CN110343182A - A kind of aldehyde group modified method based on substrate surface and the method for verifying its proteopexy effect - Google Patents
A kind of aldehyde group modified method based on substrate surface and the method for verifying its proteopexy effect Download PDFInfo
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- CN110343182A CN110343182A CN201910599807.4A CN201910599807A CN110343182A CN 110343182 A CN110343182 A CN 110343182A CN 201910599807 A CN201910599807 A CN 201910599807A CN 110343182 A CN110343182 A CN 110343182A
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
- C07K17/02—Peptides being immobilised on, or in, an organic carrier
- C07K17/08—Peptides being immobilised on, or in, an organic carrier the carrier being a synthetic polymer
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
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- C07K17/14—Peptides being immobilised on, or in, an inorganic carrier
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- G01N21/62—Systems in which the material investigated is excited whereby it emits light or causes a change in wavelength of the incident light
- G01N21/63—Systems in which the material investigated is excited whereby it emits light or causes a change in wavelength of the incident light optically excited
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- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
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- G—PHYSICS
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- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/577—Immunoassay; Biospecific binding assay; Materials therefor involving monoclonal antibodies binding reaction mechanisms characterised by the use of monoclonal antibodies; monoclonal antibodies per se are classified with their corresponding antigens
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Abstract
The aldehyde group modified method based on substrate surface that the present invention relates to a kind of, after substrate is first carried out corona treatment, it is transferred to the vacuum chamber of the gasification of amino silane and ethyl alcohol, modify to obtain the first modification substrate, it takes out the gas of vacuum chamber and accesses the ethyl alcohol diluent gas of glutaraldehyde, modify to obtain the second modification substrate；Then chemical bonding is formed in conjunction with protein antibodies molecule terminal amino by solid phase surface aldehyde groups, it again will be after the closing of the protein antibodies of incubation, it is immunoreacted with the PBS solution of proteantigen, learnt from fluorescence intensity, using the above method both can be stable fixing protein and can realize the function of low Poison signal-to-noise ratio and mass production.
Description
Technical field
The aldehyde group modified method based on substrate surface that the present invention relates to a kind of and the method for verifying its proteopexy effect.
Background technique
Increasingly developed with clinical detection, people are for quickly the demand of detection and Accurate Prediction disease is increasingly heavy immediately
It wants.Disease and pesticide residue etc. are detected using plastic chip as substrate, and inspection product constantly receives significant attention fastly, but in IVD
Can (in-vitro diagnosis) micro-fluidic field accomplish that accurately quantitatively there is also challenges.
Fast inspection and clinical detection chip and the most important program of test card are exactly in solid phase surface fixing grafting albumen
Matter.Solid phase surface has the materials such as silicon wafer, glass slide, polystyrene, polymethyl methacrylate, nitrocellulose membrane at present.It is common
Albumen assembling fixed form have a hydrophobic adsorbent, stromal surface is monomer modified and the methods of solid surface modification polymer.Such as
Where the different enough protein molecules for keeping bioactivity of solid phase surface fixing foot are challenging work, and
The target of numerous diligent pursuits of proteomics research person.
Conventional die modification is most of to use solwution method, impregnates in the concentrated sulfuric acid and hydrogen peroxide and reaches surface active, is turning
The solution for moving to amino acid solution and the molecule containing aldehyde radical reaches surface with aldehyde functions, but time-consuming in this way and low output and
Direct destruction structure can be generated to plastic chip.
Further for traditional by way of protein hydrophobic adsorption solid phase surface, protein is inhaled on hydrophobic material surface
It is attached to cause conformational change size bigger than conformational change of the protein after water wetted material absorption and protein is easy to inactivate, this
Very big challenge is generated for the quantitative and sensitivity of clinical detection.Since protein is big point of biology with space conformation
Son, so the most of method for using surface modification and grafting ligand molecule of the absorption of protein molecule, passes through covalent linkage
Realize the quantitative fixation of protein.Firstly the need of the group for deriving chemistry in solid substrate surface (silicon wafer, plastics etc.), then
Protein molecule coupling is fixed to the solid phase surface of chemical activation by chemically reacting.During this fixing protein, such as
The efficiency what improves coupling has guaranteed that background signal interference is one of significant challenge.Current surface treatment method and covalently
The method of coupling has amino, aldehyde radical, biological affine polymer (dopamine, polylysine etc.), wherein generally using amido modified
Substrate, this kind of chip majority apply genetic test due to its by physisorption proteopexy in solid phase table
Face, this method often occur that proteopexy rate is low, and the bad generation homogeneity of surface modification is poor convenient for preparation and at low cost,
There is the problems such as influencing the quantitative test of chip in the higher impure point that can have powerful connections.And it can be very for polymer-modified chip
The protein-chip that solves got well combines more stable bioaffinity good in the binding capacity and protein of solid phase surface fixation, but by
In polymer molecule chain length itself, spatial distribution is complicated and molecular weight is big, it is easy to be integrated to protein-chip in probe molecule
Very high non-specific adsorption is generated when surface leads to higher signal-to-noise ratio.
