CN102772822A - Application of collagen matrix as tissue engineering scaffold - Google Patents
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- CN102772822A CN102772822A CN2011101196364A CN201110119636A CN102772822A CN 102772822 A CN102772822 A CN 102772822A CN 2011101196364 A CN2011101196364 A CN 2011101196364A CN 201110119636 A CN201110119636 A CN 201110119636A CN 102772822 A CN102772822 A CN 102772822A
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Abstract
The invention discloses novel application of a collagen matrix as a tissue engineering scaffold. The collagen matrix comprises the following substances expressed in mass parts: 50 to 90 of collagen, 8 to 48 of chitosan and 0.5 to 5 of glycerin. A preparation method for the collagen matrix comprises the following steps: 1) dissolving collagen in an acetic acid aqueous solution with a concentration of 0.01 to 0.1% to prepare a collagen solution with a concentration of 1 to 3%; 2) dissolving chitosan in the acetic acid aqueous solution with a concentration of 0.01 to 0.1% to prepare a chitosan solution with a concentration of 1 to 3%; 3) mixing the collagen solution, the chitosan solution (in terms of dry weight) and glycerin according to a mass ratio of 50-90: 8-48: 0.5-5 and carrying out freeze drying at a temperature of -80 DEG C to -10 DEG C for 1 to 5 d so as to obtain a spongy material; 4) immobilizing the spongy material with an aldehyde cross-linking agent at a temperature of 40 to 50 DEG C for 20 to 100 min; and 5) rinsing the spongy material with an aqueous solution of glycerin and drying the spongy material in vacuum so as to obtain the collagen matrix. According to results of cell culture experiments, the collagen matrix provided by the invention can promote cell growth and can be used as a tissue engineering scaffold.
Description
Technical field
The present invention relates to the application of collagen stroma as tissue engineering bracket material.
Background technology
Collagen is the rich in protein of mammal content, and its three-dimensional spiral structure is made up of three polypeptide chains, and the repetitive of polypeptide chain is Gly-X-Y, and X and Y position are generally proline and 4-hydroxyproline.Collagen is prone to from animal tissue's purification, like people's tissue of skin, tendon and abandonment like Placenta Hominis.Collagen have antigenicity low, big with the cell affinity, produce characteristics such as hemagglutinative function with platelet, thereby be widely used at field of medicaments.Have been found that at least 27 kinds of collagen-types that gene are different at present.With the maximum type i collagen of amount is example, and about 95% of tropocollagen molecule is three coiled strand fields, and remaining about 5% is the peptide chain structure field, terminal of non-collagen property.The antigenicity of collagen is low, mainly is because three coiled strand fields of collagen lack tyrosine residue, the outer main peptide chain from collagen N and C terminal of the antigenicity removal of impurity of collagen product in the market.
With collagen is the research and development of the curable product on basis; Having obtained a lot of achievements, mainly is that collagen is made different dosage form, like solution, gel, powder, sponge, fiber, thin film etc.; Or carry out various modifications, make it have different medical or medical functions.As tissue engineering bracket material, but the differentiation of collagen cell guiding, propagation and migration.But the sponge of using collagen to process is separately caused poor mechanical property and degrades too fast as timbering material.
Summary of the invention
The new purposes that the purpose of this invention is to provide collagen stroma.
The new purposes of collagen stroma provided by the present invention is its application in the preparation tissue engineering bracket material; Especially as the timbering material of growths such as epidermis cell, fibroblast, vascular endothelial cell and osteocyte, be used as the reconstruction of tissues such as skin, bone and blood vessel.
Collagen stroma according to the invention is made up of the material of following ratio of quality and the number of copies:
Collagen 50-90
Chitosan 8-48
Glycerol 0.5-5.
Said collagen stroma can further be made up of the material of following ratio of quality and the number of copies:
Collagen 70-80
Chitosan 18-28
Glycerol 0.8-8.
