIG. 2 is a liquid chromatogram for purity determination of TVFNHEGR and LQAGGLF.
FIG. 3 ACE inhibition of TVFNHEGR, LQAGGLF at different concentrations.
FIG. 4LQAGGLF double reciprocal curve.
Table 1 discloses patents and polypeptide sequences relating to antihypertensive peptides.
Detailed Description
The invention is further explained below with reference to the figures and examples. The present invention is directed to the use of spirulina as a starting material, which is proteolytically processed, isolated and screened for a defined sequence, and it is understood that these examples are intended to be illustrative of the present invention and are not intended to limit the scope of the present invention. Furthermore, it should be understood that various changes or modifications can be made by those skilled in the art after reading the disclosure of the present invention, and such equivalents also fall within the scope of the invention.
Example 1
High Performance Liquid Chromatography (HPLC) method for determining in vitro ACE inhibitory activity of polypeptide
The experimental method comprises the following steps:
the principle of the method is as follows: the hippuroyl-histaminoyl-leucine (Hip-His-Leu, HHL, Sigma-Aldrich) can be used as a substrate of Angiotensin Converting Enzyme (ACE) to be decomposed to generate hippuric acid, after different ACE inhibitors are added, the generation amount of hippuric acid is correspondingly reduced, and the inhibitory activity of the inhibitor on the ACE activity can be evaluated by calculating the peak area of hippuric acid at 228 nm.
Experimental reagent:
ACE (0.1U/mL), hippuryl-histidine-leucine (HHL), captopril, 0.1M sodium borate solution (pH8.3, containing 0.3M sodium chloride)
ACE was dissolved in sodium borate buffer to a final concentration of 0.1U/mL for assay. Polypeptide samples are dissolved in sodium borate buffer solution to prepare polypeptide solutions with different concentrations. Then, 20. mu.L of a polypeptide solution of a certain concentration was mixed with 10. mu.L of an ACE solution. The mixture was incubated at 37 ℃ for 5min, and 50. mu.L of 5mM HHL (sodium borate buffer pH8.3, containing 0.3M sodium chloride) was added to the mixture to start the reaction. The reaction was maintained at 37 ℃ for 60min and then 150. mu.L of 1M HCl molar was added to stop the reaction. The solution was passed through a 0.22 μm filter to obtain a reaction solution. mu.L of the reaction solution was loaded into RP-HPLC, which was connected to an Eclipse XDB-C18 column (4.6 mm. times.150 mm. times.5 μm), and the concentration of Hippuric Acid (HA) was measured by UV. Hippuric acid absorbance was measured at 228 nm. All absorbance measurements were performed in triplicate. ACE inhibitory activity was calculated as follows:
ACE inhibitory activity (%) - (AControl-AInhibitor)/AControl 100)
Wherein AInhibitor is the relative area of Hippuric Acid (HA) peaks from the reaction of ACE and HHL with inhibitors. AControl is the relative area of the Hippuric Acid (HA) peak obtained from the reaction of ACE and HHL without inhibitor. IC50 is defined as the concentration of polypeptide that inhibits half of the ACE activity.
Chromatographic conditions are as follows:
c18 column (4.6mm x 150mm x 5 μm, Agilent), detection wavelength: 228 nm; mobile phase: 78% ultrapure water (containing 0.05% TFA) + 22% acetonitrile (containing 0.05% TFA); flow rate: 0.8 mL/min.
Example 2
Preparation of spirulina antihypertensive peptide
Weighing 15g of spirulina dry powder to disperse in 240mL of deionized water, freezing for 4h at-20 ℃, unfreezing at 37 ℃, and then crushing spirulina suspension by using an ultrasonic cell crusher, wherein the parameters of the ultrasonic cell crusher are set to work for 15s at an interval of 15s, and the power is 550W for ultrasonic treatment for 60 min. During ultrasonic treatment, the container is placed on ice, the temperature is controlled to be 0-4 ℃, and the liquid is prevented from being heated up due to ultrasonic treatment. Performing freeze thawing-ultrasonic circulation for 3 times, then 10000RCF, centrifuging at 4 ℃ for 10min, and taking the supernatant.
Measuring protein concentration, adjusting the protein concentration to 10mg/mL by adding deionized water, adjusting the pH to 10 by adding 0.1M NaOH solution, adding proteinase K according to 4.5% of the protein mass content, reacting at 57 ℃ for 4h, heating at 95 ℃ for 15min for inactivating enzyme, centrifuging at 12000g for 10min, taking supernatant, and freeze-drying to obtain the crude spirulina antihypertensive peptide extract. According to the determination, the ACE inhibition rate of the spirulina antihypertensive peptide is 76.44% when the concentration is 400 mu g/mL.
