CN105012342B - A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application - Google Patents
A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application Download PDFInfo
- Publication number
- CN105012342B CN105012342B CN201510271613.3A CN201510271613A CN105012342B CN 105012342 B CN105012342 B CN 105012342B CN 201510271613 A CN201510271613 A CN 201510271613A CN 105012342 B CN105012342 B CN 105012342B
- Authority
- CN
- China
- Prior art keywords
- pom
- molybdenum
- peptide
- polypeptide
- preparation
- 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.)
- Expired - Fee Related
Links
Abstract
The present invention relates to metal nano material preparation field, a kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application is specifically disclosed.The molybdenum multi-metal oxygen silicate nanometer of the polypeptide functionalization is to modify more molybdenum oxygen hydrochlorate Mo POM of vanadium doping through A β target polypeptides.Aggregation and the Zn of A β itself can effectively be inhibited2+The fibrosis of induction, meanwhile, measured degradation capability is also shown for the A betas formed；In addition, also there is the good ability through blood-brain barrier, it can be as a kind of drug of potential treatment alzheimer's disease.
Description
Technical field
The present invention relates to metal nano material preparation fields, and in particular to a kind of molybdenum multi-metal oxygen hydrochlorate of polypeptide functionalization
Nanometer and its preparation method and application.
Background technology
Alzheimer disease (AD), i.e. senile dementia are a kind of using memory and cognition dysfunction as main feature
Progressive neurodegenerative disease.AD is mainly in old group, and the illness rate of AD is about 5-10% in 60 years old or more crowd, and 85
Year old or more illness rate in crowd be up to 40-50%.Aggravation and shortage with the aging of population is effectively predicted and is controlled
The means for the treatment of, AD patient populations are increasing always, therefore AD has become after heart disease, cancer, apoplexy, leads to the elderly
The dead the fourth-largest cause of disease.Numerous studies show that the brain of AD patient generally all shows following pathological characters：Big brain volume
It reduces, the neuron and decrease of synapses of hippocampus and neopallium, the senile plaque that amyloid beta (A β) aggregation is formed extracellularly occur
And the neurofibrillary tangles that Intracellular phosphorylation Tau albumen is formed.Wherein, in terms of the pathogenetic researchs of AD, at present
Most scholars all think that the metabolic disorder of A β causes A β aggregation depositions to form generation of the amyloid beta spot in AD in brain
It plays a crucial role in development.
A β, thus in physiological conditions can be spontaneous rich in multiple hydrophobic amino acids, solubility is extremely low in aqueous solution
Form the aggregation of variform, the oligomers such as formed by 2-6 polypeptide aggregations, before this forms amyloid fiber
Intermediary, is secondly the insoluble fiber to form beta sheet lamellar structure, this is the Main Morphology of A β plaque block.These are solvable
Property oligomer and filamentous A β there is very strong neurotoxicity, can with the apoptosis of inducing nerve cell, therefore it is effective prevent or
Aggregations of the A β in intracerebral is reduced, is an available strategy for treating AD.
Research also found that A beta-aggregations formation fiber is affected by many factors, and wherein metal ion is that induction A β form aggregation
One of an important factor for body, detects the Zn of high concentration in the amyloid plaque of AD brains2+、Cu2+And Fe3+.Research shows that this
It is closely related that a kind of transition metal zinc, copper, iron etc. not only can induce neurotoxicity of the A β formation β-pleated sheets also with A β：Copper ion can
It being combined with the histidine on A beta polypeptides, forms it into histidine bridge, this Cu-A beta composites have very strong neurotoxicity,
And on the other hand, the Cu with oxidation-reduction quality2+It is catalyzed H after being combined with A β2O2The formation of isoreactivity oxygen.Excessive active oxygen oozes
It can lead to the oxidative damages such as DNA damage, lipid peroxidation through cell membrane；Zn2+Soluble A β are made to be precipitated as resistance to enzymolysis rapidly
Amyloid aggregation.