Said collagen can be commercially available collagen primary product (mainly being type i collagens), also can be to adopt following method preparation:
Animal tissue's machinery that 1) will be rich in collagen is removed impurity such as epidermal area, muscle and fat, cleans up after the pulverizing, obtains collagen tissue;
2) above-mentioned collagen tissue is used aqueous slkali, the defat of alcohols material solution washing of pH8.5-10.5 respectively, obtained the collagen bullion; The aqueous slkali that said aqueous slkali preferably is made up of sodium hydroxide, sodium bicarbonate and water, wherein, the mass ratio of sodium hydroxide, sodium bicarbonate and water is followed successively by (0.1-1): (5-10): (89-94.9); The mixed solvent that said alcohols material aqueous solution preferably is made up of ethanol, isopropyl alcohol and water, wherein the mass ratio of ethanol, isopropyl alcohol and water is followed successively by (5-10): (2-5): (85-93);
3) with the collagen dissolving crude product in the acid solution of pH5.5-6.5; Wherein acid solution preferable formic acid, acetic acid, propanoic acid or hydrochloric acid;
4) in above-mentioned solution, add compound protease, 30-35 ℃ following stir culture 10-15 hour; Said compound protease by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed; The proportioning of said collagen bullion and compound protease is (100-1000) g: 10000U;
5) centrifugal collection supernatant adds NaCl in supernatant, makes its concentration reach 2mol/L, and 0-10 ℃ was stirred 10-20 hour down, collected the precipitate that obtains, and was designated as precipitate 1;
6) precipitate 1 is dissolved in the mass concentration 0.1-0.5% acetic acid aqueous solution centrifugal collection supernatant; In supernatant, add NaCl again, make its concentration reach 1mol/L, stir and obtain precipitate 2; Repetitive operation 3-4 time obtains the purpose product.
For the character that makes the collagen stroma that obtains is more good, also can adopt following method to make with extra care to commercially available collagen primary product:
1) commercially available collagen primary product is dissolved in the dilute acid soln of pH5.5-6.5, wherein preferable formic acid, acetic acid, propanoic acid or hydrochloric acid;
2) in above-mentioned solution, add compound protease, 30-35 ℃ following stir culture 10-15 hour; Said compound protease by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed; The proportioning of said collagen bullion and compound protease is (100-1000) g: 10000U;
3) centrifugal collection supernatant adds NaCl in supernatant, makes its concentration reach 2mol/L, and 0-10 ℃ was stirred 10-20 hour down, collected the precipitate that obtains, and was designated as precipitate a;
4) precipitate a being dissolved in mass concentration is in the 0.1-0.5% acetic acid aqueous solution, centrifugal collection supernatant; In supernatant, add NaCl again, make concentration reach 1mol/L, stir and obtain precipitate b; Repetitive operation 3-4 time obtains the purpose product.
More excellent for the quality that makes collagen stroma, said chitosan selects that to take off the hexanoyl degree be 70-90% for use, and viscosity-average molecular weight is (1.0-4.0) * 10
5Chitosan.
The method for preparing of collagen stroma according to the invention comprises the steps:
1) collagen being dissolved in mass concentration is in the 0.01-0.1% acetic acid aqueous solution, and processing mass concentration is the 1-3% collagen solution;
2) chitosan being dissolved in mass concentration is in the 0.01-0.1% acetic acid solution, and processing mass concentration is the 1-3% chitosan solution;
3) be (50-90) with said collagen solution, chitosan solution and glycerol according to the mass ratio of collagen, chitosan and glycerol: (8-48): mixed (0.5-5) is even, at-80 ℃--10 ℃ following lyophilization 1-5 days, obtain spongy material;
4) above-mentioned spongy material was adopted the aldehydes cross-linking agent fixedly 20-100 minute down at 40-50 ℃;
5) with after the glycerine water solution cleaning, vacuum drying obtains collagen stroma.
In process of production, said chitosan selects that to take off the hexanoyl degree be 70-90% for use, and viscosity-average molecular weight is (1.0-4.0) * 10
5Product for well.Adopt in the step 4) aldehydes cross-linking agent fixedly spongy material in gas generator, carry out.Said aldehydes cross-linking agent can be formaldehyde, methyl-glyoxal or glutaraldehyde.
In the used glycerine water solution cleaning step, the mass ratio of glycerol and water is (0.1-10) in the glycerine water solution: (90-99.9) in the step 5).
Further, the collagen stroma that step 5) is obtained through packing,
60Process finished product behind the Co radiation sterilization.
The present invention unites utilization with collagen, chitosan and glycerol dexterously, and the collagen stroma performance of products is obviously strengthened.Sneaking into of chitosan not only increases the collagen stroma mechanical property, and makes the degradation rate of collagen stroma controlled.Aldehydes cross-linking agent such as glutaraldehyde crosslinked makes collagen stroma have stronger biological and chemical stability.The processing of glycerol, the suppleness of raising collagen stroma helps the behavior of inoculating cell developmental biology.
The ungrease treatment of diluted alkaline and alcohols material aqueous solution makes the fat content of collagen stroma reduce to minimum.Seeing that collagen product antigenicity mainly from the N and the C terminal peptide chain of collagen, is handled collagen with compound enzyme to the invention property, further cut away the terminal peptide chain, make the antigenicity of product reduce to minimum.
