JP2010024200A - Promotor for synthesizing biogenic collagen and food, drink, cosmetic and quasi-drug for promoting synthesis of biogenic collagen - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide an effective and safe promotor for synthesizing biogenic collagen, and foods, drinks, cosmetics, quasi-drugs, and pharmaceuticals for the blood vessel, arthralgia or the skin for promoting synthesis of biogenic collagen including a dipeptide or a tripeptide having synthesis promotion activity of biogenic collagen. <P>SOLUTION: The biogenic collagen synthesis promotor includes either of a dipeptide or a tripeptide of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, and Ala-Hyp. <P>COPYRIGHT: (C)2010,JPO&INPIT

Description

  The present invention relates to a collagen synthesis promoter in vivo. In addition, the present invention relates to a food and drink for promoting biosynthesis of living collagen, a cosmetic for promoting synthesis of bio-collagen, a quasi-drug for biosynthesis of bio-collagen, or a blood vessel, joint pain, or skin treatment drug.

  Collagen accounts for about 30% of proteins in the body and is abundant in skin, blood vessels and bones. In addition, since this collagen protein decreases with aging, it is considered to be one of the causes such as weakening of blood vessels and reduction of skin elasticity and flexibility. Until now, it has been considered that the intake of collagen has a property that it is difficult to be digested by digestive enzymes, so that it cannot find great utility value in terms of nutrition. However, in recent years, it has been reported that intake of collagen has an effect of promoting collagen synthesis and metabolism (Patent Document 1) and can be used as a drug for treating arthropathy (Patent Document 2). . Furthermore, a patent (Patent Document 3) relating to promotion of skin metabolism by oral intake of collagen protein or a hydrolyzate thereof is also disclosed, and many health foods mainly for beauty are sold.

  Since untreated collagen and gelatin are proteins, they have antigenicity, and there is a problem in the intake of humans who are allergic. Therefore, the antigenicity is lost by reducing the molecular weight of collagen with collagenase, and it is also used as a protein source and infusion preparation component for allergic patients (Patent Document 4).

  Further, Patent Document 5 discloses that the peptide produced by the degradation of collagen by bovine-derived collagenase is Gly-Pro-Hyp, which is the most produced tripeptide, as a peptide having an effect of promoting collagen synthesis.

  In human blood after oral ingestion of hydrolyzate of porcine collagen protein, not only free Hyp but also peptide type Hyp exists, and the peptide type Hyp is mostly composed of Pro-Hyp. -Hyp-Gly, Pro-Hyp-Gly, Ile-Hyp, Leu-Hyp, and Phe-Hyp are slightly present (Non-patent Document 1). In addition to Pro-Hyp, Ala-Hyp-Gly, Pro-Hyp-Gly, Ser-Hyp-Gly, Ile-Hyp, Leu- in addition to Pro-Hyp in human blood after oral intake of hydrolyzate of collagen protein derived from fish Hyp, Phe-Hyp, and Ala-Hyp exist (Non-patent Document 2). However, these documents do not show that the above-mentioned peptides present in human blood after intake of collagen hydrolyzate are involved in collagen synthesis.

Japanese Patent Laid-Open No. 7-278012 JP-A-63-39821 Japanese Patent Laid-Open No. 7-278012 JP-A-7-82299 JP 2006-56904 A J. et al. Agric. Food Chem. , 53, 16, 2005 J. et al. Agric. Food Chem. , 55, 4, 2007

  An object of the present invention is to provide a bio-collagen synthesis promoter that has a bio-collagen synthesis promoting effect and can improve safety. Moreover, it is provision of the food / beverage products, cosmetics, quasi-drugs, and therapeutic agents containing the dipeptide or tripeptide which have a biological collagen synthesis promotion effect | action.

  The present invention provides a biological collagen synthesis promoter containing any of dipeptide peptides or tripeptides of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp.

  In addition, the present invention provides a synthesis containing collagen or gelatin degradation product or artificially synthesized Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide or tripeptide. Provide an accelerator.

  The present invention also relates to a food, beverage, cosmetic, or quasi-drug containing any of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, and Ala-Hyp dipeptide peptides or tripeptides. And providing therapeutic agents.