Summary of the invention
A kind of aldehyde group modified side based on substrate surface is provided the invention aims to overcome the deficiencies in the prior art
Method and the method for verifying its proteopexy effect.
The first purpose of this invention is to provide a kind of aldehyde group modified method based on substrate surface, it includes following step
It is rapid:
(a) after clean substrate being carried out corona treatment, it is transferred to the vacuum chamber of the gasification of amino silane and ethyl alcohol
Room, pressure maintaining maintain, and modify to obtain the first modification substrate, and the volume ratio of the amino silane and ethyl alcohol is 1:50-1:400；
(b) it takes out the gas of the vacuum chamber and accesses the ethyl alcohol diluent gas of glutaraldehyde, pressure maintaining maintains, modification
The second modification substrate, the volume ratio of the glutaraldehyde and the ethyl alcohol are 1:50-1:200.
Specifically, in step (a), clean substrate is subjected to corona treatment 5min-10min, and in the atmosphere of oxygen
Lower holding pressure is enclosed in 30-50Pa or less.
Specifically, in step (a), the pressure maintaining, which is maintained, keeps pressure to maintain 5min at 30Pa.
Specifically, in step (b), the pressure maintaining, which is maintained, keeps pressure to maintain 10min at 100Pa.
Specifically, the substrate is selected from one of plastic chip, glass or silicon template.
Preferably, the plastic chip is selected from one of polymethyl methacrylate, polystyrene.
Preferably, the glass is chosen compared with low Poison interference and the clean glass containing boride.
Preferably, the substrate can cleaned before with ultrasonic machine, then be dried for standby after being rinsed with deionized water.
Preferably, the volume ratio of the amino silane and ethyl alcohol is 1:200-1:400.
Preferably, the volume ratio of the glutaraldehyde and the ethyl alcohol is 1:50-1:100.
In the present invention, after the clean substrate of step (a) carries out corona treatment, the substrate surface handled can be generated
A large amount of free radical and hydroxyl, the vacuum chamber for being then transferred to amino silane gasification obtain the first modification substrate, substrate surface
Amino group is grafted.Amino silane is since volatilization temperature is at 135 DEG C, and amino silane gasification temperature can drop under vacuum conditions
The proportion of low while amino silane and ethanol-diluent also plays an important role.
Step (b) takes out the gas of the vacuum chamber and accesses the ethyl alcohol diluent gas of glutaraldehyde, and pressure maintaining maintains,
The second modification substrate is modified to obtain, substrate surface has grafted aldehyde groups at this time.
Second object of the present invention is to provide a kind of proteopexy verified as described above through aldehyde group modified substrate
The method of effect, it the following steps are included:
S1, it is incubated for monoclonal antibody albumen in the point sample area through aldehyde group modified substrate, pipettes point sample to being incubated for area, then carry out
Constant-temperature incubation completes the aldehyde radical of substrate and the secure bond of monoclonal antibody albumen；
S2, it is immersed what is be incubated in the PBS solution of BSA through the coated substrate of monoclonal antibody albumen, is placed in constant temperature oscillator temperature
It educates to reach the closing to substrate surface, further takes out repeated flushing, it is spare；
S3, hydrophilic film will be pasted through the closed substrate of S2, then molten in the PBS that monoclonal antibody proteantigen is added in the sample application zone of substrate
Liquid is immunoreacted；
S4, the substrate through being immunoreacted is passed through into fluorometric investigation instrument, measures its fluorescence intensity.
In S1 of the present invention, the secure bond of aldehyde radical and monoclonal antibody albumen is the amino carried by monoclonal antibody albumen terminal and substrate
The aldehyde radical terminal of upper grafting forms the chemically stable combination of schiff alkali: DNA- (CH by dehydration2)-NH6+R-CHO→
DNA-(CH2)-N=OHC-R；This firm chemical bonding mode physisorption simple compared to common substrate,
Substantially increase the fixed rate of antibody.
In S3 of the present invention, it is immunoreacted in the PBS solution that monoclonal antibody proteantigen is added in the sample application zone of substrate, i.e. antigen
Enter the specific binding that primary antibody reaction zone realizes antigen-antibody by microchannel.