In gas generator, material is carried out crosslinked fixing, can avoid the impurity (like half chemical compound of the ring in the glutaraldehyde solution) in the cross-linking agent solution to introduce in the material, thereby make biology performance of the present invention excellent.
Through glutaraldehyde and the abundant Chemical Modifications of Chitosan in source, optimize the performance of collagen stroma, the analog cell epimatrix is used for tissue or cell culture.The cell growth test shows human vascular endothelial well-grown on collagen stroma of the present invention.
Description of drawings
Fig. 1 is the enzymolysis rate diagram of type i collagen and collagen stroma of the present invention; Wherein, A is a type i collagen, and B is a collagen stroma; A, enzymolysis 1h; B, enzymolysis 1.5h; C, enzymolysis 4h; D, enzymolysis 1d; E, enzymolysis 2d; F, enzymolysis 3d; G, enzymolysis 6d; H, enzymolysis 9d.
Fig. 2 is the laser scanning co-focusing figure that human vascular endothelial and collagen stroma are cultivated altogether.
The specific embodiment
Describe of the present invention through specific embodiment below, but the present invention is not limited thereto.
Experimental technique described in the following embodiment like no specified otherwise, is conventional method; Said reagent and biomaterial like no specified otherwise, all can obtain from commercial sources.
Compound protease used among the following embodiment by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed; The enzyme of compound protease is lived and is 10000U/g.
Embodiment 1, preparation collagen stroma
(1) produce collagen with the original structure of animal, concrete steps are following:
1, will be rich in the in vitro tissue (Corii Sus domestica, Corii Bovis seu Bubali, heel string etc.) of collagen, machinery is removed impurity such as epidermal area, muscle and fat, cleans with tap water and pure water respectively after the pulverizing, obtains collagen tissue;
Water=0.5: 7.5: 92) and alcohols material aqueous solution (ratio of quality and the number of copies, ethanol: isopropyl alcohol: water=7: 4: 89) 2, the dilute alkaline soln of preparation pH9.5 (ratio of quality and the number of copies, sodium hydroxide: sodium bicarbonate:;
3, use the dilute alkaline soln and the resulting animal tissue of the alcohols material solution washing first step of above-mentioned preparation successively, make its defat, obtain the collagen bullion;
4, with the collagen dissolving crude product in the dilute formic acid solution of pH6.0;
5, in above-mentioned solution, add compound protease, the mass ratio of collagen bullion and compound protease is 800: 1,33 ℃ of following stir culture 13 hours;
6, centrifugal, and collect supernatant, in supernatant, add NaCl, make concentration reach 2mol/L, 5 ℃ were stirred 15 hours down, collect the precipitate that obtains;
7, precipitate being dissolved in mass concentration is in 0.3% acetic acid aqueous solution, centrifugal collection supernatant; Add NaCl in the supernatant again, make concentration reach 1mol/L, stir and obtain precipitate; Repetitive operation 3 times, the collecting precipitation thing is collagen;
(2) preparation collagen stroma
1, collagen being dissolved in mass concentration is in 0.05% acetic acid aqueous solution, and processing mass concentration is 2% collagen solution;
2, will take off hexanoyl degree 80%, viscosity-average molecular weight 3.0 * 10
5Chitosan to be dissolved in mass concentration be in 0.05% acetic acid aqueous solution, processing mass concentration is 2% chitosan solution;
3, the above-mentioned collagen solution that obtains (with the collagen dry weight basis in the solution) and chitosan solution (with the chitosan dry weight basis in the solution) and glycerol are pressed 70: 28: 2 mixed of ratio of quality and the number of copies ,-70 ℃ freezing 2 days down, lyophilizing obtains spongy material;
4, above-mentioned spongy material is placed gas generator, 45 ℃ down with fixing 60 minutes of formaldehyde crosslinking agent;
5, clean with glycerine water solution, glycerol is 1: 99 with the quality ratio in the glycerine water solution;
6, vacuum drying obtains collagen stroma;
7, collagen stroma through the packing,
60Put in storage behind the Co radiation sterilization.
Embodiment 2, preparation collagen stroma
(1) refining commercially available collagen, concrete steps are following:
1, with commercially available collagenolysis in the dilute hydrochloric acid solution of pH5.8;
2, in above-mentioned solution, add compound protease; The weight ratio of collagen and compound protease is 500: 1; Compound protease by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed, 34 ℃ of following stir culture 11 hours;
3, centrifugal, and collect supernatant, in supernatant, add NaCl, make concentration reach 2mol/L, 8 ℃ were stirred 12 hours down, collect the precipitate that obtains;
4, precipitate being dissolved in mass concentration is in 0.3% acetic acid aqueous solution, centrifugal collection supernatant;
5, add NaCl in the supernatant again, make concentration reach 1mol/L, stir and obtain precipitate; Repetitive operation 4 times, the collecting precipitation thing is purified collagen.