Gel chromatography separation purification and activity evaluation of (II) spirulina antihypertensive peptide
The crude extract of the spirulina antihypertensive peptide is separated and purified by a gel chromatography column (Sephadex G15, 1.6 multiplied by 100cm), deionized water is used as a mobile phase, the flow rate is controlled to be 1mL/min, and four components with the elution time of 80-86min, 87-112min, 113-138min and 139-162min are collected, freeze-dried and named as SK-G1, SK-G2, SK-G3 and SK-G4 respectively.
Evaluation of ACE inhibitory activity of 4 components was performed according to the calculation method of ACE inhibitory activity in example 1, and the ACE inhibitory rate of SK-G4 was 86.85% at a concentration of 400. mu.g/mL.
(III) reverse chromatographic separation and purification and activity evaluation of spirulina antihypertensive peptide
SK-G4 SK-G4 separated from Sephadex G-15 was separated on an Agilent Zorbax SB-Aq C18 column (4.6X 250mm, 5 μm) by the following elution procedure:
1-5 min: 5% acetonitrile (v%); 5-55 min: 5% -95% acetonitrile (v%); 55-60 min: 95% acetonitrile (v%); the flow rate was 0.8 mL/min. 12 fractions were collected according to the following table for peak time.
TABLE 2 elution time component comparison Table
| SK-G4R1 | SK-G4R2 | SK-G4R3 | SK-G4R4 | SK-G4R5 | SK-G4R6 |
| 4-5min | 6-7min | 8-9min | 10-11min | 12-15min | 16-17min |
| SK-G4R7 | SK-G4R8 | SK-G4R9 | SK-G4R10 | SK-G4R11 | SK-G4R12 |
| 17-18min | 19-20min | 21-22min | 23-25min | 32-33min | 59-60min |
The ACE inhibitory activity of 12 components was evaluated according to the method of example 1, and three components, SK-G4R2, SK-G4R3, and SK-G4R5, had relatively good ACE inhibitory activity.
(IV) identification of spirulina antihypertensive peptide sequence
Dissolving a sample in a proper amount of ddH2O, adding DTT to enable the final concentration to be 10mmol/L, adding an IAA solution to enable the final concentration to be 50mmol/L after water bath at 56 ℃ for 1h, carrying out light-shielding reaction for 40min, desalting, volatilizing the solvent in vacuum, and redissolving by using a 0.1% formic acid solution for LC-MS/MS analysis.
Nano LC-MS/MS: the packing material of the chromatographic column is Repuril-Pur C18-AQ (1.9 μm,
) The specification was 150. mu. m.times.150 mm. The mobile phase A, B was water containing 0.1% formic acid and acetonitrile, respectively, and was subjected to gradient elution at a flow rate of 600nL/min after loading 5. mu.L. Gradient program as follows:
TABLE 3 elution gradiometer
| Time (min) | |
| 0 | 4％ |
| 2 | 8％ |
| 45 | 28％ |
| 55 | 40％ |
| 56 | 95％ |
| 66 | 95％ |
And (3) comparing secondary mass spectrum data obtained by using Q active Hybrid Quadrupole-Orbitrap-MS/MS (Thermo Fisher Scirnitic, USA) in a Byonic software self-contained database to obtain a plurality of polypeptide sequences including polypeptides with the sequences TVFNHEGR and LQAGGLF.
Example 3
Virtual screening of spirulina antihypertensive peptides
The resulting polypeptide sequences were subjected to a first round of screening based on abundance. Two-and three-dimensional structures for each polypeptide were mapped using ChemDraw. The polypeptide structure is subjected to protonation and energy minimization at pH7.0, and then is stored and subjected to molecular docking with a human tACE crystal structure (PDB ID: 1O8A) by using Pyrx, wherein the active center zinc ion is taken as the center of a docking box during docking, and the radius of a docking sphere is
The docking result shows the affinity of each polypeptide and ACE, wherein the docking score of TVFNHEGR and LQAGGLF is-9.0, and the affinity is strong. TVFNHEGR and LQAGGLF showed 68.4% and 64.09% inhibition of ACE at a concentration of 400. mu.g/mL, respectively, as determined by the method described in example 1.