Invention content
The technical problem to be solved by the invention is to provide how golden a kind of molybdenum that can inhibit the polypeptide functionalization of A beta-aggregations is
Belong to oxygen silicate nanometer.
Above-mentioned technical problem to be solved by this invention, is resolved by the following technical programs：
A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization (is write a Chinese character in simplified form：Peptide@Mo-POM), it is by vanadium doping
More molybdenum oxygen hydrochlorate Mo-POM are modified through A β target polypeptides.
The molecular formula of more molybdenum oxygen hydrochlorate Mo-POM of the vanadium doping is (H2O)3(NH4)18[Mo57V6(NO3)6O183
(H2O)183]·56H2O；
Preferably, the A β target polypeptides are Ac-QKLVFF-NH2。
A kind of preparation method of the molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization, comprises the following steps：By vanadium doping
More molybdenum oxygen hydrochlorate Mo-POM solution and Ac-QKLVFF-NH2Polypeptide solution mixes, and stirs 10~60min at room temperature, then 0~
10 DEG C of ageings 6~for 24 hours, finally by mixed solution centrifugation, ultrasound, the molybdenum multi-metal oxygen acid for washing, being drying to obtain polypeptide functionalization
Salt nanometer (is write a Chinese character in simplified form：Peptide@Mo-POM).
Preferably, a concentration of 100~500 μM of more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping, Ac-QKLVFF-NH2It is more
A concentration of 10~50mM of peptide solution.
It is highly preferred that a concentration of 100~300 μM of more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping, Ac-QKLVFF-NH2
A concentration of 10~30mM of polypeptide solution.
Most preferably, a concentration of 200 μM of more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping, Ac-QKLVFF-NH2Polypeptide
A concentration of 20mM of solution.
Preferably, the more molybdenum oxygen hydrochlorate Mo-POM solution and Ac-QKLVFF-NH of vanadium doping2The volume ratio of polypeptide solution is 5
~10:1.
Most preferably, the more molybdenum oxygen hydrochlorate Mo-POM solution and Ac-QKLVFF-NH of vanadium doping2The volume ratio of polypeptide solution
It is 10:1.
Preferably, more molybdenum oxygen hydrochlorate Mo-POM solution are more molybdenum oxygen hydrochlorate Mo-POM aqueous solutions, with Ac-QKLVFF-NH2It is more
Peptide solution is Ac-QKLVFF-NH2Polypeptid solution.
Preferably, the room temperature is 15~30 DEG C.
It is prepared by more molybdenum oxygen hydrochlorate Mo-POM of vanadium doping or the molybdenum multi-metal oxygen silicate nanometer of above-mentioned polypeptide functionalization
Treat the application in the drug of alzheimer's disease.
More molybdenum oxygen hydrochlorate Mo-POM of vanadium doping or the molybdenum multi-metal oxygen silicate nanometer of aforementioned polypeptides functionalization are poly- as A β
Collect the application of inhibitor or A beta inhibitor.
More molybdenum oxygen hydrochlorate Mo-POM of vanadium doping or the molybdenum multi-metal oxygen silicate nanometer of aforementioned polypeptides functionalization are as drug
The application of carrier.
Advantageous effect：(1) present invention discover that more molybdenum oxygen hydrochlorate Mo-POM of vanadium doping have the A for inhibiting metal ion induction
The ability of beta-aggregation and fibrosis, while the neurotoxicity of A betas can be effectively reduced, treatment alzheimer's disease can be used as
Drug use；(2) on this basis, the present invention by with targeting brain A β abilities polypeptide A c-QKLVFF-NH2 to Mo-
POMs is modified, and the molybdenum multi-metal oxygen silicate nanometer Peptide@Mo-POM of a novel polypeptide functionalization have been synthesized；Energy
Enough aggregations for effectively inhibiting A β itself and Zn2+The fibrosis of induction, meanwhile, the A betas formed are also shown good
Good degradation capability；It being found in cell experiment research in vitro, Peptide@Mo-POM can be effectively increased the activity of PC12 cells,
It plays a protective role to cell, and can effectively reduce A betas to PC12 apoptosis-inducing abilities；In addition, passing through structure
BBB external models are the study found that Peptide@Mo-POM can be used as a kind of latent with the good ability through blood-brain barrier
Treatment alzheimer's disease drug.
