CN104213238A - Method for improving tensile strength of collagen fiber material - Google Patents
Method for improving tensile strength of collagen fiber material Download PDFInfo
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Abstract
The invention discloses a method for improving the tensile strength of a collagen fiber material. The method comprises the following steps: 1) dissolving natural collagen with acetic acid solution and dialyzing a phosphate buffer solution to obtain a collagen solution with collagen concentration of 1-20mg / mL and pH value of 6.0-9.0; 2) transferring the collagen solution into centrifugal tubes in a centrifuge with a horizontal rotor, and centrifuging for 5 to 120 minutes; 3) placing the centrifugal tubes vertically in a water bath or an incubator, standing for 2-48 h to get collagen gel; 4) placing the collagen gel in a 0.5%-10% aqueous solution of glutaraldehyde for cross-linking for 1-24 h, and then repeatedly rinsing with distilled water; and 5) naturally drying for 12 to 36 h, and drying in a blast drying box for 12-36 h to obtain the collagen fiber material. The collagen fiber prepared by the method of the invention has collagen fibers in consistent arrangement direction, and the tensile strength of the material can be improved significantly.
Description
Technical field
The invention belongs to medical biotechnology field of material technology, be specifically related to a kind of method improving collagenous fiber material tensile strength.
Background technology
In recent years, natural collagen (particularly NTx) obtains in fields such as biomedical material, medical tissue engineering, medical cosmetologies and applies more and more widely.As the application of collagen sponge in wound repair, quick-acting haemostatic powder; The application of collagen glue in skin of face smoothing wrinkle, targeted drug preparation and medicament slow release; The application of collagen composite materials in artificial blood vessel, artificial skin and bone, artificial cornea transplanting and the medical tissue engineering such as artificial heel string and tendon/ligament.
Good tensile strength is an important indicator of medical tissue engineering material requirements.If artificial heel string, artificial tendon materials are after the defect implanting heel string or tendon/ligament, not only require that material has good induced cell growth function, require that material has good tensile strength to bear human body motion stress and to guarantee that material kept good material shape and mechanical property before the reparation of body autologous tissue is complete simultaneously.But existing collagen base biological material tensile strength often can not meet the actual demand of medical science packing engineering application.
Self assembly (collagenous fibres restructuring) is the important molecule behavioural characteristic of natural collagen.Research finds, is all significantly better than the external performance of collagen monomer molecule in organism with the collagenous fibres of self assembly pattern formation in heat endurance, resistance to enzyme degradability and biomechanical property etc.Therefore, the method utilizing fiber to recombinate prepares collagen base biological material becomes a kind of effective means promoting collagen-based materials properties.As, China authorizes patent of invention CN100372579C to provide a kind of crosslinked apatite-collagen porous body containing autologous tissue's apatite-collagen composite and preparation method thereof, the method utilizes fiber recombinant technique to prepare the composite of mammal collagen and apatite, can be used for bone tissue engineer; China authorizes patent of invention CN101323670B to disclose a kind of medical grade reconstructed collagen cross-linking modified method, and the method utilizes fiber recombinant technique improve the performance of collagen and be applied to biomaterial for medical purpose.
The external fiber restructuring of collagen is divided into nucleation, fiber to grow up and balance three phases.Wherein, nucleation stage is that several collagen unimolecule is assembled in order and formed the process of collagen microfibrils, and the form of collagen microfibrils in this process, distribution determine the fractions distribution of final collagenous fibres.Under normal circumstances, the distribution of collagen microfibrils and orientation are completely randoms, and therefore in the final recombinant collagen fibrous material obtained, the distribution arrangement of collagenous fibres is also isotropic.In order to meet the demand in medical tissue engineering field, particularly to the requirement of Tensile strength, scholar is had to attempt preparing the collagenous fiber material with same orientation distribution.As, the method utilizing electric field, magnetic field or hydrodynamics to induce is ordered about collagenous fibres distribution arrangement and is reached unanimity in collagenous fibres regrouping process.Chinese invention patent CN102341436A discloses a kind of preparation method of orientation collagen gel, and the method utilizes fiber recombinant technique to have height-oriented collagen gel in conjunction with hydrodynamic interaction preparation.This advantage with the material of consistent fiber-wall-element model is: because collagenous fibres distribution arrangement is consistent, thus drastically increase the tensile strength of material, simultaneously, in medical tissue engineering field, this material energy inducing cell, thus can Achilles tendon repair, tendon/ligament tissue quickly along fiber orientation directions migration and propagation.But this preparation method's also Shortcomings utilizing electric field, magnetic field or hydrodynamics to induce, as operating condition requires the preparation etc. that high, required instrument and equipment is complicated, can not realize extensive sample.The invention provides a kind of short-cut method has identical fibre orientation trend collagenous fiber material with preparation.