(2) preparation collagen stroma
1, will making with extra care collagen, to be dissolved in mass concentration be in 0.08% acetic acid solution, and processing mass concentration is 1.8% collagen solution;
2, with the commercially available hexanoyl degree 75% that takes off, viscosity-average molecular weight 2.0 * 10
5Chitosan to be dissolved in mass concentration be in 0.08% acetic acid solution, processing mass concentration is 1.8% chitosan solution;
3, the above-mentioned collagen solution that obtains (with the collagen dry weight basis in the solution) and chitosan solution (with the chitosan dry weight basis in the solution) and 80: 18: 4 by ratio of weight and the number of copies mixed of glycerol is even; Descended freezing 4 days at-30 ℃, lyophilizing obtains spongy material;
4, above-mentioned spongy material is placed gas generator, 48 ℃ down with fixing 30 minutes of glutaraldehyde cross-linking agent;
5, clean with glycerine water solution, glycerol is 7: 93 with the quality ratio in the glycerine water solution;
6, vacuum drying obtains collagen stroma;
7, collagen stroma through the packing,
60Put in storage behind the Co radiation sterilization.
The enzymolysis stability of embodiment 3, collagen stroma
Through collagen stroma enzymatic degradation measuring enzymolysis speed.
Concrete grammar is following: getting fresh DMEM culture fluid compound concentration is the collagenase solution of 5CDU/ml, stored refrigerated; Get 5mg collagen stroma sample, the plastic sheeting encapsulation
60C
0Sterilization treatment; Sample is inserted in the 1ml type i collagen enzymatic solution, cultivate down, change collagenase solution every day for 37 ℃; At 1h, 1.5h, 4h, 1d, 2d, 3d, 6d, 9d point in time sampling, every group of 3 samples; In the solution of sampling regularly, add 200 μ l 0.25mol/L EDTA solution to stop digestion process; Take out sample with tweezers folder sample one little angle, clean with phosphate buffer (pH7.2) earlier, the reuse deionized water cleans, and places in the clean tubule, more than-20 ℃ of frozen 24h; Sample lyophilization 36h takes by weighing remaining sample quality (above agents useful for same is all available from SIGMA company).
Mensuration result is as shown in Figure 1.The collagen stroma of being processed by type i collagen is almost completely degraded in 1.5h-2h, and the collagen stroma (embodiment 1 preparation) that makes through this method, enzymolysis stability significantly improves.Type i collagen major part when 2h is degraded, has only little broken cotton-shaped floating in the solution, finds into thick fuzzy thing during taking-up, and after vacuum lyophilization, can be observed collagenous fiber bundle and expose, and different in size, the three-dimensional porous structure of substrate does not thoroughly exist.Collagen stroma of the present invention its structure when 2h keeps good, and the no fibre bundle in surface exposes.When 9d, its three-dimensional porous structure and material surface do not have significant change yet.
The cell growth test of embodiment 4, collagen stroma
Human vascular endothelial (HUVECs) is inoculated on the collagen stroma of the present invention preparation and cultivated for 2 weeks altogether; After FDA (fluorescein(e) diacetate) dyeing; Living cells is yellow green under CLSM (confocal laser scanning microscope, CLSM) observes, the cell survival on the collagen stroma is good.
Claims (10)
1. the application of collagen stroma in the preparation tissue engineering bracket material;
Said collagen stroma is made up of the material of following ratio of quality and the number of copies:
Collagen 50-90
Chitosan 8-48
Glycerol 0.5-5.
2. application according to claim 1 is characterized in that: the application of said collagen stroma in the timbering material of preparation cell growth; The preferred human vascular endothelial of said cell.
3. application according to claim 1 and 2 is characterized in that: said collagen stroma is to prepare according to the method that comprises the steps:
1) collagen being dissolved in mass concentration is in the 0.01-0.1% acetic acid aqueous solution, and processing mass concentration is the 1-3% collagen solution;
2) chitosan being dissolved in mass concentration is in the 0.01-0.1% acetic acid solution, and processing mass concentration is the 1-3% chitosan solution;
3) be (50-90) with said collagen solution, chitosan solution and glycerol according to the mass ratio of collagen, chitosan and glycerol: (8-48): mixed (0.5-5) is even, at-80 ℃--10 ℃ following lyophilization 1-5 days, obtain spongy material;
4) under 40-50 ℃, adopt the aldehydes cross-linking agent that said spongy material was carried out crosslinked fixedly 20-100 minute;
5) spongy material after will fixing with glycerine water solution clean, vacuum drying, obtain collagen stroma.
