CN112812155B - Small peptide for promoting osteoblast proliferation - Google Patents

Small peptide for promoting osteoblast proliferation Download PDF

Info

Publication number
CN112812155B
CN112812155B CN202110170576.2A CN202110170576A CN112812155B CN 112812155 B CN112812155 B CN 112812155B CN 202110170576 A CN202110170576 A CN 202110170576A CN 112812155 B CN112812155 B CN 112812155B
Authority
CN
China
Prior art keywords
small peptide
promoting
proliferation
osteoblast proliferation
osteoblast
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Active
Application number
CN202110170576.2A
Other languages
Chinese (zh)
Other versions
CN112812155A (en
Inventor
沈新春
汪芳
宋海昭
李宇
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Nanjing University of Finance and Economics
Original Assignee
Nanjing University of Finance and Economics
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Nanjing University of Finance and Economics filed Critical Nanjing University of Finance and Economics
Priority to CN202110170576.2A priority Critical patent/CN112812155B/en
Publication of CN112812155A publication Critical patent/CN112812155A/en
Application granted granted Critical
Publication of CN112812155B publication Critical patent/CN112812155B/en
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
    • A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
    • 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

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Physical Education & Sports Medicine (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • Rheumatology (AREA)
  • Engineering & Computer Science (AREA)
  • Orthopedic Medicine & Surgery (AREA)
  • General Health & Medical Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Animal Behavior & Ethology (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • General Chemical & Material Sciences (AREA)
  • Molecular Biology (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • Food Science & Technology (AREA)
  • Mycology (AREA)
  • Genetics & Genomics (AREA)
  • Polymers & Plastics (AREA)
  • Peptides Or Proteins (AREA)
  • Nutrition Science (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)

Abstract

The invention provides a small peptide for promoting osteoblast proliferation, and belongs to the technical field of food processing. A small peptide with the activity of promoting the proliferation of osteoblast has an amino acid sequence shown in SEQ ID NO. 1. The small peptide is derived from soybean protein, has good safety, has remarkable effect of promoting osteoblast proliferation, can remarkably promote osteoblast differentiation, and is expected to be used for preparing medicaments or functional foods for promoting osteoblast proliferation and resisting osteoporosis. The small peptide is convenient to synthesize, can be industrially produced, and has good application prospect in the fields of food, medicine, cosmetics and the like.