  The present inventors selected peptides having an effect of promoting collagen synthesis from peptides present in human blood after oral intake of porcine collagen hydrolyzate. Therefore, dipeptides or tripeptides of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp used in the present invention can be brought into the blood by oral administration of collagen protein or collagen peptide. Because it is a reachable peptide, it is safe and effective for the human body, and can be used in foods, beverages, cosmetics, quasi drugs, and therapeutics, and its benefits are very high. .

  Japanese Patent Application Laid-Open No. 2005-289819 describes that the Pro-Hyp dipeptide has a cell growth promoting action, but it describes that the Pro-Hyp dipeptide has a collagen synthesis promoting action. There is no suggestion. Thus, Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, and Ala-Hyp dipeptide or tripeptide used in the present invention have a collagen synthesis promoting effect. Until now, the present inventors have found for the first time that these peptides have an effect of promoting collagen synthesis.

  That is, according to the present invention, by containing these peptides capable of promoting collagen synthesis, an effective in vivo collagen synthesis promoter, food and beverage for promoting collagen synthesis, cosmetics, quasi drugs, and treatment It becomes possible to provide medicine. Examples of the therapeutic agent include blood vessels, joint pain, and skin therapeutic agents, and examples of the vascular therapeutic agents include arteriosclerosis therapeutic agents. Moreover, since the peptides used in the present invention are selected from peptides present in human blood after oral intake of collagen protein hydrolysates, they are safe collagen synthesis promoters, foods, cosmetics, quasi drugs. Products and therapeutic agents can be provided.

  The peptide used in the present invention is obtained, for example, by hydrolysis from collagen protein extracted from the skin of animals such as cattle and pigs, connective tissues such as bones and tendons, or gelatin which is a heat-denatured product of collagen protein. May be used, or an artificially synthesized one may be used. In the case of obtaining from collagen protein, the collagen protein solution is applied to a collagenase enzyme-immobilized column and subjected to enzymatic degradation by the column method. The enzyme reaction completion solution passed through the column is collected, filtered through a 0.45 μm filter, and the filtrate is lyophilized to obtain a collagen tripeptide. Then, the collagen tripeptide powder is redissolved and HPLC Purify each dipeptide and tripeptide containing fraction in (gel filtration and ODS column). Furthermore, in order to obtain a single collagen tripeptide component, it can be purified using ion exchange chromatography and a carbon column. Further, when it is obtained by artificial synthesis, it is artificially synthesized by a solid phase method using a peptide synthesizer. The peptide chain is extended from the C-terminal by the Fmoc method according to the program of the equipment used. In order to prevent side reactions using a carrier that is a support for solid-phase peptide synthesis, ornithine with Fmoc and Boc previously protected α-amino group and δ-amino group and β-amino group protected with Fmoc The β-alanine Fmoc amino derivative is used. Fmoc-Orn (Boc) is bound to the carrier, the α-amino group is deprotected with piperidine or the like, the C-terminal of Fmoc-Orn (Boc) is coupled, and the second ornithine α-amino with piperidine or the like is coupled. The group is deprotected and the C-terminus of Fmoc-β-Ala is similarly coupled. Finally, all deprotection and carrier removal are performed using an acid such as trifluoroacetic acid, and dipeptides and tripeptides can be produced by lyophilizing the extracted with 0.1% aqueous trifluoroacetic acid. And can be obtained by purification with HPLC (reverse feed column) or the like.

  In order to produce a biological collagen synthesis promoter using the peptide obtained as described above as an active ingredient, the peptide obtained as described above is used as an active ingredient, and it is known for foods and beverages, cosmetics, and pharmaceuticals according to conventional methods. What is necessary is just to formulate in combination with a quasi-drug or therapeutic drug carrier.

  Biocollagen synthesis promoter containing peptide used in the present invention, food / beverage product for promoting collagen synthesis, cosmetic product for promoting collagen synthesis, quasi drug for promoting collagen synthesis, and blood vessel, joint pain, or skin treatment The drug is safe for humans and has the effect of promoting biosynthesis of living body collagen, improving symptoms such as skin tension, skin moisture retention, joint pain, hair flexibility and tension, and blood vessel elasticity. Or it is effective for prevention.

  In addition, the biological collagen synthesis promoter of the present invention can be administered in various dosage forms. For example, as oral administration agents, tea agents, capsules, tablets, granules, fine granules, syrups, dry syrups Agents and the like.

