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WO2009035169A1 - Peptide présentant une activité anti-hypertension - Google Patents

Peptide présentant une activité anti-hypertension Download PDF

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Publication number
WO2009035169A1
WO2009035169A1 PCT/JP2008/067052 JP2008067052W WO2009035169A1 WO 2009035169 A1 WO2009035169 A1 WO 2009035169A1 JP 2008067052 W JP2008067052 W JP 2008067052W WO 2009035169 A1 WO2009035169 A1 WO 2009035169A1
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WO
WIPO (PCT)
Prior art keywords
peptide
hyp
gly
seq
sequence number
Prior art date
Application number
PCT/JP2008/067052
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English (en)
Japanese (ja)
Inventor
Toru Hayakawa
Ai Egusa
Tomomi Kouguchi
Koji Iwai
Yoshihisa Takahata
Takashi Ohmori
Original Assignee
Nippon Meat Packers, Inc.
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Filing date
Publication date
Application filed by Nippon Meat Packers, Inc. filed Critical Nippon Meat Packers, Inc.
Publication of WO2009035169A1 publication Critical patent/WO2009035169A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0821—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp
    • C07K5/0823—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp and Pro-amino acid; Derivatives thereof
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A23L33/175—Amino acids
    • 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
    • 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
    • A61P9/14—Vasoprotectives; Antihaemorrhoidals; Drugs for varicose therapy; Capillary stabilisers
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06008—Dipeptides with the first amino acid being neutral
    • C07K5/06017—Dipeptides with the first amino acid being neutral and aliphatic
    • C07K5/06026—Dipeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atom, i.e. Gly or Ala
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06008—Dipeptides with the first amino acid being neutral
    • C07K5/06017—Dipeptides with the first amino acid being neutral and aliphatic
    • C07K5/06034—Dipeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms
    • C07K5/06043—Leu-amino acid
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06008—Dipeptides with the first amino acid being neutral
    • C07K5/06017—Dipeptides with the first amino acid being neutral and aliphatic
    • C07K5/0606—Dipeptides with the first amino acid being neutral and aliphatic the side chain containing heteroatoms not provided for by C07K5/06086 - C07K5/06139, e.g. Ser, Met, Cys, Thr
    • C07K5/06069—Ser-amino acid
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06008—Dipeptides with the first amino acid being neutral
    • C07K5/06078—Dipeptides with the first amino acid being neutral and aromatic or cycloaliphatic
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06104—Dipeptides with the first amino acid being acidic
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06139—Dipeptides with the first amino acid being heterocyclic
    • C07K5/06165—Dipeptides with the first amino acid being heterocyclic and Pro-amino acid; Derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/0806—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/0808—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/081—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0819—Tripeptides with the first amino acid being acidic
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/10—Tetrapeptides
    • C07K5/1002—Tetrapeptides with the first amino acid being neutral
    • C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
    • C07K5/101—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
    • 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
    • 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