Description

Small peptide for promoting osteoblast proliferation
Technical Field
The invention relates to a small peptide for promoting osteoblast proliferation, and belongs to the technical field of food processing.
Background
Osteoporosis is a metabolic disease characterized by reduced bone mass, decreased bone strength and toughness due to bone tissue degradation and microstructural destruction, and has a high incidence rate, and particularly with the advent of the aging age, osteoporosis and complications thereof such as fracture and the like increasingly become social problems endangering the health of the public.
The existing medicines for treating osteoporosis mainly act on bone absorption of osteoclasts, but the medicines for promoting bone formation by targeting osteoblast proliferation are few, and the existing anti-osteoporosis medicines on the market, such as bisphosphonates, selective estrogen receptor modulators, calcitonin and the like, have serious side effects. Therefore, the development of natural product components for resisting osteoporosis with high efficiency, safety and small side effect is increasingly concerned.
Disclosure of Invention
The invention aims to provide a small peptide with proliferative activity on osteoblasts.
The purpose of the invention is realized by adopting the following technical scheme:
a small peptide with proliferation promoting activity on osteoblasts has an amino acid sequence shown as SEQ ID NO. 1.
The invention also provides a modified peptide of the small peptide, which is used for modifying the small peptide in operation, and the N end, the C end or the middle residue of the small peptide is connected with amino acid, polypeptide, protein or PEG.
In the present invention, modifications to the small peptide include: formylating or acetylating the N-terminal of the small peptide, or connecting fatty acid, hydrazinonicotinamide, diethylenetriaminepentaacetic acid, myristic acid, palmitic acid or succinamide or PEG at the N-terminal; or the C end of the small peptide is amidated, or the C end is connected with p-nitroaniline or 7-amino-4-methylcoumarin; or glycosylation, phosphorylation, methylation, acetylation, nitration, sulfonation or PEG modification is carried out on the small peptide intermediate residue or the small peptide intermediate residue is coupled with protein.
The invention also provides application of the small peptide in preparing products for promoting osteoblast proliferation and resisting osteoporosis.
The invention also provides application of the small peptide in preparing a medicament for promoting osteoblast proliferation and resisting osteoporosis.
The invention also provides a food of the small peptide, which has the functions of promoting osteoblast proliferation and resisting osteoporosis.
Has the advantages that: the small peptide A is derived from soybean protein, has good safety, has obvious effect of promoting osteoblast proliferation, can obviously promote osteoblast differentiation, and is expected to be used for preparing medicaments or functional foods for promoting osteoblast proliferation and resisting osteoporosis. The small peptide is convenient to synthesize, can be industrially produced, and has good application prospect in the fields of food, medicine, cosmetics and the like.
Drawings
FIG. 1 Effect of papain enzyme concentration on osteoblast proliferation activity, the abscissa is the concentration of papain enzyme solution. * The difference was significant compared to the control group (P < 0.05), and the difference was very significant compared to the control group (P < 0.01), as follows.
FIG. 2 Effect of the components of the ultrafiltration product on the proliferative activity of osteoblasts. Different letters indicate significant differences (P < 0.05). The same applies below.
FIG. 3Sephadex G-15 separation chromatogram.
Figure 4 bone cell proliferation-promoting activity of each active component.
Fig. 5 effect of small peptide a on osteoblast proliferation viability, wherein 10, 25, 50 and 100 represent intervention concentrations of small peptide a in μ M.
Fig. 6 shows the effect of small peptide a on osteoblast ALP (alkaline phosphatase) viability, damdggwfrl being a well to which small peptide a was added. D7 and D10 represent the culture period of the small peptide A before intervention for 7 and 10 days, respectively.
Detailed Description
Test materials: soy protein isolate, shanghai source leaf biotechnology limited; dimethyl sulfoxide (DMSO), sigma, usa; thiazole blue (MTT), papain, beijing solibao science and technology ltd; MC3T3-E1 cell line, shanghai medusa house of cells; fetal Bovine Serum (FBS), α -MEM medium, EDTA-pancreatin (0.05%), penicilin-Streptomycin (100 ×), PBS phosphate buffer, gibco, usa; alkaline phosphatase Alcalase 2.4L, novoversson Biotechnology Ltd, denmark; sephadex G-15, GE (China) medical group; other reagents are all made in China and are purchased from chemical reagents of national drug group, inc.