  The intake of the peptide serving as an active ingredient for the biocollagen synthesis promoting action of the present invention is not particularly limited, but is usually 85 mg / kg (body weight) or more, preferably 170 mg / kg (body weight) or more per day for an adult. Is preferred. The upper limit of the dosage is preferably 17000 mg / kg (body weight) or less, more preferably 2380 mg / kg (body weight) or less per day. Therefore, the content of the peptide in the biological collagen synthesis promoter may be contained so as to be the above-described intake within a range corresponding to each form.

  As mentioned above, the food / beverage products for biological collagen synthesis of this invention can be mix | blended with the arbitrary components normally used with food / beverage products. Examples of such human or animal foods and drinks include breads, confectionery, noodles, processed meat products / fishery products, processed cereal products, processed vegetables / processed fruits, processed eggs, dairy products, flours, Examples include instant confectionery ingredients, edible fats and oils, soup ingredients, powdered beverages, seasonings, food additives, beverages, and feeds.

  The food and drink for promoting biosynthesis of biological collagen of the present invention includes, for example, nutritional supplements such as vitamins, nutritional supplement beverages, animal health foods, foods for specified health use, nutritional function foods, health function foods and the like. These are commercialized in various commonly used forms such as powders, granules, tablets, capsules, liquids, and films. In commercialization, Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptides or tripeptides, excipients, binders, disintegrants, disintegration inhibitors, Absorption accelerators, adsorbents, lubricants, colorants, preservatives, fragrances, flavoring agents, sweetening agents and the like are blended.

  These dietary supplements, dietary supplement beverages, and the like are produced by conventional methods commonly known in the art.

  The addition amount of the peptide having the collagen synthesis promoting effect in such a food or drink may be added so as to be the above-mentioned intake in a range corresponding to each form of the food or drink. It is preferable to add within the range of -70 weight%. For example, it may be added within a range of 1.5 to 40% by weight for liquid foods and drinks, 30 to 100% by weight for solid foods and drinks, and 30 to 100% by weight for tablet foods and drinks. preferable. More specifically, although not limited to the following, for example, it is preferable to add 1.5 to 40% by weight for health drinks and 1.5 to 40% by weight for functional oolong tea. .

  Examples of the cosmetic for promoting biosynthesis of biological collagen of the present invention include anti-aging cosmetics, cleansing cosmetics, hair cosmetics, bath cosmetics, medical cosmetics, and pigments, skin lotions, cosmetic liquids, emulsions, Use cream, gel, pack, liposome, liquid, clay, solid powder cosmetics, aerosol cosmetics, skin care cosmetics such as haptics, makeup cosmetics such as foundation creams, foundations, etc. or aerosol type, pump Various dosage forms such as cosmetics sprayed by a formula, an extrusion type, or a similar mechanism, and a bath agent can be provided.

  The cosmetic for promoting collagen synthesis of the present invention includes water, alcohol, surfactant (cation, anion, nonion, amphoteric surfactant, etc.), humectant (glycerin, 1,3-butylene glycol, propylene glycol, amino acid, Urea, pyrrolidone carboxylates, nucleic acids, monosaccharides, oligosaccharides and their derivatives, etc.), thickeners (polysaccharides, polyacrylates, carboxyvinyl polymers, polyvinylpyrrolidone, polyvinyl alcohol, chitin, chitosan, alginic acid , Carrageenan, xanthan gum, methylcellulose and the like and derivatives thereof), wax, petrolatum, hydrocarbon saturated fatty acid, unsaturated fatty acid, silicone oil and the like, and derivatives thereof, triglycerides such as tri (caprylic / capric) glyceryl and trioctanoic acid glyceryl Kind Ester oils such as isopropyl stearate, natural fats and oils (Olive oil, camellia oil, avocado oil, almond oil, cocoa butter, evening primrose oil, grape seed oil, macadamian nut oil, eucalyptus oil, rosehip oil, squalane, orange luffy Oil, lanolin, ceramide, etc.), preservatives (oxybenzoic acid derivatives, dehydroacetates, photosensitizers, sorbic acid, phenoxyethanol, etc. and their derivatives), fungicides (sulfur, triclocarbanilide, salicylic acid, zinc pyrithione, hinokitiol, etc.) And their derivatives), ultraviolet absorbers (paraaminobenzoic acid, methoxycinnamic acid, etc. and their derivatives, etc.), anti-inflammatory agents (allantoin, glycyrrhizic acid, etc. and their derivatives, etc.), antioxidants (tocopherol, BHA) , BHT etc. and These derivatives, etc.), chelating agents (edetic acid, hydroxyethanediphosphonic acid, etc. and their derivatives, etc.), animal and plant extracts (Ashitaba, Aloe, Ages, Ogon, Aoba, seaweed, Karin, Chamomile, licorice, kiwi, cucumber , Mulberry, birch, touki, garlic, buttons, hops, marronnier, lavender, rosemary, eucalyptus, milk, various peptides, placenta, royal jelly, etc. and their components, purified products, fermented products, etc., pH adjusters (inorganic acids , Inorganic acid salts, organic acids, organic acid salts and their derivatives), vitamins (vitamin A, vitamin B, vitamin C, vitamin D, etc. and their derivatives), titanium oxide, talc, mica Silica, zinc oxide, iron oxide, silicon and these were processed The body and the like can be blended within the range to achieve the object of the present invention. In addition, the component which comprises the whitening cosmetics of this invention is by no means limited to the above-mentioned, and if it is a component which can be used for cosmetics, it can select freely.

