Bird's nest peptide with anti-aging function and application thereof

Abstract

The invention discloses cubilose peptide with an anti-aging function and application of the cubilose peptide. The amino acid sequence of the cubilose peptide is TFSLCEICETMVK. The cubilose peptide disclosed by the invention can resist aging, prevent diseases, beautify and protect skin, and improve the immunity of the organism, and has important significance in developing the efficacy of cubilose, improving the economic value of cubilose and expanding the application of the cubilose peptide.

Description

Technical Field

[0001] This invention belongs to the field of protein engineering technology, specifically relating to a bird's nest peptide with anti-aging function and its application. Background Technology

[0002] Aging is the gradual decline in the function of various tissues and organs, the decrease in immunity, and the degenerative changes that occur in various structural components after an organism matures. After aging, the synthesis rate and activity of antioxidant enzymes and antioxidants decrease, the metabolic product malondialdehyde increases, and the balance between the production and elimination of free radicals in the body is disrupted, resulting in the accumulation of free radicals and accelerated aging.

[0003] With the increasing severity of population aging, the demand for anti-aging treatments is growing. Drugs such as rapamycin, aspirin, metformin, and resveratrol have been proven to extend the lifespan of many species, but these drugs have significant side effects. For example, rapamycin can cause adverse reactions such as hyperglycemia, hyperlipidemia, nephrotoxicity, impaired wound healing, decreased platelet count, and immunosuppression; aspirin can easily cause gastrointestinal symptoms such as nausea, vomiting, and pain, and can also lead to abnormal allergic reactions such as rashes, angioedema, and asthma; long-term high-dose use of metformin can induce lactic acidosis; and high-dose resveratrol can cause gastrointestinal and liver dysfunction in humans.

[0004] Bird's nest is the edible portion of the nest built by swiftlets (Apodidae) and other related species using secretions from their sublingual glands. It is primarily produced in Indonesia, Malaysia, Thailand, and Vietnam. Bird's nest contains various nutrients, including protein, amino acids, carbohydrates, and trace elements. Reports indicate that bird's nest has the highest natural sialic acid content among foods, with sialic acid, a hallmark component of bird's nest, accounting for 7%–12% of its dry weight. Studies show that bird's nest possesses various pharmacological effects, including improving immunity, fighting influenza viruses, promoting brain development, preventing neurodegenerative diseases, whitening and moisturizing skin, anti-oxidation, anti-aging, and promoting bone and joint health. In a hydrogen peroxide-induced oxidative stress injury model of human embryonic lung fibroblasts, bird's nest can exert anti-aging effects by increasing the activity of superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) and reducing intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) levels.

[0005] Currently, there is limited research on the amino acid sequence of bird's nest peptides and their related anti-aging functions. Therefore, in-depth research on the sequence of bird's nest peptides with anti-aging effects is of great significance for the development of bird's nest and the enrichment of anti-aging products. Summary of the Invention

[0006] To address the aforementioned technical problems, fully exploit the efficacy of polypeptides in bird's nest, promote the digestion and absorption of bird's nest in the human body, improve people's health, and enhance the application value of bird's nest, this invention provides the following technical solution:

[0007] In a first aspect, the present invention provides a bird's nest peptide with anti-aging function, the amino acid sequence of which is TFSLCEICETMVK (SEQ ID NO:1).

[0008] Secondly, the present invention provides a method for preparing the bird's nest peptide described in the first aspect, specifically comprising the following steps:

[0009] (1) Grind the bird's nest into powder, transfer it to a container, and wash it with water.

[0010] (2) Add simulated gastric juice to the bird's nest for biomimetic digestion, adjust the pH to neutral, and then add simulated intestinal juice for biomimetic digestion to obtain bird's nest biomimetic digestive liquid.

[0011] (3) Add water to the biomimetic digestive fluid, keep it warm in a boiling water bath, cool it and centrifuge it to collect the supernatant.

[0012] (4) The supernatant was subjected to alcohol precipitation, centrifugation, rotary evaporation and drying to obtain a polypeptide mixture.