Description of the drawings
Fig. 1 is the transmission electron microscope picture of Mo-POM and Peptide@Mo-POM.
Fig. 2 is the aggregation extent transmission electron microscope pictures of A β 40 under different conditions.
Fig. 3 is the aggregation extent ThT fluorescence curve figures of A β 40 under different conditions.
Fig. 4 is the aggregation extent ThT turbidity figures of A β 40 under different conditions.
Fig. 5 is inhibition and the palliating degradation degree transmission electron microscope picture of 40 fibrosis of A β.
Fig. 6 is 40 fibers of A β to PC12 cell activity influence diagrams.
Fig. 7 is Peptide@Mo-POM to PC12 cell activity influence diagrams.
Fig. 8 is that laser co-focusing detects fluorogram in PC12 cells.
Specific implementation mode
The present invention is explained further below in conjunction with specific embodiment, but embodiment does not do any type of limit to the present invention
It is fixed.
More molybdenum oxygen hydrochlorate Mo-POM (following shorthand is at Mo-POM) of vanadium doping described in following embodiment, reference literature
Dante Gatteschi.Giant Clusters with Unusual Electronic and Magnetic
Structures Due to Open Shell Metal Centers Embedded Far Apart from Each
Other:Spin Frustration and AntisymmetricExchange.Inorg.Chem.1996,35,1926-1934
In preparation method be prepared.
Ac-QKLVFF-NH in following embodiment2Polypeptide (being abbreviated as Peptide) is biochemical (Shanghai, China) purchased from gill.
The preparation of 1 Peptide@Mo-POM of embodiment
By the Ac-QKLVFF-NH of 200 μM of Mo-POM aqueous solutions and 100 μ L 20mM of 1mL2Polypeptid solution mixes, room
30min is stirred under warm (25 DEG C), 8h is then aged at 4 DEG C, finally mixed solution is centrifuged, ultrasound, washs, be drying to obtain
Peptide@Mo-POM。
Mo-POM and Peptide@Mo-POM is soluble in water, then it is added drop-wise to progress TEM characterizations in copper mesh.Fig. 1 is Mo-
The transmission electron microscope picture of POM and Peptide@Mo-POM, it can be seen that Mo-POM and Peptide@Mo-POM are spherical state, grain size
Respectively 80 ± 5nm and 110 ± 6nm, particle diameter distribution is uniform in the solution.