Instruments and equipment: spectraMax M2e microplate reader, molecular Devices, USA; protein purification System, shanghai analytical instruments Limited; model 8400 ultrafiltration cups, millipore, USA; HY-1 vortex mixer, shanghai apparatus, electrosciences instruments, inc.; micro vertical electrophoresis system, chemiluminescence gel imaging system, bio-rad, usa; a freeze dryer, labconco, USA; JY 92-II ultrasonic cell crusher, ningbo New technology ultrasonic Equipment Co.
Determination of proliferative Activity of osteoblasts:
(1) Setting a sample adding group: osteoblasts (MC 3T 3-E1) were digested and collected and then prepared to contain 5X 10 cells/ml 4 The suspension of each cell was added to 100. Mu.L of the suspension in each well of a 96-well plate, and the mixture was left at 37 ℃ under CO 2 The cells are attached to the wall after 24h of culture in an incubator. And removing the culture solution after the cells adhere to the wall, adding 100 mu L of samples to be detected into each hole, and setting 6 parallel samples to be detected. Exposing the cells to CO 2 After further culturing in the incubator for 24 hours, 10. Mu.L of5 mg/mL solution was added to each well -1 After continuously culturing for 4 hours, the MTT solution and the culture solution are sucked out, 50 microliter DMSO is added, and then the MTT solution and the culture solution are vibrated for 20 minutes in a constant temperature oscillator at 37 ℃ and then the light absorption value is measured by using an enzyme-linked immunosorbent assay (ELISA) reader at a single wavelength of 570 nm.
(2) In addition, a blank group and a control group were set. The control group replaces the sample to be detected with the same volume of alpha-MEM culture solution, and the other groups are the same. Blank control group 100. Mu.L of PBS buffer per well in CO 2 After 48 hours of incubation in an incubator, 10. Mu.L of5 mg/mL solution was added to each well -1 After further culturing for 4 hours, the MTT solution and PBS buffer solution are sucked out and 50. Mu.L of DMSO is added, and then the solution is vibrated in a constant temperature oscillator at 37 ℃ for 20min, and then the absorbance is measured at a single wavelength of 570nm by using an enzyme-linked immunosorbent assay.
(3) Osteoblast proliferation activity = (OD) Sample adding group -OD Blank group )/(OD Control group -OD Blank group )×100％。
Detailed Description
Example 1 method for preparing active peptide that promotes osteoblast proliferation
A method for preparing an active peptide for promoting osteoblast proliferation, comprising the steps of:
(1) Enzymolysis of papain
Weighing soybean protein isolate (Shanghai-derived leaf Biotechnology Co., ltd., product No. S30914), dissolving in ultrapure water to obtain a protein solution with a mass percentage concentration of 4.5%, adding NaOH solution, and adjusting pH to 7.0. Adding papain into protein solution according to the proportion of adding 3000U papain into each gram of protein, placing on a rotary mixing machine, performing enzymolysis reaction at 55 deg.C for 5h, and detecting that the hydrolysis degree of the soybean protein isolate is 11.08 + -0.31%. After the reaction is finished, heating to 85 ℃, keeping the temperature for 20min to inactivate the papain, cooling to room temperature, centrifuging for 15min under the condition of 3000 Xg, taking supernatant, dialyzing to remove salt, freeze-drying to obtain a papain enzymolysis product, and storing at-20 ℃.
The papain enzymolysis product is prepared into 50, 100, 150, 200 and 250 mu g/mL by adopting alpha-MEM culture solution -1 The solution of (1). According to the method for measuring the proliferation activity of osteoblasts, papain enzymolysis product solutions with different concentrations are used as samples to be detected, and the proliferation activity of osteoblasts after intervention of each sample is detected. As shown in FIG. 1, the concentration of the papain enzymolysis product solution was 100. Mu.g.mL -1 And 150. Mu.g.mL -1 Then, the osteoblast proliferation activity was enhanced as compared with that of the control group (P)<0.05 When the concentration is 200. Mu.g.mL) -1 And 250. Mu.g.mL -1 The time phase has very significant difference (P) compared with the control group<0.01 But no significant difference (P) between the two doses>0.05). When the concentration of the papain enzymolysis product solution is 200 mug.mL -1 Then, the osteoblast proliferation activity was 118.24 ± 2.73%.
(2) Ultra-filtration membrane separation