  In the haptic agent, in addition to the above components, a base (kaolin, bentonite, etc.) and a gelling agent (polyacrylate, polyvinyl alcohol, etc.) can be blended within the scope of achieving the object of the present invention.

  In the bath preparation, sulfate, bicarbonate, borate, dye, and humectant can be appropriately blended within the range to achieve the object of the present invention, and can be prepared into powder type and liquid type.

  These cosmetics for promoting the synthesis of biological collagen are produced by conventional methods usually known in this field.

  The amount of the peptide having the effect of promoting collagen synthesis in such cosmetics may be added so as to be the above-mentioned intake in a range corresponding to each cosmetic form. It is preferable to add within the range of%. For example, 0.01 to 5% by weight for liquid cosmetics, 0.01 to 10% by weight for creamy cosmetics, and 0.01 to 5% by weight for powdered cosmetics. Is preferred. More specifically, although not limited to the following, for example, it is preferable to add in the range of 0.01 to 5% by weight for a lotion and 0.01 to 10% by weight for a cosmetic cream.

  Further, the quasi-drugs for promoting biosynthesis of biological collagen of the present invention include moss, gums, toothpastes, liquid toothpastes, gel-like toothpastes, beverages and the like. Moreover, the quasi-drug for bone resorption can be blended together with optional components usually used in quasi-drugs.

  These quasi-drugs for promoting synthesis of biological collagen are produced by conventional methods generally known in this field.

  The addition amount of the compound in such a quasi-drug for promoting biosynthesis of biological collagen may be added so as to be the above-mentioned intake in a range according to the form of the quasi-drug. Is preferably added within a range of 0.01 to 10% by weight. For example, for solid quasi drugs, 0.01 to 10% by weight, for liquid quasi drugs, 0.01 to 5% by weight, for gel or paste quasi drugs, It is preferable to add within the range of 0.01 to 5% by weight. More specifically, although not limited to the following, for example, it is preferable to add 0.01 to 5% by weight to pet gum and 0.01 to 5% by weight with respect to toothpaste.

  Production of the therapeutic agent for promoting collagen synthesis of the present invention is usually carried out by blending the peptide used in the present invention with a pharmaceutically acceptable liquid or solid carrier, and optionally, a solvent, a dispersant, Add emulsifiers, buffers, stabilizers, excipients, binders, disintegrants, lubricants, etc., solids such as tablets, granules, powders, powders, capsules, etc., usually liquids, suspensions, It can be used as a liquid agent such as an emulsion.

  The pharmaceutical carrier can be selected according to the administration form and dosage form of the bone resorption inhibitor. In the case of an oral preparation comprising a solid composition, it can be a tablet, pill, capsule, powder, fine granule, granule, etc., for example, starch, lactose, sucrose, mannitol, carboxymethylcellulose, corn starch Inorganic salts are used. In preparation of the oral preparation, a binder, a disintegrant, a surfactant, a lubricant, a fluidity promoter, a corrigent, a colorant, a fragrance and the like can be further added. For example, in the case of a tablet or pill, if desired, it may be coated with a sugar coating such as sucrose, gelatin or hydroxypropylcellulose, or a film of a gastric or enteric substance. In the case of an oral preparation comprising a liquid composition, it can be a pharmacologically acceptable emulsion, solution, suspension, syrup, etc. For example, purified water, ethanol, etc. are used as a carrier. Is done. Further, if desired, auxiliary agents such as wetting agents and suspending agents, sweetening agents, flavoring agents, preservatives and the like may be added.