Summary of the invention
Technical problem to be solved by this invention is to provide a kind of easy and effectively can strengthen the method for collagenous fiber material tensile strength, to meet the medical materials such as artificial heel string, tendon to the requirement of material tensile property.
For solving the problems of the technologies described above, the present invention adopts following technical scheme:
1) under condition of ice bath, dissolve natural collagen protein with aqueous acetic acid, and to phosphate buffered solution (i.e. PBS) dialysis to regulate collagen solution pH, to obtain collagen concentration be 1 ~ 20mg/mL, pH be 6.0 ~ 9.0 collagen solution;
2) proceeded to by collagen solution and be placed in the centrifuge tube of centrifuge, under 15 ~ 45 DEG C of conditions, control relative centrifugal force(RCF) is 1 ~ 30g, centrifugal 5 ~ 120 minutes; The rotor of described centrifuge is horizontal rotor (swing-out rotor);
3) by step 2) process after centrifuge tube be vertically placed in 25 ~ 45 DEG C of water-baths or constant incubator, leave standstill within 2 ~ 48 hours, obtain collagen glue;
4) at ambient temperature, by step 3) the collagen glue that obtains be placed in 0.5% ~ 10% the crosslinked 1 ~ 24h of glutaraldehyde water solution, subsequently with distilled water rinsing repeatedly;
5) at ambient temperature, by step 4) the cross-linked rubber virgin rubber air dry that obtains is after 12 ~ 36 hours, and be placed in air dry oven, under 25 ~ 45 DEG C of conditions, continue dry 12 ~ 36 hours, obtain collagenous fiber material.
Further, described step 5) in natural drying process, one end of collagen glue is fixed vertically downward, the vertical tension of 0.1 ~ 10N is continuously applied to the other end.
Further, described step 1) in, described natural collagen extracts from the skin, heel string tissue of mammal, fish, amphibian and the natural collagen with complete triple helical molecule structure of separation and purification.
Further, described step 1) in, the concentration of described aqueous acetic acid is 0.1 ~ 1.0mol/L, is 0 ~ 10 DEG C to the temperature of phosphate buffered solution dialysis.
Further, described step 2) centrifugal condition be: temperature is 20 ~ 30 DEG C, and relative centrifugal force(RCF) is 3 ~ 10g, and centrifugation time is 5 ~ 20 minutes.
Further, described step 3) in, the temperature of water-bath or constant incubator is 25 ~ 45 DEG C, and time of repose is 12 ~ 36 hours.
Further, described step 4) in, the concentration of glutaraldehyde water solution is 0.5% ~ 3%, and crosslinking time is 12 ~ 24h.
The present invention has the following advantages:
Because the external fiber restructuring of collagen is divided into nucleation, fiber to grow up and balance three phases, wherein, the orientation of nucleation stage collagenous fibres core directly determines the oriented of final collagenous fibres.Inventor finds, carries out centrifugal treating at the nucleation stage of collagen assembling to assembly system, and under the influence of centrifugal force, collagenous fibres nuclear energy along the arrangement of centrifugal force direction, and keeps this arrangement trend in the fiber stage of growth of follow-up assembling.On this basis, in dry run, apply the tensile force identical with centrifugal force direction further for collagen glue, collagenous fibres orientation can be made further to reach unanimity, thus obtain that there is more high-tensile collagenous fiber material.The method is compared with the existing preparation method with uniformity orientation collagenous fiber material, more simple and easy to do, and can carry out fairly large material preparation.