Definitions

  • the present invention relates to a peptide having an antihypertensive effect. More specifically, the present invention relates to a peptide comprising a specific amino acid sequence, having an antihypertensive action, a blood vessel preservation action and the like, and a functional food or drug containing the peptide.
  • Angiotensin Converting Enzyme also referred to herein as “ACE” converts angiotensin I (inactive form) to angiotensin II (active form), which has a strong vasoconstrictor action. It breaks down bradykinin, which has vasodilator action, into three inactive peptides.
  • ACE inhibitors substances that inhibit the enzyme activity of angiotensin converting enzyme
  • angiotensin converting enzyme such as captopril and enalapril that inhibit ACE activity (the enzyme activity of angiotensin converting enzyme) have been conventionally used as antihypertensive drugs. .
  • ACE inhibitors obtained from foods or food ingredients can be expected as low-toxic and highly safe antihypertensives and health-oriented foods, and can be ingested in daily eating habits. So far, ACE inhibitors have been reported among many natural products and enzymatic degradation products such as food. In recent years, food-derived ingredients such as sea bream, bonito, and seaweed have been found to have an effect of suppressing an increase in blood pressure, and some are commercially available as foods suitable for people with high blood pressure (for example, 2-3 1 1 4 9 4 gazette, JP 2 0 0 0-4 7 9 9 gazette). There are very few ACE inhibitors derived from meat and meat products.
  • ACE inhibitors derived from meat and meat products are not well known, and even after degradation in the digestive tract, substances (peptides) that have a sufficiently high blood pressure rise inhibitory effect (peptides) It is hardly found. Because of these problems, the present inventors have studied ACE inhibitory substances derived from meat and meat products. As a result, protease degradation products of chicken and pork collagen and peptides contained in the degradation products are found. It was also found that it has an excellent antihypertensive effect even in vivo.
  • the low molecular fraction of the decomposed product has strong ACE inhibitory activity.
  • SHR spontaneously hypertensive rats
  • blood pressure decreased after 2 hours, and the increase in blood pressure was significantly suppressed even in a 4-week long-term administration study. It became clear.
  • the fraction was further fractionated by HPLC to obtain a peptide having a high ACE inhibitory activity, and its amino acid sequence was determined with a protein sequencer. As a result, a peptide having a specific amino acid sequence was obtained.
  • the peptide has a strong ACE inhibitory activity and a blood vessel preservation action. All of the peptides described in the present application are peptides that are not degraded by, for example, the digestive enzyme trypsin chymotrypsin, etc., and are not degraded by digestive enzymes in the digestion solution when ingested orally and retain their activity. It is a peptide.
  • the present invention is based on such findings, and provides a peptide having an antihypertensive action and / or a blood vessel preservation action, and a functional food or drug containing the peptide. Disclosure of the invention
  • Such a peptide has a blood pressure increase inhibitory action and / or a blood vessel preservation action.
  • the present invention is a functional food or drug having an antihypertensive action and / or a blood vessel preservation action, comprising at least one of the peptides of the present invention.
  • SEQ ID NO: 2, 3, 7 to 11, 1, 14, 16 and 18 to 20, more preferably containing at least one peptide consisting of the amino acid sequence represented by SEQ ID NOs: 2, 14, 16, and 19 Is preferred.
  • the present invention comprises the above-described configuration, and the peptide of the present invention comprises a peptide comprising the amino acid sequence represented by SEQ ID NOs: 1 to 23 shown below and an amino acid sequence comprising Hyp-Gly, Ala-Hyp or Pro-Hyp. It is a 2 to 6-mer peptide.
  • Sequence number 22 Ser-Hyp SEQ ID NO: 23: Ile-Hyp
  • Hyp 4-hydroxyl-L-proline residue.
  • the peptide of the present invention can be chemically synthesized according to a conventional peptide synthesis method.
  • collagen (or gelatin) derived from chicken or pig is subjected to enzymatic degradation using a protease according to a conventional method to obtain a collagen degradation peptide, and further subjected to enzymatic degradation as necessary.
  • Purify and isolate the resulting collagen-degrading peptide by conventional purification means such as ultrafiltration, reverse osmosis filtration, gel filtration, ion exchange ram chromatography, reversed-phase high-speed liquid chromatography, etc. Can be obtained.