[0013] (5) Perform amino acid sequence analysis on the polypeptide mixture to synthesize the bird's nest peptide.

[0014] Preferably, the preparation process of the simulated gastric juice is as follows:

[0015] Take 16.4 mL of 2.72 mol / L dilute hydrochloric acid, add about 800 mL of water, then add 10 g of pepsin, shake well, and then add water to make up to 1000 mL.

[0016] Preferably, the preparation process of the simulated intestinal fluid is as follows:

[0017] Dissolve 6.8g of potassium dihydrogen phosphate in 500mL of water, adjust the pH to 6.8 with 0.1mol / L sodium hydroxide solution, and dissolve 10g of trypsin in an appropriate amount of water. Then mix the two solutions and add water to make up to 1000mL.

[0018] Preferably, in step (2), the mass ratio of the simulated gastric juice to the bird's nest is 1:1 to 2.

[0019] Preferably, in step (2), the mass ratio of the simulated intestinal fluid to the bird's nest is 1:1 to 2.

[0020] Preferably, the biomimetic digestion temperature in step (2) is 35-37°C and the biomimetic digestion time is 90-150 min.

[0021] Preferably, the boiling water bath holding time in step (3) is 4 to 6 minutes.

[0022] Preferably, in step (3), the centrifugation speed is 9000-12000 rpm and the centrifugation time is 10-15 min.

[0023] Preferably, in step (4), during alcohol precipitation, the volume fraction of anhydrous ethanol is 40-60% of the total system, and the precipitation time is 10-30 min.

[0024] Preferably, the centrifugation speed in step (4) is 3000-5000 r / min and the centrifugation time is 15-30 min.

[0025] Preferably, the rotary evaporation speed in step (4) is 100-200 r / min and the rotary evaporation temperature is 30-50℃.

[0026] Preferably, the drying in step (4) is performed by freeze drying or low-temperature drying.

[0027] Preferably, in step (5), the amino acid sequence of the peptide chain in the polypeptide mixture is sequenced and identified using an ultra-high performance liquid chromatography-ionization tandem mass spectrometer.

[0028] Thirdly, the present invention provides a composition comprising the bird's nest peptide described in the first aspect or the polypeptide mixture described in the second aspect.

[0029] Preferably, the composition includes cosmetics, pharmaceuticals, or animal feed.

[0030] Preferably, the composition contains excipients permitted for use in cosmetics, pharmaceuticals, or animal feed.

[0031] Fourthly, the present invention provides the use of the bird's nest peptide described in the first aspect or the polypeptide mixture described in the second aspect in the preparation of anti-aging products.

[0032] Preferably, the product is a cosmetic, a pharmaceutical, or animal feed.

[0033] Preferably, the product also contains excipients permitted for use in cosmetics, pharmaceuticals, or animal feed.

[0034] The beneficial effects of this invention are:

[0035] The bird's nest peptides in this invention have anti-aging functions, can scavenge free radicals, delay aging, and prevent diseases. Polypeptide mixtures containing bird's nest peptides have broad application prospects in cosmetics, pharmaceuticals, animal feed, and other fields, promoting the further development of bird's nest products and enhancing the economic and utilization value of bird's nest. Attached Figure Description

[0036] Figure 1The results show the hyaluronidase inhibition rate of bird's nest peptides.

[0037] Figure 2 The figure shows the effects of bird's nest peptides on SOD activity, CAT activity, GPx activity and MDA content in the liver and kidneys of aging mice;

[0038] Figure 3 The figure shows the effects of bird's nest peptides on SOD activity, CAT activity, GSH-Px activity and MDA content in the serum of aging mice.

[0039] Figure 4 The image shows the effect of bird's nest peptides on the content of lipofuscin and hydroxyproline in the skin of aging mice;

[0040] Figure 5 The image shows the effect of bird's nest peptides on the expression levels of elastin (ELN), hyaluronidase 1 (HYAL-1), and hyaluronidase 2 (HYAL-2) mRNA in the skin tissue of aging mice. Detailed Implementation

[0041] The technical solution of the present invention will be clearly and completely described below with reference to the embodiments and accompanying drawings. The described embodiments are only some embodiments of the present invention, and not all embodiments. Based on the embodiments of the present invention, other embodiments obtained by those skilled in the art without creative effort are within the scope of protection of the present invention.

