WO2019107057A1 - Peptide, et application de celui-ci - Google Patents

Peptide, et application de celui-ci Download PDF

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Publication number
WO2019107057A1
WO2019107057A1 PCT/JP2018/040632 JP2018040632W WO2019107057A1 WO 2019107057 A1 WO2019107057 A1 WO 2019107057A1 JP 2018040632 W JP2018040632 W JP 2018040632W WO 2019107057 A1 WO2019107057 A1 WO 2019107057A1
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Prior art keywords
peptide
muscle
present
composition
seq
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PCT/JP2018/040632
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English (en)
Japanese (ja)
Inventor
裕孝 富
三保子 河崎
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小林製薬株式会社
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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • 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
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/05—Dipeptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/07—Tetrapeptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/08—Peptides having 5 to 11 amino acids
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P21/00—Drugs for disorders of the muscular or neuromuscular system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P21/00—Drugs for disorders of the muscular or neuromuscular system
    • A61P21/02—Muscle relaxants, e.g. for tetanus or cramps
    • 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
    • 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

Definitions

  • the present invention relates to peptides and their use.
  • Muscle is one of the important tissues in the living body, and adult muscle mass is said to account for about 40% of body weight.
  • muscle mass tends to decrease due to various factors such as aging, lack of exercise, fixation of the body due to casts, etc.
  • the decrease in muscle mass causes a decrease in exercise capacity due to muscle atrophy and thus causes inconvenience in daily life.
  • muscle protein synthesis and degradation always occur, and enhanced muscle protein degradation leads to a decrease in muscle mass. Therefore, suppressing the degradation of muscle proteins is important in suppressing muscle atrophy.
  • An object of the present invention is to provide a peptide and the like capable of suppressing muscle atrophy.
  • the present inventors conducted intensive studies in view of the above problems, and found that a specific peptide can suppress muscle atrophy. As a result of further studies based on the findings, the present inventors have completed the present invention.
  • the present invention includes the following.
  • Item 1 A peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13.
  • Item 2. A composition comprising, as an active ingredient, a peptide consisting of an amino acid sequence represented by any one of SEQ ID NOs: 1 to 13.
  • Item 3. A composition for suppressing muscle atrophy comprising, as an active ingredient, a peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13.
  • muscle atrophy can be suppressed.
  • muscle atrophy can be suppressed.
  • the muscle tissue maintenance rate in each group is shown.
  • the muscle tissue maintenance rate in each group is shown.
  • the expression rate of MuRF1 in each group is shown.
  • Peptide The present invention provides a peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13.
  • the peptide has an action of suppressing muscle atrophy.
  • the means for obtaining the peptide of the present invention is not limited, and can be prepared, for example, by conventionally known genetic engineering methods, chemical synthesis methods, and the like.
  • a polynucleotide encoding a peptide represented by any one of SEQ ID NOs: 1 to 13 is inserted into a vector or the like, and a transformant into which the vector or the like is incorporated is cultured It can be produced by obtaining a peptide.
  • the peptide of the present invention can be prepared by subjecting an object having an amino acid sequence encoding the peptide to an enzyme treatment or the like to obtain a desired fragment.
  • the peptide of the present invention can be synthesized and produced by a conventionally known chemical synthesis method according to the information of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13 and the nucleotide sequence encoding it.
  • Chemical synthesis methods include peptide synthesis methods by liquid phase method and solid phase method. Those skilled in the art can easily obtain and understand information such as the nucleotide sequence of a polynucleotide encoding a peptide of the present invention based on the sequence of the peptide of the present invention and the like.
  • the peptide of the present invention may be appropriately modified at its N-terminus, C-terminus, or internal as long as it has a muscle atrophy suppressive action, and may be in the form of a salt.
  • muscle atrophy can be suppressed.
  • Muscles can be classified roughly into skeletal muscle, smooth muscle and cardiac muscle.
  • skeletal muscle tends to decrease due to various factors such as aging, lack of exercise, fixation of body by cast, weightlessness in space, bed rest, inactivity at rest due to disease or injury, etc., malnutrition
  • the decrease causes a decrease in exercise capacity due to muscle atrophy, and in turn causes inconvenience in daily life.
  • muscle loss can be suppressed, that is, muscle atrophy can be suppressed.
  • suppression of muscle atrophy is evaluated by at least one of skeletal muscle weight, the expression level of Atrogin-1 in skeletal muscle, and the expression level of MuRF1 (muscle RING finger 1) in skeletal muscle.