  • the type of collagen and the collection site are not particularly limited, and various types of collagen can be used.
  • type I collagen derived from chicken and pig legs, skin, bones, tendons, intestines, etc. is used because of its abundant raw materials.
  • the collagen can be prepared according to a conventional method.
  • Gelatin may be used in place of collagen.
  • the protease is not particularly limited as long as it is a protease capable of enzymatically degrading collagen (gelatin), and any of acidic protease, neutral protease, and alkaline protease can be used.
  • an animal-derived protease For example, trypsin, chymotrypsin, pepsin, etc.
  • plant-derived proteases for example, papain, promeline, huisin, etc.
  • microorganism-derived protease, etc. trypsin is preferably used from the viewpoint of enzyme treatment efficiency.
  • the dipeptide in the peptides represented by SEQ ID NOs: 1 to 23 is a peptide consisting of the amino acid sequence represented by SEQ ID NOs: 4 to 7, 9 to 10, or 16 to 18, according to a conventional method, It can also be obtained by enzymatic degradation using carboxypeptidase or aminopeptidase under the optimal conditions.
  • carboxypeptidase examples include carboxypeptidase derived from a kidney or a microorganism, and examples thereof include carboxypeptidase A, B, P, and Y.
  • aminopeptidase examples include a kidney, a kidney derived from a microorganism, an aminopeptidase derived from a microorganism, and the like, and examples thereof include aminopeptidase.
  • the enzyme is deactivated by means such as heating, and then the conventional purification means ⁇ "For example, ultrafiltration, reverse osmosis filtration, gel filtration, ionic exchange ram chromatography, reverse phase high performance liquid chromatography, etc.
  • the target peptide can be obtained by purifying and isolating it.
  • the functional food of the present invention is a functional food having an antihypertensive action and / or a blood vessel preservation action, comprising at least one of the peptides of the present invention as an active ingredient.
  • functional food is a concept that includes ordinary food, beverages, confectionery, feed, and the like.
  • These functional foods are useful for the treatment and prevention of active ingredients as they are, added with various nutrients, or contained in foods and drinks for the purpose of suppressing blood pressure rise and / or maintaining blood vessels. It is eaten as (or food material).
  • an appropriate auxiliary agent for example, glucose, lactose, sucrose, starch, mannitol, dextrin, polyethylene glycol, hydroxyxetyl starch, ethylene glycol, amino acid, etc.
  • It may be formed into a form suitable for edible use, such as granules, granules, tablets, capsules, pastes, etc., and used for food.
  • Seafood processed foods such as chikuwa, confectionery such as snacks, dairy products such as breads, butter and powdered milk, soy products such as tofu and fried milk, etc.), water, fruit juice, milk, refreshing It may be used by adding to beverages such as beverages and dessert foods such as pudding and jelly. Further, it may be in the form of animal feed (including pet food).
  • the intake of the peptide of the present invention in the form of such functional food is appropriately selected and determined according to age, body weight, symptom, degree of disease, form of food, etc.For example, as the amount of peptide per day, 1. 0 mg to 10. O mg, preferably 2.0 mg to 8.0 mg, but since it has the advantage of not adversely affecting the body even if consumed in large amounts, it is more than that. You can take the amount of.
  • the peptide of the present invention is used as a drug having an antihypertensive action and / or a blood vessel preservation action, and in a method for treating hypertension comprising administering an effective amount of the peptide.
  • the peptide is used as an active ingredient, and if necessary, it is mixed with necessary ingredients in the preparation such as appropriate physiologically acceptable additives (for example, carriers, excipients, diluents, etc.) It can be obtained by preparing in an appropriate dosage form, and examples of the form include tablets, powders, granules, capsules and the like.
  • the dose can be appropriately determined according to the patient's symptoms, age, weight, etc., referring to the above intake.
  • the peptide of the present invention has an antihypertensive action and / or a blood vessel preservation action, and the effect is the method described in the following examples and the already known vascular endothelial function evaluation system.
  • the ACE inhibitory activity of the peptide consisting of the amino acid sequence represented by SEQ ID NOs: 1 to 23 was measured by the following method.