[0042] It should be noted that, unless otherwise specified, the experimental methods and reagents used in the embodiments of the present invention are all conventional experimental methods and reagents in the art.

[0043] The main reagents used in the examples are as follows:

[0044] Pepsin (porcine gastric mucosa, Yuanye Biotechnology, 1:30000).

[0045] Pancreatic enzyme (from the source plant, 1:4000).

[0046] Simulated gastric juice: Take 16.4 mL of 2.72 mol / L dilute hydrochloric acid, add about 800 mL of water, then add 10 g of pepsin, shake well, and then add water to make up to 1000 mL.

[0047] Simulated intestinal fluid: Dissolve 6.8g of potassium dihydrogen phosphate in 500mL of water, adjust the pH to 6.8 with 0.1mol / L sodium hydroxide solution, and dissolve 10g of pancreatic enzyme in an appropriate amount of water. Then mix the two solutions and add water to make up to 1000mL.

[0048] Fmoc-Lys(Boc)-Wang Resin (substitution degree 0.4 mmol / g, cross-linking degree 1%, particle size 100-200 mesh), Fmoc-Phe-OH, Fmoc-Glu-OH, Fmoc-Leu-OH, Fmoc-Val-OH, Fmoc-Thr-OH, Fmoc-Ser-OH, Fmoc-Met-OH, Fmoc-Cys-OH, Fmoc-Ile-OH, Fmoc-Ala-OH, Fmoc-Pro-OH, and Fmoc-Lys-OH were all purchased from Nanjing Peptide Biotechnology Co., Ltd.

[0049] Example 1: Preparation of a polypeptide mixture

[0050] (1) Grind the bird's nest into powder, transfer it to a 500mL beaker, and then rinse it 2-3 times with 4.5 times the weight of the bird's nest in water.

[0051] (2) Simulated gastric juice digestion: Add simulated gastric juice of the same mass as the bird's nest to a beaker and biomimetic digestion at 37°C for 120 min. Then adjust the pH of the solution to 7.0, add simulated intestinal juice of 1.6 times the mass of the dried bird's nest, and continue biomimetic digestion for 120 min to obtain biomimetic digestive solution.

[0052] (3) Enzyme inactivation centrifugation: Add water to the beaker to 400mL, place it in a boiling water bath and keep it warm for 5min, then cool it to room temperature, centrifuge at 10000r / min for 10min, and take the supernatant.

[0053] (4) Add anhydrous ethanol to the supernatant obtained in step (3) to make the ethanol volume fraction reach 60%. Stir and mix well, let stand for 15 min, centrifuge at 3500 r / min for 20 min, transfer the supernatant to a rotary evaporator flask, and remove the ethanol by rotary evaporation at 40℃ and 100 r / min. Pour out the concentrate, add a small amount of water to rinse the rotary evaporator flask to recover the concentrate, and measure the total volume of the concentrate. Repeat rotary evaporation once, dispense the concentrate into glass petri dishes, about 25-30 mL per plate, freeze quickly at -80℃ for 12 h, and freeze dry in a freeze dryer for 24 h to obtain a powdered polypeptide mixture.

[0054] Example 2: Amino acid sequence analysis of a polypeptide mixture

[0055] The amino acid sequences of peptide chains in a polypeptide mixture were sequenced and identified using ultra-high performance liquid chromatography-electron ionization tandem mass spectrometry (UPLC-ESI-MS / MS). Specific chromatographic conditions: Acclaim PepMap C 18The chromatographic column (75 μm × 25 cm) was used. Mobile phase A consisted of an aqueous solution containing 0.1% formic acid, and mobile phase B consisted of an acetonitrile solution containing 0.1% formic acid. The sample loading volume was 5.0 μL, and the elution flow rate was 300.0 nL / min. The positive charge spray voltage for mass spectrometry was 2.0 kV.