  On the other hand, in the case of a parenteral preparation, distilled water for injection, physiological saline, aqueous glucose solution, vegetable oil for injection, sesame oil, peanut oil, soybean oil, corn oil as the diluent is used as the active ingredient of the present invention according to a conventional method. It can be prepared by dissolving or suspending in propylene glycol, polyethylene glycol or the like, and adding a bactericidal agent, stabilizer, isotonic agent, soothing agent, etc., if necessary. In addition, a solid composition can be produced and dissolved in sterile water or a sterile solvent for injection before use.

  Furthermore, each of the above-mentioned preparations can contain pharmaceutically acceptable additives such as coloring agents, preservatives, fragrances, flavoring agents, sweetening agents and other therapeutic agents as desired.

  In formulating, it is preferable to add a stabilizer. Examples of the stabilizer include albumin, globulin, gelatin, mannitol, glucose, dextran, ethylene glycol and the like.

  In general, the dosage of the active ingredient contained in the preparation varies depending on various conditions, for example, the type of extraction solvent, the amount of solvent used, etc. Sometimes it is necessary beyond the scope. Administration may be performed once or within several days within a desired intake range, or may be performed over a predetermined period.

  Hereinafter, the present invention will be further described with reference to test examples and formulation examples. In addition, these do not limit this invention at all.

(Test method and evaluation method)
Artificially synthesized Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp are added to a culture solution in which NIH-3T3-L1 (mouse fibroblast) is cultured, and cultured. Collagen deposited as fluid and extracellular matrix was evaluated by ELISA and Western blotting. As Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, and Ala-Hyp, those synthesized by a combination of Fmoc synthesis method and Boc synthesis method at GL Biochem were used.

NIH-3T3-L1 cells were suspended in DMEM medium containing 0.2% FBS, and seeded at a density of 100,000 cells / well in a 24-well plate. Each peptide was synthesized as a 250 [mu] g / ml to each well was added, as 36 hours at 37 ° 5% CO ^- were incubated ₂ -. Next, the culture supernatant was recovered and used for the ELISA method. In addition, the cell monolayer of the well excluding the culture supernatant was gently washed twice with phosphate buffer. Thereafter, the cells were lysed with a cell lysis buffer (10 mM HEPES, pH 7.8, 150 mM NaCl, 2 mM EDTA, 1.5 mM MgCl ₂ , 0.5 mM dithiothreitol, and a protease inhibitor) and used for Western blotting. When culturing cells, the amount of serum in the culture solution was suppressed to eliminate the influence on collagen synthesis as much as possible. Thereby, only the effect by collagen peptide administration was able to be strictly evaluated at the cell level. In addition, in order to measure the amount of collagen produced by cells more accurately than before, collagen settled in the vicinity of the cells was solubilized (aterized), and the amount of collagen in the culture solution, the vicinity of the cells, and the cells was added and evaluated.

(ELISA method)
To 200 μl of the culture supernatant collected from each well, 100 μl of a pepsin solution (150 mM acetic acid solution, 0.6 mg / ml pepsin) was added, stirred well by inversion, and incubated overnight at 4 degrees. Thereafter, 100 μl of a neutralization solution (200 mM Tris, 150 mM NaCl) was added, and the mixture was thoroughly stirred by inversion mixing to obtain a measurement data. The measurement data was added to a NUNC MaxiSorp 96-well plate at 200 μl / well, and the protein in the culture solution was coated overnight at 4 degrees. Thereafter, the culture solution was removed, washed with a tween / phosphate buffer solution, and incubated for 1 hour in a blocking solution (5% non-fat dry milk also containing a phosphate buffer solution containing 0.1% Tween-20). . After removing the blocking solution and washing with a tween / phosphate buffer, collagen I antibody was reacted as a primary antibody for 1 hour. After removing the primary antibody and washing with a tween / phosphate buffer, it was exposed to a horseradish-conjugated secondary antibody for 1 hour. After removing the secondary antibody and washing with a tween / phosphate buffer, a color former (o-phenylenediamine, citric acid / phosphate buffer, 30% hydrogen peroxide) was added to perform a color reaction, and a reaction stop solution (2NH ₂ The reaction was stopped by adding SO ₄ ), and the absorbance at 492 nm was measured with a 1420 ARVO series multilabel counter. Table 1 shows the amount of collagen increase relative to the control. As shown in Table 1, in the group to which the peptide used in the present invention was added, the amount of collagen in the culture broth increased at about 144 to 187% compared to the group to which no peptide was added. .