4. application according to claim 3 is characterized in that: the cross-linking agent of aldehydes described in the step 4) is formaldehyde, methyl-glyoxal or glutaraldehyde; Said crosslinkedly fixedly in gas generator, carry out;
In the said glycerine water solution of step 5), the mass ratio of glycerol and water is (0.1-10): (90-99.9).
5. according to claim 3 or 4 described application, it is characterized in that: said method also comprise the collagen stroma that step 4) is obtained pack,
60The step of Co radiation sterilization.
6. according to each described application among the claim 1-5, it is characterized in that: said chitosan is that to take off the hexanoyl degree be that 70-90%, viscosity-average molecular weight are (1.0-4.0) * 10
5Chitosan.
7. according to each described application among the claim 1-6, it is characterized in that: said collagen prepares according to following method:
A) epidermal area, muscle and fat are removed by the stripped animal tissue that will be rich in collagen, clean up after the pulverizing, obtain collagen tissue;
B) said collagen tissue is used aqueous slkali, the defat of alcohols material solution washing of pH8.5-10.5 respectively, obtained the collagen bullion;
C) with said collagen dissolving crude product in the acid solution of pH5.5-6.5;
D) in step c) solution, add compound protease, at 30-35 ℃ of following stir culture 10-15 hour; Said compound protease by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed; The proportioning of said collagen bullion and compound protease is (100-1000) g: 10000U;
E) centrifugal collection supernatant adds NaCl in supernatant, makes its concentration reach 2mol/L, and 0-10 ℃ was stirred 10-20 hour down, collected the precipitate that obtains, and was designated as precipitate 1;
F) precipitate 1 is dissolved in the mass concentration 0.1-0.5% acetic acid aqueous solution centrifugal collection supernatant; In supernatant, add NaCl again, make its concentration reach 1mol/L, stir and obtain precipitate 2; Repeating step f) operation is 3-4 time, obtains collagen.
8. application according to claim 7 is characterized in that: aqueous slkali described in the step b) is made up of sodium hydroxide, sodium bicarbonate and water, and wherein, the mass ratio of sodium hydroxide, sodium bicarbonate and water is followed successively by (0.1-1): (5-10): (89-94.9); Said alcohols material aqueous solution is made up of ethanol, isopropyl alcohol and water, and wherein the mass ratio of ethanol, isopropyl alcohol and water is followed successively by (5-10): (2-5): (85-93);
Acid solution described in the step c) is formic acid solution, acetic acid solution, propanoic acid solution or hydrochloric acid solution.
9. according to each described application among the claim 1-6, it is characterized in that: said collagen prepares according to following method:
A) with commercially available collagenolysis in the acid solution of pH5.5-6.5;
B) in above-mentioned solution, add compound protease, 30-35 ℃ following stir culture 10-15 hour; Said compound protease by specific activity is: pepsin: trypsin: three kinds of protease of papain=1: 1: 0.5 are formed; The proportioning of said collagen bullion and compound protease is (100-1000) g: 10000U;
C) centrifugal collection supernatant adds NaCl in supernatant, makes its concentration reach 2mol/L, and 0-10 ℃ was stirred 10-20 hour down, collected the precipitate that obtains, and was designated as precipitate a;
D) precipitate a being dissolved in mass concentration is in the 0.1-0.5% acetic acid aqueous solution, centrifugal collection supernatant; In supernatant, add NaCl again, make concentration reach 1mol/L, stir and obtain precipitate b; Repeating step D) operation is 3-4 time, obtains collagen.
10. application according to claim 9 is characterized in that: acid solution steps A) is formic acid solution, acetic acid solution, propanoic acid solution or hydrochloric acid solution.
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| WO2023185212A1 (en) * | 2022-03-29 | 2023-10-05 | 上海市第十人民医院 | Mineralized collagen material, preparation method therefor, and application thereof |
| CN115006597A (en) * | 2022-06-02 | 2022-09-06 | 上海威高医疗技术发展有限公司 | Oral cavity repairing film and preparation method thereof |
| CN115006597B (en) * | 2022-06-02 | 2024-01-19 | 上海威高医疗技术发展有限公司 | Oral cavity repairing film and preparation method thereof |
| RU2808686C1 (en) * | 2023-04-20 | 2023-12-01 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Курский государственный университет" | Method of porous collagen matrix production |
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