The preparation of 2 Peptide@Mo-POM of embodiment
By the Ac-QKLVFF-NH of 500 μM of 100 μ L 10mM of Mo-POM aqueous solutions of 1mL2Polypeptid solution mixes, room temperature
10min is stirred under (25 DEG C), 12h is then aged at 6 DEG C, finally mixed solution is centrifuged, ultrasound, washs, be drying to obtain
Peptide@Mo-POM。
The preparation of 3 Peptide@Mo-POM of embodiment
By the Ac-QKLVFF-NH of 100 μM of Mo-POM aqueous solutions and 100 μ L 50mM of 1mL2Polypeptid solution mixes, room
90min is stirred under warm (25 DEG C), 12h is then aged at 2 DEG C, finally mixed solution is centrifuged, ultrasound, washs, be drying to obtain
Peptide@Mo-POM。
4 Peptide@Mo-POM of embodiment inhibit A β 40 to assemble transmission electron microscope experiment
Aggregation extent and fibrosis of the present embodiment by transmission electron microscope observing A β 40 under different conditions.Setting is real
It is A β 40+Zn to test group2+、Aβ40+Zn2++ Mo-POM and A β 40+Zn2++ Peptide@Mo-POM, wherein A β 40 are 20 μM, Zn2+For
40 μM, reaction final volume is 100 μ L, Mo-POM the and Peptide@Mo-POM of same concentrations is added, in 37 DEG C of constant incubators
Cultivate respectively for 24 hours, 48h.Incubation finishes, and mixing liquid is added drop-wise on copper mesh after taking 10 μ L to be incubated, and is contaminated immediately with 0.1% phosphotungstic acid
Color sucks extra dye liquor with filter paper, and finally sample is taken pictures in observation on transmission electron microscope.The results are shown in Figure 2, in Zn2+It lures
After leading lower be incubated 48 hours, 40 aggregation extents of A β are apparent, can clearly see fibrous-network structure, say Zn2+It is fine for A β 40
One of main inducing of dimensionization.Still occur fibrous aggregation individual A β 40 after Mo-POM nanometer are added, but and Zn2+
Induced aggregation degree compares opposite weaken, it can be seen that A beta shape structures are less and degree of scatter is high, and do not occur
Apparent agglomeration.But we equally observe that most Mo-POM nano-disperseds around A betas, illustrate nanometer
Compatibility between fiber is relatively low, the Mo-POM nanometers of formation that can not be effectively combined to inhibit fiber with A betas.
But in the presence of Peptide@Mo-POM, A β 40 form the A beta shape structures that major part is all shorter after being incubated for 24 hours, and
And there is a degree of agglomeration.After being incubated 48h, the A β staple fibers of reunion are disintegrated, and are formed more spherical
Particle and oligomer, wherein being mingled with a small amount of staple fiber.This shows that Peptide@Mo-POM and A betas have good affine work
With, and after being attached on fiber, by stable protein, its natural structure forms unformed monomer or oligomer, because
This Peptide@Mo-POM can be used as A beta-aggregation inhibitor, and the aggregation extent of A β is reduced with this, reaches treatment alzheimer
Disease acts on.(note：The Peptide@Mo-POM that the present embodiment uses are the Peptide@Mo-POM that embodiment 1 is prepared.)
5 Peptide@Mo-POM of embodiment inhibit A β 40 to assemble ThT fluorescence experiments
The dynamic characteristic that the present embodiment is assembled using ThT fluorescent tests research A β 40, because ThT dyestuffs being capable of specificity
Stable bond amyloid polypeptide fiber, fibre weight is more, stronger in conjunction with the fluorescence after ThT.Finally, glimmering by JASCO FP6500
Light spectrophotometer detects extent of polymerization.It is grouped by following design experiment：Aβ40、Aβ40+Zn2+、Aβ40+Zn2++Peptide、A
β40+Zn2++ Mo-POM and A β 40+Zn2++Peptide@Mo-POM.Wherein, 40 a concentration of 40 μM of A β, Zn2+A concentration of 80 μM,
The Mo-POM and a concentration of 5 μ g/mL of Peptide@Mo-POM.All samples are shaken to 10s on the oscillator makes it mix well
37 DEG C of constant incubators are placed on to be incubated.In the different times (0,1,2,3,4,5,6 day) of the process of incubation, sample part equivalent is chosen
40 solution of A β be added ThT solution.Detection mixes sample under conditions of excitation wave 450nm, transmitted wave 485nm after mixing well
Fluorescence intensity, experiment in triplicate, and is averaged as final test result.
Experimental result is as shown in figure 3, A β 40 itself incubations also will produce apparent aggtegation, because of ThT fluorescence intensities
It with the increase of incubation time, was exponentially increased at second day to the 5th day, fluorescence intensity regional stability after six days, in flat
The platform phase.And Zn is added2+Afterwards, the aggregation extent of A β 40 is dramatically increased compared with self assemble, illustrates Zn2+It can promote the aggregation of A β 40.