Accompanying drawing explanation
Fig. 1 is the Electronic Speculum collection of illustrative plates of the collagenous fiber material scanning electron microscopic observation collagenous fibres that embodiment 1 prepares.(arrow is labeled as centrifugal force direction)
Fig. 2 is the Electronic Speculum collection of illustrative plates of the collagenous fiber material scanning electron microscopic observation collagenous fibres that embodiment 2 prepares.(arrow is labeled as centrifugal force direction)
Fig. 3 is the Electronic Speculum collection of illustrative plates of the collagenous fiber material scanning electron microscopic observation collagenous fibres that comparative example prepares.
The TENSILE STRENGTH comparison diagram (often group measures material sample number n=10) of the collagenous fiber material that Fig. 4 is embodiment 1, embodiment 2 and comparative example prepare.
Detailed description of the invention
Below in conjunction with the drawings and specific embodiments, the present invention is further detailed explanation.
The method of the raising collagenous fiber material tensile strength designed by the present invention comprises the following steps:
1) under condition of ice bath, dissolve natural collagen protein with aqueous acetic acid, and to phosphate buffered solution (i.e. PBS) dialysis to regulate collagen solution pH, to obtain collagen concentration be 1 ~ 20mg/mL, pH be 6.0 ~ 9.0 collagen solution; The concentration of aqueous acetic acid is 0.1 ~ 1.0mol/L, is 0 ~ 10 DEG C to the temperature of phosphate buffered solution dialysis;
2) proceeded to by collagen solution and be placed in the centrifuge tube of centrifuge, under 15 ~ 45 DEG C of conditions, control relative centrifugal force(RCF) is 1 ~ 30g, centrifugal 5 ~ 120 minutes; The rotor of described centrifuge is horizontal rotor;
3) by step 2) process after centrifuge tube be vertically placed in 25 ~ 45 DEG C of water-baths or constant incubator, leave standstill within 2 ~ 48 hours, obtain collagen glue;
4) at ambient temperature, by step 3) the collagen glue that obtains be placed in 0.5% ~ 10% the crosslinked 1 ~ 24h of glutaraldehyde water solution, subsequently with distilled water rinsing repeatedly;
5) at ambient temperature, by step 4) the cross-linked rubber virgin rubber air dry that obtains is after 12 ~ 36 hours, and be placed in air dry oven, under 25 ~ 45 DEG C of conditions, continue dry 12 ~ 36 hours, obtain collagenous fiber material.
Embodiment 1
Under condition of ice bath, dissolve with the aqueous acetic acid of 0.5mol/L the NTx albumen extracted from grass carp fish-skin.Under 4 DEG C of conditions, make the pH of collagen solution be adjusted to 7.0 to phosphate buffered solution dialysis, obtain the collagen solution that concentration is 3mg/mL.Collagen solution is transferred in 10mL centrifuge tube, at 25 DEG C, under relative centrifugal force(RCF) 3g condition centrifugal 5 minutes.Taking-up centrifuge tube is careful, vertical subsequently vertical transitions, in insulating box, continue under 30 DEG C of conditions to leave standstill 24 hours.From centrifuge tube, take out collagen glue, be transferred to crosslinked 24h in the glutaraldehyde solution of 1%, take out collagen glue subsequently and use distilled water cyclic washing; Then at ambient temperature, one end of collagen glue is vertically fixed, be continuously applied the pulling force vertically downward of 0.7 N to the other end, air dry obtains collagenous fiber material after within 24 hours, being transferred to by collagen glue afterwards and continuing dry 24 hours under 30 DEG C of conditions in air dry oven.
Embodiment 2
Under condition of ice bath, dissolve with the aqueous acetic acid of 0.5mol/L the NTx albumen extracted from grass carp fish-skin.Under 4 DEG C of conditions, make the pH of collagen solution be adjusted to 7.0 to phosphate buffered solution dialysis, obtain the collagenic acid solution that concentration is 3mg/mL.Collagen solution is transferred in 10mL centrifuge tube, at 25 DEG C, under centrifugal force 3g condition centrifugal 5 minutes.Taking-up centrifuge tube is careful, vertical subsequently vertical transitions, in insulating box, continue under 30 DEG C of conditions to leave standstill 24 hours.From centrifuge tube, take out collagen glue, be transferred to crosslinked 24h in the glutaraldehyde solution of 1%, take out collagen glue subsequently and use distilled water cyclic washing; Then collagen glue is transferred to after air dry 24 hours at ambient temperature after continuing dry 24 hours under 30 DEG C of conditions in air dry oven and obtains collagenous fiber material.