  • Atrogin-1 and MuRF1 are genes associated with muscle atrophy, and it has been conventionally known that their expression levels increase in accelerated muscle protein degradation and muscle atrophy. Therefore, if at least one of suppression of decrease in skeletal muscle weight, suppression of expression of Atrogin-1 in skeletal muscle and suppression of expression of MuRF1 in skeletal muscle is observed using the peptide of the present invention, The peptide is determined to have a muscle atrophy inhibitory action, and the higher the degree of inhibition, the higher the muscle atrophy inhibitory action.
  • the skeletal muscle weight, the expression levels of Atrogin-1 and MuRF1, the degree of increase and decrease of these, and the like may be determined according to a conventionally known method in the present field, and can be determined with reference to, for example, the methods described in the following examples.
  • composition Containing Peptide The present invention provides a composition comprising, as an active ingredient, a peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13.
  • a peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13 (hereinafter sometimes referred to as the peptide of the present invention) is described in the same manner as described above.
  • composition of the present invention contains the peptide of the present invention as an active ingredient, and may contain the peptide of the present invention singly or in combination of two or more.
  • composition of the present invention comprises, in addition to the peptide of the present invention, an optionally pharmaceutically acceptable ingredient, It may further contain any component such as an edible component and a component usable for feed.
  • an excipient as an optional ingredient, an excipient, a binder, a disintegrant, a disintegration inhibitor, a lubricant, a stabilizer, an antiseptic, a pH adjuster, a filler, a solvent (water, Lower alcohols such as methanol, ethanol, isopropanol etc.
  • Alcohols such as polyhydric alcohols such as propylene glycol and 1,3-butylene glycol (anhydrous, water containing or not), hydrocarbons such as isoparaffin etc., diluent Flavor, coloring agent, flavoring agent, suspending agent, wetting agent, emulsifying agent, solubilizing agent, dispersing agent, buffer, bulking agent, thickening agent, surfactant, absorption promoter, adsorbent, coating agent, film Examples are forming agents, cooling agents, gelling agents, sweeteners, anti-inflammatory agents, various nutritional components and the like.
  • the optional components may be suitably determined in accordance with the form of the composition, the application subject, the route of application, the degree of symptoms, the degree of expected effects, etc.
  • One type may be used alone, or two or more types may be used. It may be used in combination, and the compounding amount may be determined appropriately.
  • composition of the present invention is not limited either, and may be appropriately set according to the application subject, application route and the like.
  • the composition of the present invention may be in the form of solution, emulsion, suspension, syrup, elixir, liquid form such as injection, powder, granule, fine granule, tablet (including troche, chewable etc.), round Examples are various forms such as semisolid or solid forms such as freeze-dried products of agents, capsules (including hard capsules and soft capsules), gels, creams, pastes, mousses, sheets, and liquid forms.
  • the composition of the present invention when it is in solid form, it may be used by mixing with a liquid such as water, and the composition of the present invention may be a sustained release dosage form .
  • the tablet may be, if necessary, a tablet having a conventional coating, such as sugar coated tablets, gelatin coated tablets, enteric coated tablets, film coated tablets, double tablets and multilayer tablets. it can.
  • the usage mode of the composition of the present invention is also not limited, and may be appropriately set according to the purpose.
  • Food compositions including beverages, functional health foods (including foods for specified health, nutritionally functional foods, functional indication foods, supplements, etc.), foods for sick persons) as usage modes of the composition of the present invention, Examples thereof include pharmaceutical compositions, feed compositions, food compositions, pharmaceutical compositions, additives to feeds and the like.
  • composition of the present invention may be produced according to a conventional procedure conventionally known in the form, mode of use, etc., and may be produced by mixing the peptide of the present invention and the above-mentioned optional components as required. .
  • the application target of the composition is also not limited, but human, non-human mammals and the like are exemplified.
  • the application amount of the composition of the present invention is not limited as long as the effects of the present invention can be obtained, and the physical size, age, symptoms, application route, application form, degree of symptoms, expected effects of subjects (target animals). It may be set appropriately according to the degree or the like.
  • the dose (intake) may be a daily dose (intake), based on an adult weighing 60 kg. It is exemplified that the peptide is preferably administered (ingested) to be 0.1 to 5000 mg, more preferably 0.5 to 5000 mg.
  • the composition of the present invention may be single dose (intake) or multiple dose (ingestion) per day.