  • the peptides consisting of the amino acid sequences shown in SEQ ID NOs: 1 to 23 were prepared by an automatic peptide synthesizer (PSSM8 Shimadzu) by the Fmoc solid phase method. After deprotection, confirm the peptide structure using reverse-phase HPLC (PEGASIL-300, 20 X 250 mm; Senshu, Tokyo, Japan) and mass spectrometer ESI mass spectrometer LC-Q (Thermo Finnigan, San jose, CA). I went. Peptide synthesis reagents were purchased from Shimadzu (Kyoto, Japan).
  • the inhibitory activity against ACE was measured according to the method of Cheung et al. (Cheung et al. J. Biol. Chem. 1980, 255, 401-407).
  • lOOraM folic acid solution pH 8.3
  • 5mM Hip-HL 500mM NaCl
  • 20mU Usagi Lung ACE 20mU Usagi Lung ACE
  • test sample was added at 37 ° C for 30 minutes. Inn I did a cuvate.
  • the enzyme reaction was stopped by adding 1NHC1.
  • -Hip-HL was measured for the amount of hippuric acid released at an absorbance of 228 nm.
  • the inhibitor concentration at which the inhibition of ACE activity 50% was defined as IC 50.
  • Table 1 shows the results of the ACE inhibitory activity (IC 5 ) of the peptides consisting of the amino acid sequences represented by SEQ ID NOs: 1 to 23. As shown in Table 1, all the peptides consisting of the amino acid sequences represented by SEQ ID NOs: 1 to 23 had ACE inhibitory activity. In particular, peptides consisting of the amino acid sequences represented by SEQ ID NOs: 2, 3, 7 to: 11, 14, and 18 to 20 had extremely strong ACE inhibitory activity.
  • a 2 to 6-mer preferably 2 to 5-mer peptide having an amino acid sequence consisting of Hyp-Gly, Ala-Hyp or PnrHyp is effective as an ACE inhibitor. It is done.
  • Sequence number 18 Ser-Hyp-Gly 0. 305
  • L-NAME N-nitro-L-arginine methyl ester
  • a NO synthase inhibitor N-nitro-L-arginine methyl ester
  • drinking water lmg / ml in water, 8 weeks old
  • a peptide 5 g / kg / day
  • water containing NAME was used for drinking water throughout the breeding period.
  • the thoracic aorta was collected, immediately Krebs-Henseleit solution (118. 4mM NaCl, 4. 7 mM KCl, 2. 5mM CaCl 2, 1. 2mM KH 2 P0 4, 1. 2mM MgS0 4 - 7H 2 0, 25 mM NaHC0 3 , 11.6 mM C 6 H 12 0 6 .PH 7.4, 4 ° C), cut into a ring shape of about 3-4 mm, and installed in an organ yanbar 'microbus .
  • Krebs-Henseleit solution 118. 4mM NaCl, 4. 7 mM KCl, 2. 5mM CaCl 2, 1. 2mM KH 2 P0 4, 1. 2mM MgS0 4 - 7H 2 0, 25 mM NaHC0 3 , 11.6 mM C 6 H 12 0 6 .PH 7.4, 4 ° C
  • the organ chamber's microbus was filled with Kerbs-Henseleit solution (same as above, 37 ° C) and bubbled with a mixture of 95% 0 2 and 5% C0 2 so as not to impair the function of the blood vessel specimen. .
  • the blood vessel sample was set to be loaded with lg and left for about 60 minutes to stabilize. Thereafter, phenylene Refurin the After (final concentration 1 X 10- 7 M) was added to cause the blood vessel specimens are contraction, measuring the extension reaction upon addition of acetylcholine (final concentration 1 X 10- 6 M) Total
  • the degree of dilation was evaluated as a blood vessel preservation action, and the effect was shown in four stages (1: No effect 2: Slightly effective 3: Effective) 4: Significant effect).
  • Natural fruit juice (concentrated juice reduction) is mixed with 10 mg of the peptide of the present invention (peptide consisting of the amino acid sequence represented by SEQ ID NO: 2) per 20 O ml of the juice, and then sterilized according to a conventional method. Asse boutique packaging to obtain a juice product.
  • the sausage casing After mixing 10 mg of the peptide of the present invention (peptide consisting of the amino acid sequence shown in SEQ ID NO: 14) per 15 g of the paste, the sausage casing is filled according to a conventional method. Smoked, sterilized, packaged after cooling to obtain wiener sausage.
  • Peptide of the present invention (peptide consisting of the amino acid sequence represented by SEQ ID NO: 19) 6 According to a conventional method, mg was filled into a hard capsule to produce a capsule. Industrial applicability
  • the peptide of the present invention has strong ACE inhibitory activity, vascular endothelial damage recovery, function maintenance, and the like, and has a function of suppressing blood pressure elevation and / or blood vessel preservation. It can be used as a sex food or medicine. Since it is a low molecular weight compound, it has excellent absorbability and can maintain its effect even after being absorbed by the living body.
  • the functional food or drug of the present invention contains a peptide having the above-described action, and it is important to prevent and improve high blood pressure, which is a lifestyle-related disease, through daily life.
  • high blood pressure which is a lifestyle-related disease
  • the functional food or drug of the present invention contains a peptide having the above-described action, and it is important to prevent and improve high blood pressure, which is a lifestyle-related disease, through daily life.

