CN106115792A - One prepares Fe with collagen protein for biomineralization template2o3the method of nanoparticle - Google Patents
One prepares Fe with collagen protein for biomineralization template2o3the method of nanoparticle Download PDFInfo
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- CN106115792A CN106115792A CN201610458525.9A CN201610458525A CN106115792A CN 106115792 A CN106115792 A CN 106115792A CN 201610458525 A CN201610458525 A CN 201610458525A CN 106115792 A CN106115792 A CN 106115792A
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- 102000008186 Collagen Human genes 0.000 title claims abstract description 63
- 108010035532 Collagen Proteins 0.000 title claims abstract description 63
- 238000000034 method Methods 0.000 title claims abstract description 27
- 230000033558 biomineral tissue development Effects 0.000 title claims abstract description 18
- 239000002105 nanoparticle Substances 0.000 title claims abstract description 18
- 229920001436 collagen Polymers 0.000 claims abstract description 41
- 239000002086 nanomaterial Substances 0.000 claims abstract description 19
- 238000002360 preparation method Methods 0.000 claims abstract description 19
- XEEYBQQBJWHFJM-UHFFFAOYSA-N iron Substances [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims abstract description 16
- NQXWGWZJXJUMQB-UHFFFAOYSA-K iron trichloride hexahydrate Chemical compound O.O.O.O.O.O.[Cl-].Cl[Fe+]Cl NQXWGWZJXJUMQB-UHFFFAOYSA-K 0.000 claims abstract description 15
- 229910003145 α-Fe2O3 Inorganic materials 0.000 claims abstract description 15
- 238000000746 purification Methods 0.000 claims abstract description 14
- 238000001027 hydrothermal synthesis Methods 0.000 claims abstract description 13
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 10
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 10
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 10
- 239000002131 composite material Substances 0.000 claims abstract description 8
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 6
- 238000005516 engineering process Methods 0.000 claims abstract description 5
- 239000008240 homogeneous mixture Substances 0.000 claims abstract description 4
- 239000007787 solid Substances 0.000 claims description 21
- 210000004027 cell Anatomy 0.000 claims description 19
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 18
- 230000000844 anti-bacterial effect Effects 0.000 claims description 9
- 230000001580 bacterial effect Effects 0.000 claims description 9
- 239000001963 growth medium Substances 0.000 claims description 9
- 239000006228 supernatant Substances 0.000 claims description 9
- 239000000725 suspension Substances 0.000 claims description 9
- 239000007788 liquid Substances 0.000 claims description 8
- 239000000203 mixture Substances 0.000 claims description 8
- FRXSZNDVFUDTIR-UHFFFAOYSA-N 6-methoxy-1,2,3,4-tetrahydroquinoline Chemical compound N1CCCC2=CC(OC)=CC=C21 FRXSZNDVFUDTIR-UHFFFAOYSA-N 0.000 claims description 6
- 235000019750 Crude protein Nutrition 0.000 claims description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- 230000003115 biocidal effect Effects 0.000 claims description 6
- 239000000872 buffer Substances 0.000 claims description 6
- 239000012460 protein solution Substances 0.000 claims description 6
- 238000010792 warming Methods 0.000 claims description 6
- 241000588724 Escherichia coli Species 0.000 claims description 5
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 claims description 4
- 229960002897 heparin Drugs 0.000 claims description 4
- 229920000669 heparin Polymers 0.000 claims description 4
- 239000013612 plasmid Substances 0.000 claims description 4
- 241000894006 Bacteria Species 0.000 claims description 3
- 230000003321 amplification Effects 0.000 claims description 3
- 239000007853 buffer solution Substances 0.000 claims description 3
- 239000006227 byproduct Substances 0.000 claims description 3
- 238000005119 centrifugation Methods 0.000 claims description 3
- 239000012531 culture fluid Substances 0.000 claims description 3
- 230000007850 degeneration Effects 0.000 claims description 3
- 239000008367 deionised water Substances 0.000 claims description 3
- 229910021641 deionized water Inorganic materials 0.000 claims description 3
- 238000009792 diffusion process Methods 0.000 claims description 3
- 238000001035 drying Methods 0.000 claims description 3