  • the content of the peptide of the present invention is not limited as long as the effects of the present invention can be obtained, and the daily dose (intake) preferably falls within the above range. It may be set appropriately for reference.
  • the content of the peptide of the present invention to be incorporated into the composition of the present invention is preferably 0.001 to 99.9% by mass, more preferably 0.095 to 95%, as the content of the peptide of the present invention incorporated into the composition of the present invention. %, More preferably 0.1 to 95% by mass.
  • the decrease in muscle mass can be suppressed.
  • muscle atrophy can be suppressed.
  • the suppression of muscle atrophy is evaluated by at least one of skeletal muscle weight, the expression level of Atrogin-1 in skeletal muscle, and the expression level of MuRF1 in skeletal muscle, which is explained in the same manner as described above.
  • the present invention provides a composition for suppressing muscle atrophy, which comprises a peptide consisting of the amino acid sequence represented by any one of SEQ ID NOs: 1 to 13 as an active ingredient.
  • the peptide of the present invention described above and the composition of the present invention containing the peptide are aging, lack of exercise, fixation of the body by casting etc., weightlessness in space etc etc., bedridden, It is useful for suppressing muscle atrophy due to various factors such as inactivity at rest due to diseases or injuries, and malnutrition. Therefore, for the peptide of the present invention and a composition containing the peptide, for example, sarcopenia (primary or secondary), muscles, bones, joints, etc. involved in physical exercise are deteriorated, and it is necessary for bedriding or nursing care.
  • sarcopenia primary or secondary
  • the peptide of the present invention and a composition containing the peptide are, for example, for the purpose of maintaining the opportunity for employment of the senior generation, for the purpose of suppressing the aging of movement due to muscle loss due to aging and the like. It can be used preferably for the purpose of maintaining the enjoyment of a hobby requiring muscle strength such as tennis and dance, and also for the purpose of maintaining the muscle and muscle strength of a senior athlete.
  • the peptide of the present invention of the present invention and the composition containing the peptide are, for example, muscle weakness, aging, lack of exercise, inactivity due to diseases or injuries, etc., malnutrition, physical ability Decrease, activity in weightlessness, bedriding and needing care, muscle building, daily health maintenance, maintenance of youthfulness of movement, maintenance of fun of the required hobby of golf, tennis, dance etc. muscular strength, senior athletes It can be preferably used for a subject (target animal) concerned with muscles, muscle weakness and the like.
  • Test Example 1 Preparation of peptide A peptide consisting of the amino acid sequence represented by SEQ ID NO: 1 was synthesized. A peptide consisting of the amino acid sequence represented by each of SEQ ID NOs: 2 to 13 was similarly synthesized.
  • Test Example 2 Muscle atrophy suppression test 2-1. Test and evaluation procedure The muscle atrophy inhibitory effect of each peptide was evaluated according to the following procedure.
  • the mouse myoblast cell line C2C12 (manufactured by ATCC) is inoculated into Dulbecco's modified Eagle's medium (DMEM, manufactured by Wako) containing 10% FBS (fetal bovine serum) and then cultured in a carbon dioxide incubator (37 ° C.) Cultured. The resulting culture was seeded in a 24-well plate and cultured until it became semi-confluent. Then, the obtained culture solution was replaced with DMEM containing 2% horse serum, and cultured for 5 days to differentiate C2C12 cells into myotubes.
  • DMEM Dulbecco's modified Eagle's medium
  • FBS fetal bovine serum
  • DMEM medium without fetal calf serum
  • the culture medium was added such that the amount of peptide in each well was 0.01 mg / ml and 0.001 mg / ml.
  • cDNA was synthesized according to the procedure using PrimeScriptTM RT reagent Kit (manufactured by Takara Bio Inc.). Procedure using the obtained cDNA as a template and SYBR (registered trademark) Premix EX Taq (registered trademark) II (manufactured by Takara Bio Inc.) and Thermal Cycler Dice (registered trademark) Real Time System III (manufactured by Takara Bio Inc.) According to, real-time PCR was performed to quantify the expression amount of Atrogin-1 gene. GAPDH (glyceraldehyde-3-phosphate dehydrogenase) was used as an internal control gene.
  • Atrogin-1 gene was analyzed using Thermal Cycler Dice (registered trademark) Real Time System III dedicated software (manufactured by Takara Bio Inc.). The analysis results are shown as relative values to the expression level of Atrogin-1 gene in the control group.
  • the Atrogin-1 gene is a gene specifically expressed in muscle tissue, and it is judged that the degradation of muscle protein is enhanced when the expression of the gene is high. As apparent from the results shown in Table 1, according to the peptide used in this test, the expression level of Atrogin-1 gene could be reduced. From this, it was found that the peptide used in this test is useful for suppressing the degradation of muscle proteins, particularly for suppressing the degradation of skeletal muscle proteins, that is, useful for suppressing muscle atrophy.