[0056] The identified peptide amino acid sequence is as follows:

[0057] TFSLCEICETMVK(SEQ ID NO:1);

[0058] PAPPKPEPKPK(SEQ ID NO:2);

[0059] KPAPPKPEPK(SEQ ID NO:3);

[0060] LTLSALLDGK(SEQ ID NO:4);

[0061] DSYVGDEAQSK(SEQ ID NO:5);

[0062] VALTGLTVAEYFR (SEQ ID NO:6);

[0063] VVDLLAPYAK (SEQ ID NO:7);

[0064] YFLHQSHEER (SEQ ID NO:8);

[0065] DGFFGNPLAPNPADK (SEQ ID NO:9).

[0066] Then, the Mascot Server online system is used to compare data against the database and select those with high matching scores, resulting in a relative strength greater than 10. 9 The three peptide segments (SEQ ID NO: 1-3).

[0067] Example 3: Synthesis of Bird's Nest Peptide (SEQ ID NO:1)

[0068] Bird's nest peptide (TFSLCEICETMVK, SEQ ID NO:1) was synthesized using a solid-phase synthesis process, following the direction from C-terminus to N-terminus. The specific process is as follows:

[0069] Weigh 4.0 g of Fmoc-Lys(Boc)-Wang Resin with a substitution degree of 0.4 mmol / g, add it to a solid-phase reaction column, wash twice with 20 mL of DMF to remove the solvent, and add 60 mL of DMF to swell for 30 min. Wash twice with DMF, add a piperidine-DMF mixed solution (volume ratio 1:3), and stir for 20 min. Monitor the completion of the reaction using the ninhydrin colorimetric method. Wash five times each with DMF and DCM, dissolve 2.17 g (6.40 mmol) of Fmoc-Val-OH and 1.04 g (7.60 mmol) of HOBt in DMF, add 1.20 mL (7.6 mmol) of DIC under ice bath conditions, stir for 8 min in the dark, and then add it to the above-mentioned solid-phase reaction column with the solvent removed. Add 0.08 g (0.64 mmol) of DMAP, stir under nitrogen protection for 3 h, and monitor the completion of the reaction using the ninhydrin colorimetric method. The solvent was removed, and the resin was washed five times with DMF to obtain Fmoc-Val-Lys-Wang Resin. Following the coupling method described above, the corresponding Fmoc protecting amino acids were added sequentially according to the peptide sequence to elongate the peptide chain. After the final coupling reaction, the resin was washed four times each with DCM, DMF, and MeOH.

[0070] After drying the resin with nitrogen, it was transferred to a round-bottom flask and subjected to three cycles of 209 mL of a HOAc-TFE-DCM mixed solution (volume ratio 1:3:6) for 30 min, 15 min, and 5 min respectively. The mixture was filtered, and the filtrate was concentrated to one-quarter of its original volume. The concentrate was then added to 10 times its volume of diethyl ether for precipitation, and the mixture was allowed to stand overnight in a refrigerator. The filter cake was then filtered again, washed six times with a small amount of diethyl ether, and vacuum dried to obtain fully protected crude bird's nest peptides with a yield of 91.50%.

[0071] The synthesized bird's nest peptides were analyzed and identified according to the method in Example 2: sequencing and identification methods were used.

[0072] The crude bird's nest peptides were dissolved in an appropriate amount of DMSO and purified by high-performance liquid chromatography (HPLC). A C18 reversed-phase column was used. The eluents were: solution A, an aqueous solution of 0.1% TFA; and solution B, an aqueous solution of acetonitrile containing 0.1% TFA. The detection wavelength was 220 nm. The purified liquid was lyophilized to obtain the bird's nest peptide product with a purity of 99.6%.

[0073] Example 4 Hyaluronidase Inhibition Experiment of Bird's Nest Peptide (SEQ ID NO:1)

[0074] 4.1 The experimental groups and specific treatments for each group are as follows:

[0075] Control solution: 0.4 mg / mL sodium hyaluronate + 600-1000 U / mL HAase + deionized water.

[0076] Control blank solution: acetic acid buffer solution + deionized water.