Comparative example
Under condition of ice bath, dissolve with the aqueous acetic acid of 0.5mol/L the NTx albumen extracted from grass carp fish-skin.Under 4 DEG C of conditions, make the pH of collagen solution be adjusted to 7.0 to phosphate buffered solution dialysis, obtain the collagenic acid solution that concentration is 3mg/mL.Be transferred to by collagen solution in 10mL centrifuge tube, vertical transitions, in insulating box, leaves standstill 24 hours under 30 DEG C of conditions.From centrifuge tube, take out collagen glue, be transferred to crosslinked 24h in the glutaraldehyde solution of 1%, take out collagen glue subsequently and use distilled water cyclic washing; Then collagen glue is transferred to after air dry 24 hours at ambient temperature after continuing dry 24 hours under 30 DEG C of conditions in air dry oven and obtains collagenous fiber material.
Can find from the collection of illustrative plates of the ESEM of Fig. 1-3, the arrangement mode of collagenous fibres completely random in comparative example, in embodiment 2 there is the trend significantly arranged along centrifugal force direction in collagenous fibres.And after drying stage applies vertical tension, in embodiment 1, this orientation arrangement trend of collagenous fibres is more obvious.
Can observe from Fig. 4, the materials variances that the TENSILE STRENGTH of embodiment 2 collagen-based materials and comparative example method prepare extremely significantly (p < 0.01), illustrate that after adopting the inventive method, the stretch-proof mechanical property of collagen-based materials is able to remarkable lifting.Meanwhile, compared with embodiment 2 collagen-based materials, the TENSILE STRENGTH of embodiment 1 collagen-based materials is further improved again, illustrates that applying vertical tension at drying stage can strengthen beneficial effect of the present invention further.
Claims (10)
1. one kind is improved the method for collagenous fiber material tensile strength, be included under condition of ice bath with aqueous acetic acid dissolve natural collagen prepare collagen solution step, to phosphate buffered solution dialysis with the step regulating collagen solution pH, it is characterized in that: after above step process, gained collagen solution concentration is 1 ~ 20mg/mL, pH is 6.0 ~ 9.0; And then carry out following steps:
1) proceeded to by collagen solution and be placed in the centrifuge tube of centrifuge, under 15 ~ 45 DEG C of conditions, control relative centrifugal force(RCF) is 1 ~ 30g, centrifugal 5 ~ 120 minutes; The rotor of described centrifuge is horizontal rotor;
2) by step 1) process after centrifuge tube be vertically placed in 25 ~ 45 DEG C of water-baths or constant incubator, leave standstill within 2 ~ 48 hours, obtain collagen glue;
3) at ambient temperature, by step 2) the collagen glue that obtains be placed in 0.5% ~ 10% the crosslinked 1 ~ 24h of glutaraldehyde water solution, subsequently with distilled water rinsing repeatedly;
4) at ambient temperature, by step 3) the cross-linked rubber virgin rubber air dry that obtains is after 12 ~ 36 hours, and be placed in air dry oven, under 25 ~ 45 DEG C of conditions, continue dry 12 ~ 36 hours, obtain collagenous fiber material.
2. the method for raising collagenous fiber material tensile strength according to claim 1, is characterized in that: described step 4) in natural drying process, one end of collagen glue is fixed vertically downward, the vertical tension of 0.1 ~ 10N is continuously applied to the other end.
3. the method for raising collagenous fiber material tensile strength according to claim 1 and 2, is characterized in that: described natural collagen extracts from the skin, heel string tissue of mammal, fish, amphibian and the natural collagen with complete triple helical molecule structure of separation and purification.