Example 4
Mass spectrum identification of TVFNHEGR and LQAGGLF
0.1mg of the sample is dissolved in 0.5mL of ultrapure water, the sample passes through a C18 column and is analyzed by a Q-active mass spectrometer, the sample loading amount is 1 mu L, the carrier gas flow rate is 1.5L/min, and the liquid phase mobile phase is 50% H2O + 50% MeOH.
As shown in figure 1, the molecular weights of two polypeptides TVFNHEGR and LQAGGLF are identified by mass spectrum to be 959.03Da and 704.82Da respectively.
Example 5
Purity identification of TVFNHEGR and LQAGGLF
0.5mg of the sample was weighed, dissolved in 0.5mL of ultrapure water, and then analyzed by a high performance liquid chromatography system equipped with a NanoChrom Chromcore TM 120C 18 (4.6X 250MM X5. mu.M) column. The loading was 40. mu.L, and the mobile phases were acetonitrile containing 0.1% trifluoroacetic acid and ultrapure water, respectively. The flow rate was 1.0mL/min, and a peak was detected at 214nm, and the chromatogram was shown in FIG. 2.
The purity of TVFNHEGR and LQAGGLF polypeptide is more than or equal to 95 percent by analyzing the polypeptide chromatographic peak by a normalization method.
Example 6
IC50 determination of TVFNHEGR, LQAGGLF
ACE inhibition of TVFNHEGR, LQAGGLF was determined as described in example 2 at concentrations of 100, 50, 10, 1, 0.1, 0.01, 0.001. mu.g/mL, three replicates were set up for the experiment, and the average was plotted as log concentration versus inhibition (FIG. 3) to calculate the IC50 value for the polypeptide.
The spirulina blood pressure lowering peptides TVFNHEGR and LQAGGLF are determined to have IC50 values of 190.3 mu M and 60.01 mu M respectively.
Example 7
The inhibitory pattern of LQAGGLF was evaluated by preparing HHL solutions of 4, 2, 1, 0.5, 0.25, 0.1mM and polypeptide solutions of 0.5mg/mL and 0.1mg/mL in boric acid buffer, and taking out the polypeptide solutions of different concentrations and HHL solutions of different concentrations, respectively, as described in example 2. The inverse of the rate of hippuric acid production was plotted against the inverse of substrate concentration, and the inhibition pattern of the polypeptide against ACE was analyzed by the double reciprocal method.
As shown in fig. 4, as the concentration of the polypeptide increases, the slope of the reciprocal curve increases while the vertical intercept does not change, i.e., Vmax does not change, Km increases, and the curve intersects the vertical axis, so that the inhibition pattern of the polypeptide is considered to be competitive inhibition, which is consistent with the effect of LQAGGLF on the ACE active center in the virtual screening.
Sequence listing
<110> oceanographic institute of Chinese academy of sciences
<120> spirulina antihypertensive peptide and application thereof
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 8
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Thr Val Phe Asn His Glu Gly Arg
1 5
<210> 2
<211> 7
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 2
Leu Gln Ala Gly Gly Leu Phe
1 5
Claims (5)
1. A spirulina antihypertensive peptide is characterized in that: the spirulina polypeptide has an amino acid sequence shown in a sequence table SEQ ID NO. 1; the specific sequence is Thr-Val-Phe-Asn-His-Glu-Gly-Arg (abbreviated as TVFNHEGR).
2. A spirulina antihypertensive peptide is characterized in that: the spirulina polypeptide is an amino acid sequence in a sequence table SEQ ID NO. 2; the specific sequence is Leu-Gln-Ala-Gly-Gly-Leu-Phe ((LQAGGLF for short).
3. Use of the spirulina antihypertensive peptide of claim 1 or 2, wherein: use of one or both of the spirulina platensis antihypertensive peptides of claim 1 or claim 2 as an active ingredient (which has an inhibitory effect on Angiotensin Converting Enzyme (ACE)) for the preparation of an Angiotensin Converting Enzyme (ACE) inhibitor or a food, health product or pharmaceutical preparation related to the prevention of hypertension, the alleviation of hypertension or the treatment of hypertension.
4. An angiotensin converting enzyme inhibitor or a preparation for the treatment of hypertension, the alleviation of hypertension or the prevention of hypertension, characterized in that: one or two of the spirulina antihypertensive peptides of claim 1 or claim 2 are used as an active ingredient.
5. The formulation of claim 4, wherein: is prepared by one or two spirulina antihypertensive peptides or spirulina antihypertensive peptide extracts of the 1 and the 2 and any carrier or auxiliary material which is allowed by food or drug production.
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