[0077] Positive group solution: 0.4 mg / mL sodium hyaluronate + 600-1000 U / mL HAase + 10 mg / mL dipotassium glycyrrhizate.

[0078] Positive control blank solution: Acetic acid buffer solution + 10 mg / mL dipotassium glycyrrhizate.

[0079] Test sample solution: 0.4 mg / mL sodium hyaluronate + 600~1000 U / mL HAase + 10 mg / mL bird's nest peptide (SEQ ID NO:1) solution.

[0080] Blank solution for test sample: Acetic acid buffer solution + bird's nest peptide (SEQ ID NO:1) solution.

[0081] 4.2 Experimental Procedure

[0082] The HAase activity inhibition rate was determined using the Elson-Morgan method: 0.1 mL of 2.5 mmol / L CaCl2 was added to 0.5 mL of HAase and incubated at 37 °C for 20 min; 0.5 mL of different sample solutions were added and incubated at 37 °C for 20 min; 2 mL of sodium hyaluronate was added and incubated at 37 °C for 30 min; 1 mL of acetylacetone solution was added, and the mixture was heated in a boiling water bath for 15 min, immediately cooled with ice water for 5 min, and then 1.0 mL of Ehrlich reagent was added. After incubation for 20 min, the absorbance was measured at 530 nm. The HAase activity inhibition rate was calculated using the following formula.

[0083] HAase inhibition rate (%) = [(ab) - (cd)] / (ab) × 100%

[0084] In the formula: a is the OD value of the control solution (sodium hyaluronate + HAase + deionized water); b is the OD value of the control blank solution (acetic acid buffer solution + deionized water); c is the OD value of the test sample solution (sodium hyaluronate + hyaluronidase + sample solution); d is the OD value of the test sample blank solution (acetic acid buffer solution + sample solution).

[0085] Hyaluronic acid is a natural polysaccharide whose main function is moisturizing. It can effectively improve the skin's hydration, elasticity, and softness. It can also promote skin metabolism, reduce skin sensitivity, and inhibit skin aging, thus maintaining healthy skin. Hyaluronidase is an enzyme that hydrolyzes hyaluronic acid. When hyaluronidase activity increases, it promotes the breakdown of hyaluronic acid, leading to moisture loss and the formation of fine lines and wrinkles.

[0086] like Figure 1 As shown, the bird's nest peptide (SEQ ID NO:1) sample had an inhibitory effect on hyaluronidase, with an inhibition rate of 38.76%, indicating that bird's nest peptide (SEQ ID NO:1) can significantly inhibit hyaluronidase activity and inhibit skin aging.

[0087] Example 5: Effects of Bird's Nest Peptide (SEQ ID NO:1) on Anti-aging in Mice

[0088] ICR mice were selected as the experimental system. An aging model was established by subcutaneous injection of a 50 g / L D-galactose solution. Two weeks after membrane formation began, the mice were grouped. Forty-eight mice were divided into four groups: control group, model group, example group (bird's nest peptide (SEQ ID NO:1), 20 mg / kg), and comparative group (bird's nest peptide with the sequence SEQ ID NO:3 synthesized according to the method in Example 3, 20 mg / kg). After grouping, drug administration began. Four weeks after drug administration, the mice were anesthetized and sacrificed. The heart, liver, and kidneys were harvested for the following tests.

[0089] (1) Determination of superoxide dismutase (SOD) activity, catalase (CAT) activity, glutathione peroxidase (GSH-Px) activity, and malondialdehyde (MDA) content.

[0090] Methods: A small amount of liver and kidney tissue was added to 9 times the volume of ice-cold physiological saline. The tissue pieces were cut into small pieces and poured into homogenization tubes. The tissues were centrifuged at 4500 rpm for 15 min in a refrigerated centrifuge. The supernatant was collected to determine the SOD activity, CAT activity, GSH-Px activity, and MDA content in each tissue homogenate (see [link to sample homogenate]). Figure 2 ).