- 239000012530 fluid Substances 0.000 claims description 3
- 230000008014 freezing Effects 0.000 claims description 3
- 238000007710 freezing Methods 0.000 claims description 3
- 239000008187 granular material Substances 0.000 claims description 3
- 150000002460 imidazoles Chemical class 0.000 claims description 3
- 102000006495 integrins Human genes 0.000 claims description 3
- 108010044426 integrins Proteins 0.000 claims description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 claims description 3
- 238000011068 loading method Methods 0.000 claims description 3
- 239000002609 medium Substances 0.000 claims description 3
- 238000003199 nucleic acid amplification method Methods 0.000 claims description 3
- 210000002706 plastid Anatomy 0.000 claims description 3
- 239000011780 sodium chloride Substances 0.000 claims description 3
- 229910000162 sodium phosphate Inorganic materials 0.000 claims description 3
- 239000001488 sodium phosphate Substances 0.000 claims description 3
- 238000010257 thawing Methods 0.000 claims description 3
- 230000009466 transformation Effects 0.000 claims description 3
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 claims description 3
- 241000193830 Bacillus <bacterium> Species 0.000 claims 1
- 239000004744 fabric Substances 0.000 claims 1
- 210000002429 large intestine Anatomy 0.000 claims 1
- 230000008569 process Effects 0.000 abstract description 8
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 abstract description 5
- 238000012805 post-processing Methods 0.000 abstract description 5
- 239000003153 chemical reaction reagent Substances 0.000 abstract description 4
- 239000002994 raw material Substances 0.000 abstract description 4
- 238000011031 large-scale manufacturing process Methods 0.000 abstract description 3
- 229910000859 α-Fe Inorganic materials 0.000 description 7
- 239000000243 solution Substances 0.000 description 6
- 238000002156 mixing Methods 0.000 description 4
- 229910021578 Iron(III) chloride Inorganic materials 0.000 description 3
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- RBTARNINKXHZNM-UHFFFAOYSA-K iron trichloride Chemical compound Cl[Fe](Cl)Cl RBTARNINKXHZNM-UHFFFAOYSA-K 0.000 description 3
- 229910052500 inorganic mineral Inorganic materials 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 238000002411 thermogravimetry Methods 0.000 description 2
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 239000003519 biomedical and dental material Substances 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000012776 electronic material Substances 0.000 description 1
- 238000005265 energy consumption Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 239000000383 hazardous chemical Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000003837 high-temperature calcination Methods 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- UQSXHKLRYXJYBZ-UHFFFAOYSA-N iron oxide Inorganic materials [Fe]=O UQSXHKLRYXJYBZ-UHFFFAOYSA-N 0.000 description 1
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 229910044991 metal oxide Inorganic materials 0.000 description 1
- 150000004706 metal oxides Chemical class 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 230000006911 nucleation Effects 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 235000006408 oxalic acid Nutrition 0.000 description 1
- NDLPOXTZKUMGOV-UHFFFAOYSA-N oxo(oxoferriooxy)iron hydrate Chemical compound O.O=[Fe]O[Fe]=O NDLPOXTZKUMGOV-UHFFFAOYSA-N 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 230000007096 poisonous effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 235000013759 synthetic iron oxide Nutrition 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01G—COMPOUNDS CONTAINING METALS NOT COVERED BY SUBCLASSES C01D OR C01F
- C01G49/00—Compounds of iron
- C01G49/02—Oxides; Hydroxides
- C01G49/06—Ferric oxide [Fe2O3]
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2002/00—Crystal-structural characteristics
- C01P2002/70—Crystal-structural characteristics defined by measured X-ray, neutron or electron diffraction data
- C01P2002/72—Crystal-structural characteristics defined by measured X-ray, neutron or electron diffraction data by d-values or two theta-values, e.g. as X-ray diagram
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2002/00—Crystal-structural characteristics
- C01P2002/80—Crystal-structural characteristics defined by measured data other than those specified in group C01P2002/70