Zn2+In the presence of, Peptide or Mo-POM is added and is incubated jointly, ThT fluorescence intensity decreases to some degree, explanation
Polypeptide and Mo-POM have certain ability for inhibiting 40 fibrosis of A β.When Peptide@Mo-POM are added, fluorescence intensity is aobvious
It writes and declines, illustrate that it can effectively be combined with A β 40, prevent itself aggregation and fibrosis.This may be due to peptide modified Mo-
After POM, due to the A β targetings of polypeptide, Peptide@Mo-POM can be combined effectively with A betas, destroy the shape of beta sheet structure
At to greatly increase the ability that Mo-POM inhibits A beta-aggregations and fibrosis.(note：The Peptide@that the present embodiment uses
Mo-POM is the Peptide@Mo-POM that embodiment 2 is prepared.)
6 Peptide@Mo-POM of embodiment inhibit A β 40 to assemble results of turbidity
Turbidity is the indicator reaction of 40 solution optical density of A β variation, it can indicate the total amount that all types of A β 40 assemble,
Including various dimers, oligomer and amorphous aggregation etc..Take respectively configured good 50 μ LA β, 40 mother liquors be placed in 1mL from
Heart pipe presses above-mentioned experimental setup control group, experimental group respectively, and the liquor zinci chloridi and various concentration of 4 μ L is added in experimental group
Mo-POM and Peptide@Mo-POM (5 μ g/mL, 10 μ g/mL, 20 μ g/mL), it is 100 μ L that buffer solution to total volume, which is then added,
It mixes well.The sample configured is placed in 37 DEG C and is incubated 2 days.Buffer solution is finally added in each centrifuge tube to total volume 1000
μ L, mixing, with UV spectrophotometer measuring absorbance (405nm).
As a result such as Fig. 4, as addition Zn2+Afterwards, the turbidity of 40 solution of A β obviously rises, and illustrates Zn2+It can aggravate A betas
Degree.And after Mo-POM the or Peptide@Mo-POM of various concentration are added, it is found that with the increasing that nanometer concentration is added
Add, the turbidity of 40 solution of A β is then gradually reduced, and illustrates that Mo-POM and Peptide@Mo-POM can effectively inhibit the aggregation of A β 40
And fibrosis, and Peptide@Mo-POM show better inhibition.(note：What the present embodiment used
Peptide@Mo-POM are the Peptide@Mo-POM that embodiment 3 is prepared.)
The inhibition of 7 A betas of embodiment and degradation experiment
The present embodiment studies inhibition and degradation of Mo-POM the and Peptide@Mo-POM to A betas.Inhibiting fiber
Change in experiment, first by the A β solution and Zn of Fresh2+Solution mixes, and after 5min, is separately added into Mo-POM and Peptide@Mo-
POM is incubated 72h jointly.In Degrading experiment, first by Fresh A β solution and Zn2+Solution mixes, and is incubated 48h jointly, is formed
After fiber, adds Mo-POM and Peptide@Mo-POM and be incubated 72h jointly.First, we are seen using TEM transmission electron microscopes
It surveys, as shown in figure 5, (a) is to inhibit to test, it is (b) Degrading experiment.It can be found that in inhibiting to test (a), Mo-POM and Zn2+
Common to be incubated, A beta structures are reduced, but fibre structure still remains, and mutually winding, and most Mo-POM is then
It is gathered into larger nano particle, is scattered and is distributed in around fiber.Illustrate that the compatibility of Mo-POM and A betas is not high, inhibits
Effect is bad.And after Peptide@Mo-POM are added, A betas substantially reduce, and only exist a small amount of shorter oligomer, explanation
The good abilities for inhibiting A betas of Peptide@Mo-POM, most A β still exist with monomeric form, only on a small quantity
Assembled.Likewise, in Degrading experiment (b), A β and Zn2+After common incubation 48h, a large amount of fiber is formd, and
There is the phenomenon that winding of reuniting.Mo-POM is added after 48h, A betas reduce but still high-visible more longer fiber.