4. the method for raising collagenous fiber material tensile strength according to claim 1 and 2, is characterized in that: described step 1) centrifugal condition be: temperature is 20 ~ 30 DEG C, and relative centrifugal force(RCF) is 3 ~ 10g, and centrifugation time is 5 ~ 20 minutes.
5. the method for raising collagenous fiber material tensile strength according to claim 3, is characterized in that: described step 1) centrifugal condition be: temperature is 20 ~ 30 DEG C, and relative centrifugal force(RCF) is 3 ~ 10g, and centrifugation time is 5 ~ 20 minutes.
6. the method for raising collagenous fiber material tensile strength according to claim 1 and 2, is characterized in that: described step 2) in, the temperature of water-bath or constant incubator is 25 ~ 45 DEG C, and time of repose is 12 ~ 36 hours.
7. the method for raising collagenous fiber material tensile strength according to claim 3, is characterized in that: described step 2) in, the temperature of water-bath or constant incubator is 25 ~ 45 DEG C, and time of repose is 12 ~ 36 hours.
8. the method for raising collagenous fiber material tensile strength according to claim 1 and 2, is characterized in that: described step 3) in, the concentration of glutaraldehyde water solution is 0.5% ~ 3%, and crosslinking time is 12 ~ 24h.
9. the method for raising collagenous fiber material tensile strength according to claim 3, is characterized in that: described step 3) in, the concentration of glutaraldehyde water solution is 0.5% ~ 3%, and crosslinking time is 12 ~ 24h.
10. the method for raising collagenous fiber material tensile strength according to claim 1 and 2, is characterized in that: described step 1) in, the concentration of described aqueous acetic acid is 0.1 ~ 1.0mol/L, is 0 ~ 10 DEG C to the temperature of phosphate buffered solution dialysis.
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Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105641747A (en) * | 2016-04-19 | 2016-06-08 | 北京航空航天大学 | Flow shear stress mediated collagen self-assembly method |
| CN105918761A (en) * | 2016-04-22 | 2016-09-07 | 武汉轻工大学 | Method for improving thermal stability of collagen through ultrahigh pressure treatment |
| CN108976442A (en) * | 2018-06-22 | 2018-12-11 | 武汉轻工大学 | Fibrosis collagen gel and preparation method thereof is assembled altogether |
| CN110343169A (en) * | 2019-08-12 | 2019-10-18 | 武汉轻工大学 | A kind of modified I-type collagen and method of modifying and collagen gel using modification I-type collagen preparation |
| CN111773431A (en) * | 2020-06-17 | 2020-10-16 | 北京大学口腔医学院 | Preparation method of tendon-like scaffold material and application of tendon-like scaffold material in tendon injury regeneration and repair |
| CN114618017A (en) * | 2022-01-27 | 2022-06-14 | 华东理工大学 | Collagen membrane with highly oriented and crystalline collagen fiber structure and preparation method thereof |
Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0376931A1 (en) * | 1984-12-24 | 1990-07-04 | Collagen Corporation | Process for making collagen membranous materials for medical use |
| JP2001009020A (en) * | 1999-05-19 | 2001-01-16 | Coletica | Sea-origin collagen-containing collagen product having low odorous property and improved mechanical characteristics and its use as cosmetics or medicinal composition or product |
| KR20040024303A (en) * | 2002-09-13 | 2004-03-20 | 이진호 | Fabrication method of porous polymeric scaffolds for tissue engineering application |
| US20060135638A1 (en) * | 2004-12-22 | 2006-06-22 | Pedrozo Hugo A | Method for organizing the assembly of collagen fibers and compositions formed therefrom |
| US20080105998A1 (en) * | 2006-11-03 | 2008-05-08 | R&D Green Materials, Llc | Process for Preparing Biodegradable Articles |
| CN101323670A (en) * | 2008-07-29 | 2008-12-17 | 四川大学 | Medical grade reconstructed collagen cross-linking modified method |