- C01P2002/85—Crystal-structural characteristics defined by measured data other than those specified in group C01P2002/70 by XPS, EDX or EDAX data
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2002/00—Crystal-structural characteristics
- C01P2002/80—Crystal-structural characteristics defined by measured data other than those specified in group C01P2002/70
- C01P2002/88—Crystal-structural characteristics defined by measured data other than those specified in group C01P2002/70 by thermal analysis data, e.g. TGA, DTA, DSC
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2004/00—Particle morphology
- C01P2004/01—Particle morphology depicted by an image
- C01P2004/03—Particle morphology depicted by an image obtained by SEM
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2004/00—Particle morphology
- C01P2004/01—Particle morphology depicted by an image
- C01P2004/04—Particle morphology depicted by an image obtained by TEM, STEM, STM or AFM
-
- C—CHEMISTRY; METALLURGY
- C01—INORGANIC CHEMISTRY
- C01P—INDEXING SCHEME RELATING TO STRUCTURAL AND PHYSICAL ASPECTS OF SOLID INORGANIC COMPOUNDS
- C01P2004/00—Particle morphology
- C01P2004/60—Particles characterised by their size
- C01P2004/61—Micrometer sized, i.e. from 1-100 micrometer
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Inorganic Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses one and prepare Fe with collagen protein for biomineralization template2O3The method of nanoparticle, comprises the steps: that (1) utilizes biology gene engineering technology to prepare recombined collagen: 1., determine the sequence of recombined collagen；2., the nucleic acid of composite coding recombined collagen；3., the preparation of recombined collagen and purification；(2)α‑Fe2O3The preparation of nano material: 1., the preparation of recombined collagen and Iron(III) chloride hexahydrate homogeneous mixture solotion；2. hydrothermal reaction kettle, is utilized to prepare nanometer alpha Fe2O3；3., nano material prepared by purification kept dry.The present invention uses recombined collagen as raw material, by hydrothermal method, to be prepared for the α Fe of size and morphology controllable as biological template, Iron(III) chloride hexahydrate2O3Nano material.The present invention in whole building-up process without adding any other chemical reagent or carrying out post processing, simple and convenient, it is easy to operation, have great application prospect, can be large-scale production α Fe2O3Nano material provides basis.
Description
Technical field
The present invention relates to Fe2O3Nanoparticle preparation method, is specifically related to a kind of with collagen protein for biomineralization template system
Standby Fe2O3The method of nanoparticle, belongs to Inorganic biomatetials preparing technical field.
Background technology
Biomineralization refers to that organism passes through the process of the regulating and controlling effect generation inorganic mineral of biomacromolecule, and it is chain
Connect the bridge between inorganic and biology.From different being of general mineralising maximum, it is biological at specific position, certain
Under physical and chemical condition, biological organism matter participation control or under the influence of, be solid phase mineral by the ion transit in solution
Process.As skeleton, scale, the formation of tooth etc. is all biomineralization process relatively common in nature.With commercial production
Condition is different, and biomineralization need not exacting terms, and it is a mild condition, low power consuming and free of contamination physical chemistry mistake
Journey.Biomineralization have employed component fairly simple and common in nature, and can realize sample from nucleation to crystallization
The regulation and control of process.Therefore, explore and inorganic matter mineralising mechanism under biomolecule regulates and controls in mimic biology mineralising, can be for preparation
There is the visual angle that the composite offer of unique texture and performance is new.
Alpha-type ferric oxide (α-Fe2O3) it is a kind of critically important metal-oxide, owing to it is nontoxic, non-environmental-pollution,
The feature such as with low cost, is all widely used at aspects such as flash coating material, plastics, electronic material and biomedical engineerings.