And similar with the above results, most of Mo-POM is only distributed across surrounding there is no being combined with A betas.Work as addition
After Peptide@Mo-POM are incubated jointly, it is seen that a large amount of fiber is broken, the shorter small fiber of formation length.Result above
Illustrate, Peptide@Mo-POM not only have the ability for inhibiting A beta monomers to form fiber, but also with the energy of degradation A betas
Power.(note：The Peptide@Mo-POM that the present embodiment uses are the Peptide@Mo-POM that embodiment 1 is prepared.)
8 A β of embodiment, 40 fiber-induction PC12 Apoptosis
The present embodiment has studied the guarantor of 40 fiber-induction PC12 Apoptosis of A β and Peptide@Mo-POM to nerve cell
Shield acts on.Using PC12 cells as cell model, exception and the alzheimer's disease of PC12 cells have close pass
System, is the Main Patterns cell of in vitro study AD.By mtt assay to itself being incubated 72h A β 40 and in Zn2+Induction is lower to be incubated
72h A β 40, also individual Zn2+, Peptide, Mo-POM and Peptide@Mo-POM comment the cytotoxicity of PC12
Estimate.As a result it such as Fig. 6, is added after being individually incubated the 40 function cells 48h of A β of 72h, cell activity drops to 60% or so；In Zn2+Altogether
Under being acted on the A β 40 being incubated, toxicity dramatically increases, and cell activity is reduced to 50% or less.Illustrate in Zn2+Under induction, A β 40 are poly-
Collection effect aggravation, the A betas of formation have prodigious neurotoxicity.And the Zn being individually added into2+, Peptide, Mo-POM and
Peptide@Mo-POM do not have overt toxicity, and cell activity is unaffected, all 90% or more.Further to study Peptide@
Protective effects of the Mo-POM to PC12 cells, in Zn2+In the presence of, be separately added into Peptide, Mo-POM and
Peptide@Mo-POM and A β 40 jointly be incubated 72h after, then with PC12 cytosiies.The results are shown in Figure 7, Peptide and Mo-
POM has certain protective effect to PC12 cells, with Zn2+A β 40 are compared under induction, and cell activity is increased separately by 38.9%
To 43.9% and 52.8%.And after Peptide@Mo-POM are added, PC12 cell activity dramatically increases, and reaches 75% or more.With
Upper result explanation, Peptide@Mo-POM have the function of it is good protect PC12 from 40 toxicity of A β, can effectively reduce Zn2+It lures
Lead the cytotoxicity of 40 fibrosis of A β generation.(note：The Peptide@Mo-POM that the present embodiment uses are that embodiment 1 is prepared
Peptide@Mo-POM.)
9 Peptide@Mo-POM of embodiment penetrate the ability of blood-brain barrier BBB
The present embodiment penetrates blood-brain barrier using bEnd.3 as blood-brain barrier model, using Transwell experimental study nanometers
Ability.
Build BBB external models：BEnd.3 cells are inoculated on the upper layers Transwell, initial density is 1 × 105A cell/
Hole.Lower layer be inoculated with PC12 cells, after cell is adherent in the upper layers Transwell be added fluorescent marker PeptideFAM and
Mo-POM nanometers of PeptideFAM@, after cultivating 3 days, with the fluorescence of nanometer in laser co-focusing detection lower layer PC12 cells.As a result
As shown in figure 8, the fluorescence detected in PC12 cells after individual PeptideFAM incubations are added in the upper layers Transwell is very
It is few, illustrate that individual PeptideFAM penetrates the poor ability of blood-brain barrier, and for PeptideFAM Mo-POM,
The upper layers Transwell be incubated 3 days after, detect very strong fluorescence in lower layer's PC12 cells, this explanation with individually
PeptideFAM is compared, and Peptide@Mo-POM can effectively improve the ability that polypeptide penetrates blood-brain barrier.(note：The present embodiment
The Peptide@Mo-POM used are the Peptide@Mo-POM that embodiment 1 is prepared.)