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
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  • Genetics & Genomics (AREA)
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  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Chemical & Material Sciences (AREA)
  • Pharmacology & Pharmacy (AREA)
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  • Public Health (AREA)
  • Animal Behavior & Ethology (AREA)
  • Cardiology (AREA)
  • Heart & Thoracic Surgery (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Mycology (AREA)
  • Food Science & Technology (AREA)
  • Vascular Medicine (AREA)
  • Nutrition Science (AREA)
  • Polymers & Plastics (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Abstract

L'invention concerne un peptide présentant une activité inhibitrice sur une ACE (une enzyme de conversion de l'angiotensine) (c'est-à-dire une activité anti-hypertension)/une activité de protection des vaisseaux sanguins. L'invention concerne également un aliment fonctionnel ou un agent médicinal comprenant ledit peptide. Ce peptide comprend une séquence d'acides aminés décrite dans une quelconque des SEQ ID NOs: 1 à 23. Ledit peptide présente une activité anti-hypertension et/ou une activité de protection des vaisseaux sanguins. L'aliment fonctionnel ou l'agent médicinal comprend ledit peptide comme principe actif et peut être ingéré quotidiennement pour améliorer l'hypertension ou présenter un effet de protection des vaisseaux sanguins, y compris pour guérir un trouble endothélial et garantir les fonctions endothéliales.
PCT/JP2008/067052 2007-09-14 2008-09-16 Peptide présentant une activité anti-hypertension WO2009035169A1 (fr)

Applications Claiming Priority (2)

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JP2007240270 2007-09-14
JP2007-240270 2007-09-14

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WO2009035169A1 true WO2009035169A1 (fr) 2009-03-19

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Cited By (9)

* Cited by examiner, † Cited by third party
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JP2012100612A (ja) * 2010-11-12 2012-05-31 Nippon Meat Packers Inc 白内障予防食品
WO2012102308A1 (fr) * 2011-01-27 2012-08-02 新田ゼラチン株式会社 Agent thérapeutique et agent préventif contre le diabète
US20130123167A1 (en) * 2009-03-11 2013-05-16 Kanazawa Medical University Drug inhibiting the progression of atherosclerosis, preventive drug, blood cholesterol-lowering drug, functional food, and specific health food
JP2014001182A (ja) * 2012-06-20 2014-01-09 Nitta Gelatin Inc 骨、軟骨または皮膚に関連する疾患の治療もしくは予防剤
JP2014141450A (ja) * 2012-12-26 2014-08-07 Nitta Gelatin Inc エラスチン産生促進剤
CN104271144A (zh) * 2012-12-13 2015-01-07 新田明胶株式会社 成肌细胞分化促进剂
JP2015059087A (ja) * 2013-09-17 2015-03-30 新田ゼラチン株式会社 変形性関節症または骨粗鬆症の治療剤もしくは予防剤
CN107586318A (zh) * 2017-05-25 2018-01-16 青岛大学 一种降血压肽及其制备方法
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