| CN101579247A (en) * | 2009-06-23 | 2009-11-18 | 许和平 | I-type collagen peripheral nerve sheath keeping the peculiar triple helical structure of collagen, preparation method and applications thereof |
| CN102416200A (en) * | 2011-12-02 | 2012-04-18 | 四川大学 | Preparation method for constructing collagen-based bio-macromolecular/hydroxyapatite microsphere composite bracket material |
| CN103408787A (en) * | 2013-07-29 | 2013-11-27 | 武汉轻工大学 | Sponge material of collagen from freshwater fish and preparation method thereof |
-
2014
- 2014-08-11 CN CN201410392802.1A patent/CN104213238B/en active Active
Patent Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0376931A1 (en) * | 1984-12-24 | 1990-07-04 | Collagen Corporation | Process for making collagen membranous materials for medical use |
| JP2001009020A (en) * | 1999-05-19 | 2001-01-16 | Coletica | Sea-origin collagen-containing collagen product having low odorous property and improved mechanical characteristics and its use as cosmetics or medicinal composition or product |
| KR20040024303A (en) * | 2002-09-13 | 2004-03-20 | 이진호 | Fabrication method of porous polymeric scaffolds for tissue engineering application |
| US20060135638A1 (en) * | 2004-12-22 | 2006-06-22 | Pedrozo Hugo A | Method for organizing the assembly of collagen fibers and compositions formed therefrom |
| US20080105998A1 (en) * | 2006-11-03 | 2008-05-08 | R&D Green Materials, Llc | Process for Preparing Biodegradable Articles |
| CN101323670A (en) * | 2008-07-29 | 2008-12-17 | 四川大学 | Medical grade reconstructed collagen cross-linking modified method |
| CN101579247A (en) * | 2009-06-23 | 2009-11-18 | 许和平 | I-type collagen peripheral nerve sheath keeping the peculiar triple helical structure of collagen, preparation method and applications thereof |
| CN102416200A (en) * | 2011-12-02 | 2012-04-18 | 四川大学 | Preparation method for constructing collagen-based bio-macromolecular/hydroxyapatite microsphere composite bracket material |
| CN103408787A (en) * | 2013-07-29 | 2013-11-27 | 武汉轻工大学 | Sponge material of collagen from freshwater fish and preparation method thereof |
Non-Patent Citations (1)
| Title |
|---|
| 徐新宇: ""胶原的提取、改性、交联及其应用"", 《透析与人工器官》, vol. 15, no. 3, 30 September 2004 (2004-09-30), pages 38 - 46 * |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105641747A (en) * | 2016-04-19 | 2016-06-08 | 北京航空航天大学 | Flow shear stress mediated collagen self-assembly method |
| CN105641747B (en) * | 2016-04-19 | 2020-07-10 | 北京航空航天大学 | Collagen self-assembly method mediated by fluid shear force |
| CN105918761A (en) * | 2016-04-22 | 2016-09-07 | 武汉轻工大学 | Method for improving thermal stability of collagen through ultrahigh pressure treatment |
| CN108976442A (en) * | 2018-06-22 | 2018-12-11 | 武汉轻工大学 | Fibrosis collagen gel and preparation method thereof is assembled altogether |
| CN110343169A (en) * | 2019-08-12 | 2019-10-18 | 武汉轻工大学 | A kind of modified I-type collagen and method of modifying and collagen gel using modification I-type collagen preparation |
| CN111773431A (en) * | 2020-06-17 | 2020-10-16 | 北京大学口腔医学院 | Preparation method of tendon-like scaffold material and application of tendon-like scaffold material in tendon injury regeneration and repair |
| CN114618017A (en) * | 2022-01-27 | 2022-06-14 | 华东理工大学 | Collagen membrane with highly oriented and crystalline collagen fiber structure and preparation method thereof |
| CN114618017B (en) * | 2022-01-27 | 2023-06-02 | 华东理工大学 | Collagen film with highly oriented and crystalline collagen fiber structure and preparation method thereof |
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Effective date of registration: 20200206 Address after: 510663 floor 4, zone a, No.1 Xiangshan Road, Guangzhou high tech Industrial Development Zone, Guangzhou, Guangdong Province Patentee after: Guangzhou Chuang Er Biotechnology Co., Ltd. Address before: 430023 School of chemical engineering, Wuhan light industry university, No. 68, South Road, evergreen garden, Wuhan, Hubei Patentee before: Wuhan Polytechnic University |