Claims (7)
1. a kind of molybdenum multi-metal oxygen hydrochlorate of polypeptide functionalization, which is characterized in that be by more molybdenum oxygen hydrochlorate Mo-POM of vanadium doping
It is modified through A β target polypeptides；The molecular formula of more molybdenum oxygen hydrochlorate Mo-POM of the vanadium doping is (H2O) 3 (NH4) 18
[Mo57V6(NO3)6O183(H2O)183]·56H2 O；The A β target polypeptides are Ac-QKLVFF-NH2.
2. the preparation method of the molybdenum multi-metal oxygen hydrochlorate of polypeptide functionalization described in claim 1, which is characterized in that comprising as follows
Step：More molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping are mixed with Ac-QKLVFF-NH2 polypeptide solutions, at room temperature stir 10~
60min, the then ageing 6~for 24 hours at 0~10 DEG C, finally by mixed solution centrifugation, ultrasound, wash, be drying to obtain polypeptide functionalization
Molybdenum multi-metal oxygen hydrochlorate.
3. preparation method according to claim 2, which is characterized in that more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping
A concentration of 100~500 μM, a concentration of 10~50mM of Ac-QKLVFF-NH2 polypeptide solutions.
4. preparation method according to claim 3, which is characterized in that more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping
A concentration of 100~300 μM, a concentration of 10~30mM of Ac-QKLVFF-NH2 polypeptide solutions.
5. preparation method according to claim 4, which is characterized in that more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping
A concentration of 200 μM, a concentration of 20mM of Ac-QKLVFF-NH2 polypeptide solutions.
6. preparation method according to claim 2, which is characterized in that more molybdenum oxygen hydrochlorate Mo-POM solution of vanadium doping and
The volume ratio of Ac-QKLVFF-NH2 polypeptide solutions is 5~10:1.
7. application of the molybdenum multi-metal oxygen hydrochlorate of polypeptide functionalization described in claim 1 as pharmaceutical carrier.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510271613.3A CN105012342B (en) | 2015-05-25 | 2015-05-25 | A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510271613.3A CN105012342B (en) | 2015-05-25 | 2015-05-25 | A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN105012342A CN105012342A (en) | 2015-11-04 |
| CN105012342B true CN105012342B (en) | 2018-08-28 |
Family
ID=54402888
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510271613.3A Expired - Fee Related CN105012342B (en) | 2015-05-25 | 2015-05-25 | A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN105012342B (en) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3532289B1 (en) * | 2016-10-26 | 2024-03-06 | Emory University | Polyoxometalate complexes and uses in managing cancer |
| CN114469992B (en) * | 2021-11-18 | 2022-11-08 | 中山大学附属第五医院 | Application of molybdenum-based polyoxometallate cluster in preparation of medicine for treating ulcerative colitis |
| CN115300527B (en) * | 2022-03-30 | 2023-09-26 | 河北医科大学 | Application of chiral heteropolyacid enantiomer-selective inhibition of beta-amyloid peptide aggregation in preparation of drug for treating Alzheimer's disease |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102304152A (en) * | 2011-04-20 | 2012-01-04 | 南开大学 | Molybdenum-containing polyoxometalate and adamantane hybrid compound and preparation method thereof |
| CN102491997A (en) * | 2011-11-25 | 2012-06-13 | 南开大学 | Cholic acid-molybdenum polyoxometallate-cholic acid compound and synthetic method |
-
2015
- 2015-05-25 CN CN201510271613.3A patent/CN105012342B/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102304152A (en) * | 2011-04-20 | 2012-01-04 | 南开大学 | Molybdenum-containing polyoxometalate and adamantane hybrid compound and preparation method thereof |