Have now been established α-Fe2O3The multiple synthetic method of nano material, including: (1) uses ferric chloride and oxalic acid to be that raw material is first
The primary structure of first synthetic iron oxide, the most again by fusiformis and the spherical structure α-Fe of high-temperature calcination synthesis hollow2O3；(2) make
With ferric chloride and tetrabutyl desert money in the basic conditions, flower-shaped α-Fe2O3 nanostructured is prepared through post processing.These sides
The needs that method has add poisonous and hazardous chemical reagent in building-up process, and some needs remove solvent or template etc. through heating up
Post processing just can obtain product, the most relatively complicated, and there is time consumption and energy consumption and relatively costly shortcoming.Simultaneously as
At present to α-Fe2O3Still system not is with abundant, therefore for meeting difference in the basic research of nano-particle pattern and dimensional controllability
Demand, uses the method for simple, easily-controllable, environmental protection to regulate and control α-Fe2O3The pattern of nano-particle and size have particularly significant
Meaning.
Collagen protein be extracellular matrix mainly comprise composition, be almost distributed in all of histoorgan, it feed
In breast animal, content is up to 1/4th of total protein concentration.Collagen protein has good biocompatibility, biological degradability, inhales
The various functions such as the property received and promotion cell formation, therefore, in fields such as bio-medical material, organizational project, cosmetics, food
Have a wide range of applications.The present invention uses recombined collagen as biological template, and Iron(III) chloride hexahydrate, as raw material, passes through
Hydrothermal method, is prepared for the α-Fe of size and morphology controllable2O3Nano material.The present invention in whole building-up process without add
Any other chemical reagent or carry out post processing, simple and convenient, it is easy to operation, there is suitable feasibility and using value, can
For large-scale production α-Fe2O3Nano material provides basis.
Summary of the invention
It is an object of the invention to for deficiency of the prior art, it is provided that a kind of with collagen protein for biomineralization template system
Standby Fe2O3The method of nanoparticle, use the most protein collagen protein of animal in-vivo content as biological template, six hydrations
Ferric chloride, as raw material, by hydrothermal method, is prepared for the α-Fe of size and morphology controllable2O3Nano material.
For achieving the above object, the invention discloses following technical scheme:
One prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle, comprises the steps:
(1) biology gene engineering technology is utilized to prepare recombined collagen
1. the sequence of recombined collagen, is determined；
The sequence of recombined collagen is:
GSPGLPGPRGEQGPTGPTGPAGPRGLQGLQGLQGERGEQGPTGPAGPRGLQGERGEQGPTGLAGKAGEAGAKGETGP
AGPQGPRGEQGPQGLPGKDGEAGAQGRPGKRGKQGQKGEKGEPGTQGAKGDRGETGPVGPRGERGEAGPAGKDGERG
FPGERGVEGQNGQDGLPGKDGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQDGKDGLPGKDGKDGLPGKDGKD
GQPGKPGKYGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP, this recombined collagen possesses good triple helices structure,
Hot temperature is close to 37 DEG C；There is the binding site GERGFPGERGVE of integrin, can adhere well to cell；There is liver
The binding site GRPGKRGKQGQK of element, can be with Heparin-binding；
2., the nucleic acid of composite coding recombined collagen；
The nucleic acid of composite coding step 1. recombined collagen, builds the plasmid importing above-mentioned nucleic acid, and by Plastid transformation
E. coli bl21-DE3 bacterial strain；
3., the preparation of recombined collagen and purification；
Thawing it is placed in ice bath, by competent cell and 3-5ul matter by freezing the competent escherichia coli cell at-80 DEG C
Grain mixing, mixture places into 90s in 42 DEG C of water-baths in ice bath, then places into 2min in ice bath after 30min；Above-mentioned mixed
Zoarium adds the 1ml LB culture medium without antibiotic, then is positioned over 1hrs in 37 DEG C of constant-temperature tables, then at 4 DEG C,