  • Test Example 3 Muscle atrophy suppression evaluation 3-1. Test procedure The muscle atrophy inhibitory effect of the peptide was evaluated according to the following procedure. In this test example, a peptide consisting of the amino acid sequences represented by SEQ ID NOS: 4 and 5 was used.
  • each rat was anesthetized by isoflurane inhalation anesthesia (2.5%). After that, the left leg was left untreated (normal foot), and the sciatic nerve in the right leg was excised (neurectomy leg). Then, each rat was continuously administered a test sample for 7 days, and was exsanguinated under inhalation deep anesthesia of isoflurane on the day after the end of administration, and was euthanized. Then, the muscles (legitimate muscle) of both sides (normal foot and nerve excision foot) were immediately separated and excised, the weight of each was measured, about 50 mg cut and immersed in RNA-Later (0.75 mL) and cryopreserved.
  • test group 1 As the sample administration, the peptide represented by SEQ ID NO: 4 in consideration of feed intake per rat (about 18 g / day), body weight (sample administration day), etc. on 2-3 days immediately before the test.
  • test sample 2 in which the peptide represented by SEQ ID NO: 5 was added to 1 ml of water was orally taken once a day to rats (peptide 6.90 mg / kg / day), and this was used as test group 2 did.
  • test samples 1 and 2 instead of the test samples 1 and 2, 1 ml of water was orally taken by the rat once a day, and this was used as a control group.
  • test samples 1 and 2 intended for people who want to maintain muscle in place of test samples 1 and 2 (leucine, lysine, valine, isoleucine, threonine, phenylalanine, methionine, citric acid, sucrose fatty acid ester, histidine, sweetener (Containing tryptophan, shellfish Ca, lecithin, flavoring agent, coloring agent, vitamin D / reduced maltose) according to the instruction of the commercial product, taking into account the equivalent of administration to rats, 1 The rats were orally ingested once a day (3000 mg / kg / day), and this was designated test group 3.
  • test samples 1 and 2 During the 7 days of administration of test samples 1 and 2, control, and commercial products, normal rat feed and water were used ad libitum except these were given.
  • the muscle tissue retention ratio (neural excise foot muscle weight ⁇ 100 / normal foot muscle weight) of the nerve excision foot muscle weight (right side) to the normal foot muscle weight (left side) of each group was determined. The calculation results are shown in FIG.
  • the amount of beta actin mRNA was quantified.
  • the primer used for real-time PCR used what was synthesize
  • Primer for MuRF1 aggactcctgccgagtgac (SEQ ID NO: 16, Forward primer) ttgtggctcagttcctcctttt (SEQ ID NO: 17, ReversePrimer) The results are shown in FIG.
  • FIG. 1 shows the muscle tissue retention rate of the nerve-resection foot muscle weight (right side) relative to the normal foot muscle weight (left side) of each group.
  • the muscle tissue maintenance rate was improved compared to the control group.
  • the test group 3 group given the commercially available product
  • FIG. 2 shows the muscle tissue maintenance rates in test groups 1 to 3 when the muscle tissue maintenance rate of the nerve tissue for foot muscle weight (right side) with respect to the normal foot muscle weight for the control group (left side) is 100%. Similar to FIG. 1, in FIG. 2 also, in the test groups 1 and 2, the muscle tissue maintenance rate was improved as compared with the control group. On the other hand, in the test group 3, the muscle tissue maintenance rate was lower than in the control group. This also shows that the peptide of the present invention was able to suppress the decrease in muscle weight.
  • FIG. 3 shows the expression rate of MuRF1.
  • the expression level of MuRF1 was reduced in test groups 1 and 2 as compared to the control group.
  • the expression level of the mRNA level of MuRF1 was increased compared to the control group.
  • the expression level of the MuRF1 gene is high, it is judged that the degradation of muscle protein is accelerated. From this, it was found that the peptide of the present invention is useful for suppressing the degradation of muscle protein.
  • the amount of the peptide of the present invention is, for example, preferably 0.1 to 5000 mg, more preferably 0.5 to 50 mg, as a daily dose (intake) based on an adult weighing 60 kg.
  • the administration (intake) of 5000 mg is exemplified.
  • the peptide represented by SEQ ID NO: 4 is, for example, more preferably 1 to 2000 mg, particularly preferably as a daily dose (intake) based on an adult of 60 kg body weight. Is administered (ingested) at 2 to 120 mg.
  • the peptide represented by SEQ ID NO: 5 is, for example, more preferably 1 to 3000 mg, particularly preferably, as a daily dose (intake) based on an adult of 60 kg body weight. Is administered (ingested) at 6 to 360 mg.
  • the administration (intake) amount is an example in the case of oral administration, and in parenteral administration, it may be appropriately determined with reference to the value.
  • a peptide consisting of an amino acid represented by any one of SEQ ID NOs: 1 to 13 and a composition containing the same are useful for inhibiting the degradation of muscle proteins, particularly for inhibiting the degradation of skeletal muscle proteins.
  • the peptide and a composition containing the same are useful for suppressing muscle atrophy, particularly for suppressing muscle atrophy of skeletal muscle.
  • the peptide and a composition containing the same are useful for sarcopenia, locomotive syndrome and the like, particularly muscle atrophy such as age-related muscle atrophy, disuse muscle atrophy and the like.