| CN102491997A (en) * | 2011-11-25 | 2012-06-13 | 南开大学 | Cholic acid-molybdenum polyoxometallate-cholic acid compound and synthetic method |
Non-Patent Citations (1)
| Title |
|---|
| Mo polyoxometalate nanoclusters capable of inhibiting the aggregation of Aβ-peptide associated with Alzheimer’s disease;Qingchang Chen et al.;《The Royal Society of Chemistry》;20141231;第6卷(第12期);文章摘要 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN105012342A (en) | 2015-11-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Darvishi et al. | Advances in the sensing and treatment of wound biofilms | |
| Liu et al. | Quercetin-modified gold-palladium nanoparticles as a potential autophagy inducer for the treatment of Alzheimer's disease | |
| Halbreich et al. | Biomedical applications of maghemite ferrofluid | |
| Kuang et al. | A novel nanosystem realizing curcumin delivery based on Fe3O4@ carbon dots nanocomposite for Alzheimer’s disease therapy | |
| CN105012342B (en) | A kind of molybdenum multi-metal oxygen silicate nanometer of polypeptide functionalization and its preparation method and application | |
| Lee et al. | PEGylated bilirubin-coated iron oxide nanoparticles as a biosensor for magnetic relaxation switching-based ROS detection in whole blood | |
| Skaat et al. | Acceleration and inhibition of amyloid-β fibril formation by peptide-conjugated fluorescent-maghemite nanoparticles | |
| Shin et al. | Membrane potential mediates the cellular binding of nanoparticles | |
| Sun et al. | Chiral penicillamine-modified selenium nanoparticles enantioselectively inhibit metal-induced amyloid β aggregation for treating Alzheimer’s disease | |
| Özel et al. | Effect of cerium oxide nanoparticles on intestinal serotonin in zebrafish | |
| Zou et al. | Toxicity of silver nanoparticle in rat ear and BALB/c 3T3 cell line | |
| Saleh et al. | Tagged halloysite nanotubes as a carrier for intercellular delivery in brain microvascular endothelium | |
| Gao et al. | Y2O3 nanoparticles caused bone tissue damage by breaking the intracellular phosphate balance in bone marrow stromal cells | |
| Wang et al. | Construction of perfluorohexane/IR780@ liposome coating on Ti for rapid bacteria killing under permeable near infrared light | |
| CN103948935B (en) | Suppress A β and metal ion induces nano-particle and preparation and the application of its aggregation | |
| Katagiri et al. | Variable on-demand release function of magnetoresponsive hybrid capsules | |
| BR112019012984A2 (en) | nanoparticles for use to treat a neuronal disorder | |
| CN105399680B (en) | Chiral more PCBN tools and preparation method and application | |
| Zheng et al. | Flexible modulation of cellular activities with cationic photosensitizers: insights of alkyl chain length on reactive oxygen species antimicrobial mechanisms | |
| Tram et al. | Bacteria‐Responsive Self‐Assembly of Antimicrobial Peptide Nanonets for Trap‐and‐Kill of Antibiotic‐Resistant Strains | |
| Xu et al. | The Behavior of Carbonized Polymer Dots at the Nano‐Bio Interface and Their Luminescent Mechanism: A Physical Chemistry Perspective | |
| Liu et al. | Fe3O4 magnetic nanoparticles ameliorate albumin-induced tubulointerstitial fibrosis by autophagy related to Rab7 | |
| JP2020111562A (en) | Composite amphipathic peptide nanomicelle, and production method and application thereof | |
| Yuan et al. | A diselenide bond-containing ROS-responsive ruthenium nanoplatform delivers nerve growth factor for Alzheimer's disease management by repairing and promoting neuron regeneration | |
| Yang et al. | l‐Arginine‐Modified CoWO4/FeWO4 S‐Scheme Heterojunction Enhances Ferroptosis against Solid Tumor |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant | ||
| CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20180828 |
|
| CF01 | Termination of patent right due to non-payment of annual fee |