Under the conditions of 4000rpm, centrifugal 20min, discards the supernatant；Make antibacterial after Eddy diffusion in remaining culture liq, culture fluid is equal
On the even AMP culture plate being applied to 37 DEG C, it is placed in incubated overnight in 37 DEG C of constant-temperature tables；Next day the preferable bacterium colony of picking growing way
Putting in the 100ml LB fluid medium containing antibiotic, constant-temperature table overnight carries out Zengjing Granule；By 100ml incubated overnight
Antibacterial is poured in 1L LB culture medium, continues amplification cultivation in 37 DEG C of constant-temperature tables；Treat that OD value reaches 0.8-1 scope, by shaking table
Temperature is adjusted to 25 DEG C, adds 1mM IPTG abduction delivering, constant temperature incubated overnight；
The antibacterial expressed by above-mentioned albumen is centrifugal in refrigerated centrifuge, makes thalline separate with culture medium, centrifugal condition:
12000rpm, 4 DEG C, centrifugal 1.0-3.0min；Thalline A buffer solution after being centrifuged, A buffer is 20mM imidazoles,
20mM sodium phosphate, 0.5M sodium chloride, pH is 7.4；Bacterial suspension is put into ultrasonic cell disruption instrument carries out cell breakage,
Albumen can be discharged and albumen can be dissolved in A buffer；Bacterial suspension need to be put in ice bath time ultrasonic, in case temperature
Too high cause albuminous degeneration；The suspension recentrifuge that will have crushed, makes cell debris separate with protein solution, centrifugal condition:
14000rpm, 4 DEG C, 30-50min；Collecting supernatant, this is crude protein solution；After being filtered by crude protein, pass through liquid chromatograph
It is further purified；By lyophilizing, obtain white fluffy solid；This solid is put in-20 DEG C of Refrigerator stores, by claiming during use
Weight method demarcates concentration.
(2)α-Fe2O3The preparation of nano material
1., recombined collagen and the preparation of Iron(III) chloride hexahydrate homogeneous mixture solotion；
In 1ml water, add 1-50mg Iron(III) chloride hexahydrate and 0-10mg collagen solids, mix homogeneously, slowly stir
After mixing 5-90min, obtain pale yellow transparent and uniform liquid；
2. hydrothermal reaction kettle, is utilized to prepare nanometer alpha-Fe2O3；
Gained mixed liquor is poured in 5ml hydrothermal reaction kettle, puts into Muffle furnace and be warming up to the speed of 3-18 DEG C/min
120-200 DEG C, and react 1-15hrs at such a temperature；
3., nano material prepared by purification kept dry；
After hydrothermal reaction kettle is cooled to room temperature, by product by centrifugation, centrifugal condition is 1200r, supernatant discarded
Liquid, leaves solid；And use deionized water dispersing solid, then centrifugal purification 3-5 time, it is dried in 50-80 DEG C of thermostatic drying chamber.
As a preferred technical solution of the present invention, the purity of the recombined collagen that step obtains the most after purification reaches
More than 95%.
As a preferred technical solution of the present invention, the collagen solids addition described in step (2) is 0.1-
5mg, collagen protein quality mark is 0.01-0.5wt%.
As a preferred technical solution of the present invention, the Iron(III) chloride hexahydrate solids loading content described in step (2)
For 2.7-27mg, the concentration of ferrum (III) is distributed from 0.01 to 0.1mol/L.
As a preferred technical solution of the present invention, the Iron(III) chloride hexahydrate described in step (2) and collagen protein
It is 20-50min that mixed liquor is slowly stirred the time.
As a preferred technical solution of the present invention, the mixed liquor described in step (2) in Muffle furnace with 3-10 DEG C/
The speed of min is warming up to 140-180 DEG C, and reacts 6-12hrs at such a temperature.
One disclosed by the invention prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle, have with
Lower advantage: without adding any other chemical reagent or carrying out post processing in whole building-up process, simple and convenient, it is easy to behaviour
Make, there is suitable feasibility and using value, can be large-scale production α-Fe2O3Nano material provides basis.