Dissolving the papain enzymolysis product obtained in the step (1) in deionized water to prepare 10 mu g/mL -1 The solution of (4) was filtered through a 0.45-. Mu.m cellulose membrane to remove insoluble substances. Separating the filtrate by adopting a 10kDa ultrafiltration membrane to respectively obtain a trapped fluid A and a permeate A. And separating the trapped fluid A by adopting a 30kDa ultrafiltration membrane to obtain trapped fluid B and permeate B. The conditions of ultrafiltration were: the temperature was 4 ℃ and the pressure was 0.2MPa. Respectively freeze-drying the permeate A (containing less than 10kDa component), the retentate B (containing greater than 30kDa component) and the permeate B (containing 10-30kDa component) to obtain less than 10kDa component, greater than 30kDa component and 10-30kDa component.
Respectively preparing the components with less than 10kDa, more than 30kDa and 10-30kDa into 200 μ g/mL with alpha-MEM culture solution -1 The solution of (1) is used as a sample to be tested, and the osteoblast proliferation activity is detected according to the osteoblast proliferation activity measuring method. The results are shown in FIG. 2. Compared with the control group, the component with the molecular weight of more than 30kDa has no obvious proliferation promoting effect on osteoblast (P)>0.05 10-30kDa component and less than 10kDa component have remarkable proliferation promoting effect, wherein the less than 10kDa component has high proliferation promoting activity, and the osteoblast proliferation activity reaches 120.45 +/-2.28 percent, and has significant difference (P) with other groups<0.05). Therefore, the smaller the molecular weight of the papain enzymolysis product is, the higher it contributes to the proliferative activity of bone cells. Thus, permeate a (less than 10kDa fraction) was selected for subsequent enzymatic hydrolysis experiments.
(3) Enzymolysis with alkaline protease
Dissolving the component less than 10kDa obtained in the step (2) in ultrapure water to prepare a protein solution with the mass percentage concentration of 5%, then adjusting the pH to 8.0 by using a NaOH solution, adding 3000U of alkaline protease (Denmark Novicin biotechnology, co., ltd.) into each gram of protein, carrying out enzymolysis for 0.5h at 55 ℃, heating to 85 ℃, keeping the temperature for 20min to inactivate the alkaline protease, cooling to room temperature, centrifuging for 15min at 3000 Xg, taking supernatant, dialyzing to remove salt, freeze-drying to obtain an alkaline protease enzymolysis product, and storing at-20 ℃.
Preparing alkaline protease enzymolysis product into 200 mug/mL culture solution by adopting alpha-MEM (membrane-organic Membrane) culture solution -1 The solution of (1) is used as a sample to be tested, and the osteoblast proliferation activity is measured according to a method for measuring the osteoblast proliferation activity. As a result: the proliferation activity of the alkaline protease enzymolysis product on osteoblasts reaches 123.02 +/-2.69%.
(4) Sephadex G-15 separation
And (4) separating the alkaline protease enzymolysis product obtained in the step (3) by using Sephadex G-15. Firstly, swelling Sephadex G-15 dry powder, then loading the powder into a chromatographic column with the diameter of 15mm multiplied by 600mm, dissolving an alkaline protease enzymolysis product in ultrapure water to prepare a solution with the concentration of 2 percent (mass percentage concentration), filtering the solution by a filter membrane with the diameter of 0.22 mu m to remove particles, wherein the loading amount is 3 percent of the volume of the column, and the separation process is carried out at the temperature of 4 ℃. Using ultrapure water at a flow rate of 0.6 mL/min -1 Eluting at flow rate, detecting light absorption value at 220nm with ultraviolet detector, collecting 1 tube (about 2 mL) of eluate every 5min with automatic collector, and recording ultraviolet detection result with recorder. According to the recorded curve, the eluates at the same elution peak are combined and freeze-dried.
As shown in FIG. 3, after Sephadex G-15 separation, 4 elution peaks were obtained, which were respectively named as active component F1 (retention time 40-55 min)F2 (retention time of 70-90 min), F3 (retention time of 95-115 min) and F4 (retention time of 115-130 min). F1, F2, F3 and F4 were each freeze-dried and prepared to 200. Mu.g/mL using α -MEM -1 The solution of (1) is used as a sample to be tested, and the osteoblast proliferation activity is detected according to the osteoblast proliferation activity measuring method. As a result, as shown in FIG. 4, F1, F2, F3 and F4 all had a proliferative activity on osteoblasts (P) as compared with the control group<0.05 Wherein the osteoblast proliferation activity is up to 125.80 +/-2.94% after F3 intervention.