[0091] Blood was collected from the abdominal aorta of mice and centrifuged at 3000 r / min and 4℃ for 10 min. The supernatant was used to detect SOD activity, CAT activity, GSH-Px activity, and MDA content in the serum (see [link to relevant documentation]). Figure 3 ).

[0092] GSH-Px can scavenge intracellular peroxides, protecting cells from free radical damage. SOD catalyzes the dismutation reaction of superoxide anions, playing a crucial role in biological antioxidant systems. CAT is the most important H2O2 scavenging enzyme, playing a vital role in reactive oxygen species scavenging systems. In vivo, free radicals act on lipids, causing peroxidation reactions, with the final oxidation product being MDA. This MDA can lead to cross-linking and polymerization of biomolecules such as proteins and nucleic acids, and is cytotoxic.

[0093] like Figure 2As shown, compared with the control group, the activities of SOD, CAT, and GSH-Px in the model group were significantly reduced, indicating that the activity of antioxidant-related enzymes in the anti-aging model mice was reduced, and the model was successfully constructed. Compared with the model group, the activities of SOD, CAT, and GSH-Px in the example group and the comparative group were significantly increased, and the effect of the example group was better than that of the comparative group, indicating that bird's nest peptide (SEQ ID NO:1) can significantly enhance the activity of antioxidant-related enzymes in aging mice and has an anti-aging effect. In the MDA experiment, compared with the control group, the MDA content in the model group was significantly increased, indicating that the activity of antioxidant-related enzymes in the anti-aging model mice was reduced, and the model was successfully constructed. Compared with the model group, the MDA content of bird's nest peptide (SEQ ID NO:1) was significantly reduced, indicating that bird's nest peptide (SEQ ID NO:1) can alleviate the cytotoxicity in aging mice.

[0094] like Figure 3 As shown, compared with the control group, the activities of SOD, CAT, and GSH-Px in the model group were significantly reduced (p<0.05), indicating that the activities of antioxidant-related enzymes in the anti-aging model mice were reduced, and the model was successfully constructed. Compared with the model group, the CAT activities in the example group and the comparative group were significantly increased, and the SOD activity in the example group was also significantly higher than that in the model group, and the SOD activity in the example group was significantly higher than that in the comparative group, indicating that bird's nest peptide (SEQ ID NO:1) has a higher antioxidant effect, significantly improves the activity of antioxidant-related enzymes in aging mice, and has an anti-aging effect. In the MDA experiment, compared with the model group, the MDA content in the example group was significantly reduced, indicating that bird's nest peptide (SEQ ID NO:1) can alleviate the cytotoxicity in aging mice.

[0095] (2) Determination of the content of lipofuscin and hydroxyproline in skin tissue.

[0096] Methods: A small amount of back skin was rapidly frozen and stored, and the skin tissue was homogenized. The contents of lipofuscin and hydroxyproline in the skin tissue homogenate were then detected.

[0097] Lipofuscin is a yellowish-brown granule composed of oxidized lipids and proteins, commonly found in aging cells. The accumulation of lipofuscin is one of the hallmarks of cellular aging and functional decline. Aging cells undergo prolonged metabolic activity and oxidative stress, leading to the accumulation of intracellular waste products such as lipofuscin.

[0098] like Figure 4As shown, compared with the control group, the lipofuscin content in the model group was significantly increased, indicating that the anti-aging mice in the D-galactose model group had a large number of cellular aging processes, leading to lipofuscin deposition, and the model was successfully constructed. Compared with the model group, the lipofuscin content in the example group and the comparative group was significantly reduced, indicating that bird's nest peptide (SEQ ID NO:1) can alleviate cellular aging and reduce lipofuscin deposition.

[0099] Hydroxyproline is one of the main components of collagen tissue. It is a unique amino acid in collagen, accounting for approximately 13% of the total amino acids in collagen. Hydroxyproline content is a sensitive biochemical indicator reflecting changes in collagen fibers. Measuring hydroxyproline levels can reveal the extent of collagen breakdown and metabolism in the body.