Accompanying drawing explanation
Fig. 1 is the α-Fe of preparation2O3X-ray powder polycrystalline diffraction (XRD) figure of nano material；
Fig. 2 is the α-Fe of preparation2O3X-ray photoelectron power spectrum (XPS) figure of nano material；
Fig. 3 is the α-Fe of preparation2O3Thermogravimetric analysis (TGA) figure of nano material；
Fig. 4 is the α-Fe of preparation2O3The scanning electron microscope of nano material, transmission electron microscope, electronic diffraction and energy dispersive X penetrate
Line analysis figure；
Fig. 5 is that the recombined collagen of variable concentrations is to α-Fe2O3The impact of nanoparticle structure；
Detailed description of the invention
For the technological means making the present invention realize, creation characteristic, reach purpose and be easy to understand with effect, below in conjunction with
Detailed description of the invention, is expanded on further the present invention.
As Figure 1-Figure 5, one prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle, including
Following steps:
(1) biology gene engineering technology is utilized to prepare recombined collagen
1. the sequence of recombined collagen, is determined；
The sequence of recombined collagen is:
GSPGLPGPRGEQGPTGPTGPAGPRGLQGLQGLQGERGEQGPTGPAGPRGLQGERGEQGPTGLAGKAGEAGAKGETGP
AGPQGPRGEQGPQGLPGKDGEAGAQGRPGKRGKQGQKGEKGEPGTQGAKGDRGETGPVGPRGERGEAGPAGKDGERG
FPGERGVEGQNGQDGLPGKDGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQDGKDGLPGKDGKDGLPGKDGKD
GQPGKPGKYGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP, this recombined collagen possesses good triple helices structure,
Hot temperature is close to 37 DEG C；There is the binding site GERGFPGERGVE of integrin, can adhere well to cell；There is liver
The binding site GRPGKRGKQGQK of element, can be with Heparin-binding；
2., the nucleic acid of composite coding recombined collagen；
The nucleic acid of composite coding step 1. recombined collagen, builds the plasmid importing above-mentioned nucleic acid, and by Plastid transformation
E. coli bl21-DE3 bacterial strain；
3., the preparation of recombined collagen and purification；
Thawing it is placed in ice bath, by competent cell and 3-5ul matter by freezing the competent escherichia coli cell at-80 DEG C
Grain mixing, mixture places into 90s in 42 DEG C of water-baths in ice bath, then places into 2min in ice bath after 30min；Above-mentioned mixed
Zoarium adds the 1ml LB culture medium without antibiotic, then is positioned over 1hrs in 37 DEG C of constant-temperature tables, then at 4 DEG C,
Under the conditions of 4000rpm, centrifugal 20min, discards the supernatant；Make antibacterial after Eddy diffusion in remaining culture liq, culture fluid is equal
On the even AMP culture plate being applied to 37 DEG C, it is placed in incubated overnight in 37 DEG C of constant-temperature tables；Next day the preferable bacterium colony of picking growing way
Putting in the 100ml LB fluid medium containing antibiotic, constant-temperature table overnight carries out Zengjing Granule；By 100ml incubated overnight
Antibacterial is poured in 1L LB culture medium, continues amplification cultivation in 37 DEG C of constant-temperature tables；Treat that OD value reaches 0.8-1 scope, by shaking table
Temperature is adjusted to 25 DEG C, adds 1mM IPTG abduction delivering, constant temperature incubated overnight；
The antibacterial expressed by above-mentioned albumen is centrifugal in refrigerated centrifuge, makes thalline separate with culture medium, centrifugal condition:
12000rpm, 4 DEG C, centrifugal 1.0-3.0min；Thalline A buffer solution after being centrifuged, A buffer is 20mM imidazoles,
20mM sodium phosphate, 0.5M sodium chloride, pH is 7.4；Bacterial suspension is put into ultrasonic cell disruption instrument carries out cell breakage,
Albumen can be discharged and albumen can be dissolved in A buffer；Bacterial suspension need to be put in ice bath time ultrasonic, in case temperature
Too high cause albuminous degeneration；The suspension recentrifuge that will have crushed, makes cell debris separate with protein solution, centrifugal condition:
14000rpm, 4 DEG C, 30-50min；Collecting supernatant, this is crude protein solution；After being filtered by crude protein, pass through liquid chromatograph
It is further purified；By lyophilizing, obtain white fluffy solid；This solid is put in-20 DEG C of Refrigerator stores, by claiming during use
Weight method demarcates concentration.