(5) Analysis of amino acid content and structural identification of peptides and their effect on osteoblast proliferation viability
And (4) carrying out amino acid analysis on the active component F3 obtained in the step (4), and determining the amino acid content by referring to GB 5009.124-2016. 0.2g of active ingredient F3 was weighed into a hydrolysis tube, and 10mL of 6mol.L was added -1 The tube is sealed after hydrochloric acid is obtained, the tube is hydrolyzed in a baking oven at 110 ℃ for 24 hours, and then the content of amino acid in a sample is determined by using a sulfonic acid type cationic resin column by using a full-automatic amino acid analyzer.
And trusting Shanghai flatstem milkvetch Biotechnology limited to complete the structural identification of the small peptide in the active component F3. And (3) carrying out structural identification on the active component F3 by adopting a tandem mass spectrometry technology (ESI-TOF MS/MS). Mobile phase A: an aqueous solution containing 2% (by volume) acetonitrile and 0.1% (by volume) formic acid; and (3) mobile phase B: acetonitrile, formic acid and water in a volume ratio of 98:0.1:1.9 the solvent. The mass spectrum was obtained using a TripleTOF5600 system (AB SCIEX) in combination with a nanoliter spray III ion source at a spray voltage of 2.5kV, an atomization pressure of 5PSI, an air curtain pressure of 30PSI, and a heater temperature of 150 ℃.
Small peptide a is present in active component F3. The sequence of the small peptide A (SEQ ID NO: 1) is: DAMDGWFRL. The small peptide A (with the purity of more than 95 percent) is synthesized by a chemical method in a solid phase, and the experiment is finished by Jiangsu Kinshi Biotechnology Co., ltd.
The small peptide A prepared by a chemical solid-phase synthesis method is prepared into 10, 25, 50 and 100 mu M solutions respectively by adopting alpha-MEM culture solution and is used as a sample to be detected, and the proliferation activity of osteoblasts is detected according to a method for determining the proliferation activity of osteoblasts so as to investigate whether the small peptide A has the effect of promoting the proliferation of the osteoblasts. The detection result is shown in fig. 5, the proliferation activity of osteoblasts is gradually increased along with the increase of the concentration of the small peptide a, and when the concentration is 100 μ M, the proliferation activity of osteoblasts by the small peptide a reaches 127.98 ± 3.06%, so that the small peptide a has a remarkable effect of promoting the proliferation of osteoblasts.
Example 7 Effect of Small peptide A on osteoblast ALP (alkaline phosphatase) Activity
The effect of small peptide a on osteoblast ALP viability was examined using the alkaline phosphatase kit. The specific method comprises the following steps: osteoblasts MC3T3-E1 were digested and then prepared in alpha-MEM medium at a concentration of 1X 10 5 Cell suspension per mL, seeded in 6-well plates, 2mL per well. After the MC3T3-E1 cells were grown to confluence, the medium was removed, cultured in a mineralization induction medium (ODM from Sigma, USA supplemented with ascorbic acid at a final concentration of 50. Mu.g/mL and 4 mM. Beta. -glycerophosphate) for 7 to 10 days for induction and differentiation, and then the serum-free medium was replaced while small peptide A at a final concentration of 20. Mu.M was added for treatment for 48h, 3 replicates were set. Meanwhile, a control group is set, and small peptide A is not intervened, and the others are not changed. ALP viability was determined according to the alkaline phosphatase kit instructions; the BCA method was used to detect the total protein content in the cells and to correct ALP activity. As shown in FIG. 6, the activity of ALP was 13.68. + -. 0.30U/g in the control group and 26.02. + -. 1.28U/g in the well to which the small peptide A was added at the differentiation time of 7 days; the activity of ALP in the control group was 19.45. + -. 1.30U/g and the activity of ALP in the well to which the small peptide A was added was 54.64. + -. 2.48U/g at 10 days of differentiation. The experimental results show that the ALP activity of osteoblasts interfered by small peptide A is obviously higher than that of a control group (P) on the 7 th day and the 10 th day of differentiation<0.05 Shows that the small peptide A can obviously promote the differentiation of osteoblast.
SEQUENCE LISTING
<110> university of financial institution of Nanjing
<120> a small peptide for promoting osteoblast proliferation
<130> 202102071
<160> 1
<170> PatentIn version 3.3
<210> 1
<211> 9
<212> PRT
<213> Soybean
<400> 1
Asp Ala Met Asp Gly Trp Phe Arg Leu
1 5