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Abstract

L'invention a pour objet de fournir un peptide, ou similaire, permettant une inhibition de la myatrophie. Ce peptide est constitué d'une séquence d'acides aminés représentée par une des SEQ ID N°1 à 13. L'invention concerne également une composition ayant pour principe actif ce peptide constitué d'une séquence d'acides aminés représentée par une des SEQ ID N°1 à 13. Enfin, l'invention concerne une composition pour inhibition de myatrophie ayant pour principe actif ce peptide constitué d'une séquence d'acides aminés représentée par une des SEQ ID N°1 à 13.
PCT/JP2018/040632 2017-11-30 2018-11-01 Peptide, et application de celui-ci WO2019107057A1 (fr)

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Citations (5)

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Publication number Priority date Publication date Assignee Title
JP2004277329A (ja) * 2003-03-14 2004-10-07 Nipro Corp ポルフィリン化合物、そのアルブミン包接化合物および人工酸素運搬体
WO2009145363A1 (fr) * 2008-05-30 2009-12-03 ソムノクエスト株式会社 Composition comprenant un extrait dans l’eau chaude de plantes hemerocallis, ladite composition étant efficace dans le traitement de la fatigue en ayant des propriétés antidépressives ou en améliorant le sommeil
WO2011106717A1 (fr) * 2010-02-26 2011-09-01 University Of Florida Research Foundation, Inc. Antioxydants à cible mitochondriale pour lutter contre un dysfonctionnement membranaire et l'atrophie des muscles squelettiques induits par une ventilation mécanique
JP2015189683A (ja) * 2014-03-27 2015-11-02 小林製薬株式会社 アキノワスレグサを含有する筋肉量増加剤及び筋萎縮改善剤
WO2017001515A1 (fr) * 2015-06-30 2017-01-05 Firmenich Sa Peptides marins et santé musculaire

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2004277329A (ja) * 2003-03-14 2004-10-07 Nipro Corp ポルフィリン化合物、そのアルブミン包接化合物および人工酸素運搬体
WO2009145363A1 (fr) * 2008-05-30 2009-12-03 ソムノクエスト株式会社 Composition comprenant un extrait dans l’eau chaude de plantes hemerocallis, ladite composition étant efficace dans le traitement de la fatigue en ayant des propriétés antidépressives ou en améliorant le sommeil
WO2011106717A1 (fr) * 2010-02-26 2011-09-01 University Of Florida Research Foundation, Inc. Antioxydants à cible mitochondriale pour lutter contre un dysfonctionnement membranaire et l'atrophie des muscles squelettiques induits par une ventilation mécanique
JP2015189683A (ja) * 2014-03-27 2015-11-02 小林製薬株式会社 アキノワスレグサを含有する筋肉量増加剤及び筋萎縮改善剤
WO2017001515A1 (fr) * 2015-06-30 2017-01-05 Firmenich Sa Peptides marins et santé musculaire

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Title
YAMADA SHIGERU ET AL.: "Effects of soybean peptide AM intake on muscle weakness in the Elderly", SOY PROTEIN RESEARCH, JAPAN, vol. 16, no. 34, 2013, pages 112 - 118 *

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