(3)α-Fe2O3The preparation of nano material
1., recombined collagen and the preparation of Iron(III) chloride hexahydrate homogeneous mixture solotion；
In 1ml water, add 1-50mg Iron(III) chloride hexahydrate and 0-10mg collagen solids, mix homogeneously, slowly stir
After mixing 5-90min, obtain pale yellow transparent and uniform liquid；
2. hydrothermal reaction kettle, is utilized to prepare nanometer alpha-Fe2O3；
Gained mixed liquor is poured in 5ml hydrothermal reaction kettle, puts into Muffle furnace and be warming up to the speed of 3-18 DEG C/min
120-200 DEG C, and react 1-15hrs at such a temperature；
3., nano material prepared by purification kept dry；
After hydrothermal reaction kettle is cooled to room temperature, by product by centrifugation, centrifugal condition is 1200r, supernatant discarded
Liquid, leaves solid；And use deionized water dispersing solid, then centrifugal purification 3-5 time, it is dried in 50-80 DEG C of thermostatic drying chamber.
Wherein, the purity of the recombined collagen that step obtains the most after purification reaches 95%.
Wherein, the collagen solids addition described in step (2) is 1mg, and collagen protein quality mark is
0.1wt%.
Wherein, the Iron(III) chloride hexahydrate solids loading content described in step (2) is 16mg, the concentration distribution of ferrum (III)
From 0.06mol/L.
Wherein, the Iron(III) chloride hexahydrate described in step (2) and collagen protein mixed liquor are slowly stirred the time and are
30min。
Wherein, the mixed liquor described in step (2) is warming up to 160 DEG C with the speed of 5 DEG C/min in Muffle furnace, and at this
At a temperature of react 10hrs.
The above is the details of an exemplary case study on implementation of the present invention.For a person skilled in the art,
The present invention can have various modifications and variations according to concrete preparation condition in actual application, is not limited to this
Bright.All should be included within the scope of the present invention within the spirit and principles in the present invention, should be by claim
Any reference be considered as limiting involved claim.
Claims (6)
1. prepare Fe with collagen protein for biomineralization template for one kind2O3The method of nanoparticle, it is characterised in that include walking as follows
Rapid:
(1) biology gene engineering technology is utilized to prepare recombined collagen
1. the sequence of recombined collagen, is determined；
The sequence of recombined collagen is:
GSPGLPGPRGEQGPTGPTGPAGPRGLQGLQGLQGERGEQGPTGPAGPRGLQGERGEQGPTGLAGKAGEAGAKG
ETGPAGPQGPRGEQGPQGLPGKDGEAGAQGRPGKRGKQGQKGEKGEPGTQGAKGDRGETGPVGPRGERGEAGPAGKD
GERGFPGERGVEGQNGQDGLPGKDGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQDGKDGLPGKDGKDGLPGK
DGKDGQPGKPGKYGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP, this recombined collagen possesses good triple helices
Structure, hot temperature is close to 37 DEG C；There is the binding site GERGFPGERGVE of integrin, can adhere well to cell；
There is the binding site GRPGKRGKQGQK of heparin, can be with Heparin-binding；
2., the nucleic acid of composite coding recombined collagen；
The nucleic acid of composite coding step 1. recombined collagen, builds the plasmid importing above-mentioned nucleic acid, and by Plastid transformation large intestine
Bacillus BL21-DE3 bacterial strain；
3., the preparation of recombined collagen and purification；
It is placed in ice bath thawing by freezing the competent escherichia coli cell at-80 DEG C, competent cell is mixed with 3-5ul plasmid
Closing, mixture places into 90s in 42 DEG C of water-baths in ice bath, then places into 2min in ice bath after 30min；At above-mentioned mixture
The middle addition 1ml LB culture medium without antibiotic, then it is positioned over 1hrs in 37 DEG C of constant-temperature tables, then at 4 DEG C, 4000rpm bar
Under part, centrifugal 20min, discards the supernatant；Make antibacterial after Eddy diffusion in remaining culture liq, culture fluid even spread is arrived