Claims (4)

1. A small peptide for promoting osteoblast proliferation has an amino acid sequence shown as SEQ ID NO. 1.
2. Use of the small peptide according to claim 1 for the preparation of a product for promoting osteoblast proliferation and anti-osteoporosis.
3. Use of the small peptide of claim 1 for the preparation of a medicament for promoting osteoblast proliferation and anti-osteoporosis.
4. A pharmaceutical agent having an osteoblast proliferation promoting effect, which contains the small peptide according to claim 1.
CN202110170576.2A 2021-02-08 2021-02-08 Small peptide for promoting osteoblast proliferation Active CN112812155B (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN202110170576.2A CN112812155B (en) 2021-02-08 2021-02-08 Small peptide for promoting osteoblast proliferation

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN202110170576.2A CN112812155B (en) 2021-02-08 2021-02-08 Small peptide for promoting osteoblast proliferation

Publications (2)

Publication Number Publication Date
CN112812155A CN112812155A (en) 2021-05-18
CN112812155B true CN112812155B (en) 2023-01-06

Family

ID=75863708

Family Applications (1)

Application Number Title Priority Date Filing Date
CN202110170576.2A Active CN112812155B (en) 2021-02-08 2021-02-08 Small peptide for promoting osteoblast proliferation

Country Status (1)

Country Link
CN (1) CN112812155B (en)

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN114480264B (en) * 2022-03-03 2024-01-30 烟台大学 Application of soybean peptide in promotion of osteogenesis activity
CN116082454B (en) * 2022-09-09 2024-07-09 大连工业大学 Polypeptide with bone mineral density regulating activity and application thereof

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN107375261A (en) * 2017-06-27 2017-11-24 东北林业大学 Application of the pinostrobin in osteoporosis is prevented and treated
CN110627897A (en) * 2019-10-12 2019-12-31 中国科学院理化技术研究所 Active peptide for promoting osteoblast proliferation and application thereof

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN107375261A (en) * 2017-06-27 2017-11-24 东北林业大学 Application of the pinostrobin in osteoporosis is prevented and treated
CN110627897A (en) * 2019-10-12 2019-12-31 中国科学院理化技术研究所 Active peptide for promoting osteoblast proliferation and application thereof

Also Published As

Publication number Publication date
CN112812155A (en) 2021-05-18

Similar Documents

Publication Publication Date Title
CN112940093B (en) Small peptide for promoting osteoblast proliferation
CN112812155B (en) Small peptide for promoting osteoblast proliferation
US11673925B2 (en) Oligopeptide with anti-inflammatory activity, preparation method, and application thereof
US20180258147A1 (en) Pearl protein preparation method and a water-soluble pearl protein and acid-soluble pearl protein obtained by adopting this method
CN116063386B (en) Deer antler plate immunocompetent peptide, and preparation method and application thereof
CN115785201A (en) Pea antioxidant peptide and preparation method and application thereof
CN113321705B (en) Elastase inhibitory peptide and preparation method and application thereof
CN101570565A (en) Functional component prepared from earthworms for promoting growth of microorganisms and improving culture units and preparation method thereof
CN114032267A (en) Preparation method and application of active peptide
CN115819504B (en) Sturgeon functional polypeptide and application thereof
CN116240256A (en) Ginseng glycopeptide and preparation process thereof
CN111825745B (en) Immunoregulatory active heptapeptide and preparation method and application thereof
JP7103702B2 (en) A polypeptide that suppresses the growth of leukemia cells
CN115947778B (en) Small peptide with lipid-lowering activity, preparation method and application thereof
CN111848735B (en) Immunoregulation active peptide and preparation method and application thereof
CN111978374B (en) Immunoregulation active hexapeptide and preparation method and application thereof
CN117069798B (en) Quinoa small peptide with anti-inflammatory activity and preparation method and application thereof
CN117700484B (en) High F value corn peptide and corn oligopeptide composition, and preparation method and application thereof
KR20130031194A (en) The obtaining method of hydrolysate from silkworm gland
CN115974967B (en) Oligopeptide POP1, and preparation method and application thereof
CN117624328B (en) Sheep placenta polypeptide with high antioxidant activity and preparation method and application thereof
CN118344436A (en) Sturgeon active peptide with alpha-glucosidase inhibitory activity and insulin resistance improving function and application thereof
CN116804042A (en) Polypeptide, composition and application thereof
CN116063376A (en) Polypeptide with blood pressure reducing function and preparation method thereof
CN115947781A (en) Fermented wheat antihypertensive peptide, preparation method thereof, antihypertensive peptide combination and application

Legal Events

Date Code Title Description
PB01 Publication
PB01 Publication
SE01 Entry into force of request for substantive examination
SE01 Entry into force of request for substantive examination
GR01 Patent grant
GR01 Patent grant