[0100] like Figure 4 As shown, compared with the control group, the hydroxyproline content in the skin of the model group mice was significantly decreased, indicating that collagen in the anti-aging mice in the D-galactose model group underwent degradation and loss, and the model was successfully constructed. Compared with the model group, the hydroxyproline content in the example group and the comparative group was significantly increased, and the hydroxyproline content in the example group was the highest, indicating that bird's nest peptide (SEQ ID NO:1) can promote the production of hydroxyproline in the skin of aging mice and promote collagen production, thus having an anti-aging effect.

[0101] (3) Expression of elastin (ELN), hyaluronidase 1 (HYAL-1) and hyaluronidase 2 (HYAL-2) mRNA in skin tissue.

[0102] Methods: A small amount of back skin was minced and homogenized. Total RNA was isolated from the skin sample using TRIzol reagent, and cDNA was synthesized using a reverse transcription kit. The mRNA expression levels of ELN, HYAL-1, and HYAL-2 in the skin tissue were detected by real-time polymerase chain reaction (RT-PCR).

[0103] Elastin is the main component of elastic fibers, which coexist with collagen fibers, giving tissues elasticity and tensile strength. A decrease in elastin is a major cause of skin aging, resulting in sagging, drooping, and fine wrinkles.

[0104] like Figure 5 As shown, compared with the control group, the mRNA expression of ELN in the model group was significantly reduced, indicating that the D-galactose-based anti-aging model mice experienced elastin loss, leading to decreased skin elasticity and thus aging. Compared with the model group, the mRNA expression of ELN in the example group and the comparative group was significantly increased, indicating that bird's nest peptide (SEQ ID NO:1) can increase the expression of the elastin gene (ELN) in the skin of aging mice.

[0105] Hyaluronidase is an enzyme that hydrolyzes hyaluronic acid. When hyaluronidase activity increases, it promotes the decomposition of hyaluronic acid, leading to moisture loss from the skin and the formation of fine lines and wrinkles.

[0106] like Figure 5 As shown, compared with the control group, the expression of HYAL-1 and HYAL-2 genes in the model group mice was significantly increased, indicating that the D-galactose-based anti-aging model mice showed increased expression of hyaluronidase, leading to the hydrolysis of hyaluronic acid and resulting in wrinkles. Compared with the model group, the expression levels of HYAL-1 and HYAL-2 in the example group and the comparative group were significantly decreased, indicating that bird's nest peptide (SEQ ID NO:1) can reduce the expression levels of hyaluronidase HYAL-1 and HYAL-2, thereby achieving an anti-aging effect.

[0107] The above description is merely an embodiment of the present invention and does not limit the patent scope of the present invention. Any equivalent structural transformations made based on the content of the present invention specification, or direct or indirect applications in other related technical fields, are similarly included within the patent protection scope of the present invention.

Claims

1. A bird's nest peptide with anti-aging function, characterized in that, The amino acid sequence of the bird's nest peptide is TFSLCEICETMVK.

2. A polypeptide mixture, characterized in that, The polypeptide mixture comprises the bird's nest peptide of claim 1.

3. The polypeptide mixture according to claim 2, characterized in that, The preparation process of the polypeptide mixture includes the following steps: (1) Grind the bird's nest into powder, transfer it to a container, and wash it with water; (2) Add simulated gastric juice to the bird's nest for biomimetic digestion, adjust the pH to neutral, and then add simulated intestinal juice for biomimetic digestion to obtain bird's nest biomimetic digestion liquid; (3) Add water to the biomimetic digestive fluid, keep it warm in a boiling water bath, cool it and centrifuge it to collect the supernatant; (4) The supernatant was subjected to alcohol precipitation, centrifugation, rotary evaporation and drying to obtain a polypeptide mixture.

4. A composition, characterized in that, The composition contains the bird's nest peptide of claim 1.

5. The composition according to claim 4, characterized in that, The composition also contains excipients permitted for use in cosmetics, pharmaceuticals, or animal feed.

6. The use of the bird's nest peptide of claim 1 or the polypeptide mixture of any one of claims 2-3 in the preparation of anti-aging products.

7. The application according to claim 6, characterized in that, The product in question is a cosmetic, pharmaceutical, or animal feed.

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