On the AMP culture plate of 37 DEG C, it is placed in incubated overnight in 37 DEG C of constant-temperature tables；Next day, the preferable bacterium colony of picking growing way was put into
In the 100ml LB fluid medium containing antibiotic, constant-temperature table overnight carries out Zengjing Granule；Antibacterial by 100ml incubated overnight
Pour in 1L LB culture medium, 37 DEG C of constant-temperature tables continue amplification cultivation；Treat that OD value reaches 0.8-1 scope, by shaking table temperature
It is adjusted to 25 DEG C, adds 1mM IPTG abduction delivering, constant temperature incubated overnight；
The antibacterial expressed by above-mentioned albumen is centrifugal in refrigerated centrifuge, makes thalline separate with culture medium, centrifugal condition:
12000rpm, 4 DEG C, centrifugal 1.0-3.0min；Thalline A buffer solution after being centrifuged, A buffer is 20mM imidazoles,
20mM sodium phosphate, 0.5M sodium chloride, pH is 7.4；Bacterial suspension is put into ultrasonic cell disruption instrument carries out cell breakage,
Albumen can be discharged and albumen can be dissolved in A buffer；Bacterial suspension need to be put in ice bath time ultrasonic, in case temperature
Too high cause albuminous degeneration；The suspension recentrifuge that will have crushed, makes cell debris separate with protein solution, centrifugal condition:
14000rpm, 4 DEG C, 30-50min；Collecting supernatant, this is crude protein solution；After being filtered by crude protein, pass through liquid chromatograph
It is further purified；By lyophilizing, obtain white fluffy solid；This solid is put in-20 DEG C of Refrigerator stores, by claiming during use
Weight method demarcates concentration.
(2)α-Fe2O3The preparation of nano material
1., recombined collagen and the preparation of Iron(III) chloride hexahydrate homogeneous mixture solotion；
In 1ml water, add 1-50mg Iron(III) chloride hexahydrate and 0-10mg collagen solids, mix homogeneously, be slowly stirred 5-
After 90min, obtain pale yellow transparent and uniform liquid；
2. hydrothermal reaction kettle, is utilized to prepare nanometer alpha-Fe2O3；
Gained mixed liquor is poured in 5ml hydrothermal reaction kettle, puts into Muffle furnace and be warming up to 120-with the speed of 3-18 DEG C/min
200 DEG C, and react 1-15hrs at such a temperature；
3., nano material prepared by purification kept dry；
After hydrothermal reaction kettle is cooled to room temperature, by product by centrifugation, centrifugal condition is 1200rpm, abandoning supernatant,
Leave solid；And use deionized water dispersing solid, then centrifugal purification 3-5 time, it is dried in 50-80 DEG C of thermostatic drying chamber.
One the most according to claim 1 prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle,
It is characterized in that: the purity of the recombined collagen that step obtains the most after purification reaches more than 95%.
One the most according to claim 1 prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle,
It is characterized in that: the collagen solids addition described in step (2) is 0.1-5mg, collagen protein quality mark is 0.01-
0.5wt%.
One the most according to claim 1 prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle,
It is characterized in that: the Iron(III) chloride hexahydrate solids loading content described in step (2) is 2.7-27mg, the concentration of ferrum (III) is divided
Cloth is from 0.01 to 0.1mol/L.
One the most according to claim 1 prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle,
It is characterized in that: it is 20-that the Iron(III) chloride hexahydrate described in step (2) and collagen protein mixed liquor are slowly stirred the time
50min。
One the most according to claim 1 prepares Fe with collagen protein for biomineralization template2O3The method of nanoparticle,
It is characterized in that: the mixed liquor described in step (2) is warming up to 140-180 DEG C with the speed of 3-10 DEG C/min in Muffle furnace,
And react 6-12hrs at such a temperature.
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