(Western blotting method)
The cell eluate dissolved in the cell lysis buffer was fractionated on a polyacrylamide-SDS gel, and the protein was transferred to a nitrocellulose membrane using a BIO CRAFFT semi-drive lotter. Membranes were incubated overnight at 4 degrees with blocking solution (5% non-fat dry milk with phosphate buffer containing 0.1% Tween-20). The membrane was washed and incubated with collagen I primary antibody for 1 hour, then exposed to a horseradish-bound secondary antibody for 1 hour, and finally detected with an ELC Plus Western Blotting Detection System from GE Healthcare Bio-sciences. Glyceraldehyde-3-phosphate dehydrogenase (hereinafter referred to as GAPDH), which is known to be constantly expressed using the same method, was measured as a standard protein. The results are shown in FIG. As shown in FIG. 1, in the group to which the peptide used in the present invention was added, collagen expression in the extracellular matrix was increased. In addition, in the group to which the dipeptide was added, the amount of collagen production was larger than that in the group to which the tripeptide was added.

  As described above, the peptides used in the present invention have been newly confirmed to have a collagen synthesis promoting action, and a biological collagen synthesis promoter containing these peptides, a food and beverage for promoting collagen synthesis. Products, cosmetics for promoting collagen synthesis, quasi-drugs for promoting collagen synthesis, and vascular, joint pain, or skin therapeutic agents are useful as those having a collagen synthesis promoting action.

  In addition, as shown in the examples, the amount of collagen production was greater in the group to which the dipeptide used in the present invention was added than in the group to which the tripeptide was added. Therefore, the administration efficiency can be improved. In addition, since the tripeptides Gly-Pro-Hyp and Pro-Hyp-Gly are degraded between Gly-Pro and Hyp-Gly, the bond between the dipeptides Pro-Hyp and Ala-Hyp is Gly. -Stronger and more stable than bonds between Pro and Hyp-Gly. Therefore, dipeptides are less likely to be decomposed and more stable than tripeptides, so that they can be handled easily in production and the production efficiency can be improved.

(Prescription example)
Biological collagen synthesis promoter containing any of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptide or tripeptide of the present invention Products, cosmetics for promoting collagen synthesis, quasi-drugs for promoting collagen synthesis, and production of blood vessels, joint pain, or skin treatment drugs, according to the above evaluation results, the formulation examples are shown below. May be produced by a conventional method for producing each product, and only the blending amount is shown. The present invention is not limited to these.

The peptide obtained as described above can be added to a normal food or drink or quasi drug. The food / beverage product for promoting biosynthesis of living collagen or the quasi-pharmaceutical product for promoting biosynthesis of biocollagen thus obtained can be expected to have an effect of promoting biosynthesis of biosynthesis and is safe for the human body. It is very useful as an external product.

Moreover, it is also possible to add the peptide obtained as mentioned above to cosmetics. The thus obtained cosmetic for promoting biosynthesis of biological collagen is very useful as a cosmetic because it can be expected to promote biosynthesis of biogenic collagen and is safe for the human body.

It is also possible to add the peptide obtained as described above to a therapeutic agent. The therapeutic agent for promoting biosynthesis of biological collagen obtained in this manner is very useful as a therapeutic agent because it can be expected to promote biosynthesis of biogenic collagen and is safe for the human body.

It is the photographic data which showed the measurement result by the western blotting method about the collagen synthesis promotion effect of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptide or tripeptide.

Claims (5)

  A biological collagen synthesis promoter containing any one of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptide or tripeptide.   Food / beverage products for promoting biosynthesis of biological collagen containing any one of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptides or tripeptides.   A cosmetic for promoting biosynthesis of biological collagen, comprising any one of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptide or tripeptide.   A quasi-pharmaceutical product for promoting collagen synthesis containing any one of Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, Ala-Hyp dipeptide peptide or tripeptide.   A blood vessel, arthralgia, or skin treatment containing either Ala-Hyp-Gly, Pro-Hyp-Gly, Pro-Hyp, Leu-Hyp, or a dipeptide peptide or tripeptide of Ala-Hyp.