Specifically, in S1, the monoclonal antibody albumen is alpha-fetoprotein antibody, and the concentration of the alpha-fetoprotein antibody is
100-200ng/ml。
Preferably, the concentration of the alpha-fetoprotein antibody is 100ng/ml.
Specifically, in S1, the temperature of constant-temperature incubation is 37 DEG C, time 4-12h.
Preferably, the temperature of the constant-temperature incubation is 37 DEG C, time 4h.
Specifically, in S2, the concentration of the PBS solution of BSA is 5-10mg/ml, is placed in 37 DEG C of incubation 1-2 of constant temperature oscillator
Hour is to reach the closing to substrate surface.
Preferably, the concentration of the PBS solution of the BSA is 8-10mg/ml.
Specifically, in S3, the concentration of the PBS solution of monoclonal antibody proteantigen is 1-3ug/ml.
Preferably, the concentration of the PBS solution of the monoclonal antibody proteantigen is 2-3ug/ml.
Specifically, in S4, the substrate through being immunoreacted is carried out to the survey of fluorescence intensity in 15min by fluorometric investigation instrument
Examination.
Due to the above technical solutions, the present invention has the following advantages over the prior art: first substrate surface is repaired
Aldehyde radical is adornd, recycles the aldehyde radical molecule of solid phase substrate modification to carry out ankyrin, passes through solid phase surface aldehyde groups and protein molecular
Terminal amino combines and forms chemical bonding, fixing protein that both can be stable and the function that can realize low signal-to-noise ratio and mass production
Energy.
Detailed description of the invention
Fig. 1 is the flow chart of substrate surface aldehyde radical of the present invention；
Fig. 2 is the structural schematic diagram of substrate；
Fig. 3 is the schematic diagram that albumen combines in the substrate of aldehyde radical.
Specific embodiment
The present invention will be further described in detail combined with specific embodiments below, but the present invention is not limited to following implementations
Example.Implementation condition used in the examples can do further adjustment according to specifically used different requirements, the implementation being not specified
Condition is the normal condition in the industry.
Choice of the substrates plastic chip of the invention, is known as " chip " directly below.
Embodiment 1
The aldehyde group modified method based on chip surface that the present embodiment provides a kind of and the method for verifying its proteopexy effect,
It the following steps are included:
(a) coring piece is placed in a beaker, ultrasound 15 minutes, then to be put into baking oven after being rinsed with deionized water spare；Then will
Clean chip carries out corona treatment 5min, and pressure is maintained at 50Pa or less under the atmosphere of oxygen；It will process
Chip be transferred to amino silane and ethyl alcohol gasification vacuum chamber (volume ratio of amino silane and ethyl alcohol be 1:200), core
Piece pressure in the vacuum chamber of gasification amino silane keeps maintaining 5min under 50Pa, so that ammonia has directly been grafted on the surface of chip
Base group obtains the first modification chip；
(b) gas of the vacuum chamber of gasification amino silane is taken out, while accessing the ethyl alcohol dilution of glutaraldehyde into chamber
Gas (volume ratio of glutaraldehyde and ethyl alcohol is 1:100), chip maintains 15min at the strong 50Pa of chamber inner pressure；To chip
It has directly grafted aldehyde groups and has obtained the second modification chip in surface.
Test: after the completion of chip modification, we verify the effect of its proteopexy with the following method:
S1: it is incubated for alpha-fetoprotein 100ng/ml in the point sample area of modified chip, then pipettes 1uL point sample with liquid-transfering gun
To area is incubated for, it is put into 38 DEG C of constant temperature of baking oven and is incubated for 4h；
S2: the coated chip of the alpha-fetoprotein being incubated for is immersed in the PBS solution containing 10mg/ml BSA, perseverance is placed in
37 DEG C of incubation 1h of warm oscillator are to reach the closing to chip surface；The chip closed takes out PBS buffer solution repeated flushing 3 times
It is spare to be put into 37 DEG C of baking ovens；
S3: the chip that closing is completed pastes hydrophilic film, and the alpha-fetoprotein of 2ug/ml is then added in the point sample area of chip
The PBS solution of antigen (antigenic surface has fluorescent microsphere), realizes the specific binding of antigen-antibody；
S4: the chip after immune response is measured into its fluorescence intensity by fluorometric investigation instrument in 15min.
Test is 8.45% with the coefficient of variation CV value of batch 10 groups of fluorescence signals obtained of same treatment processing chip.
Embodiment 2
The aldehyde group modified method based on chip surface that the present embodiment provides a kind of, it with it is almost the same in embodiment 1, no
With: in step (a), the volume ratio of amino silane and ethyl alcohol is 1:50.Same batch 10 groups of same treatment processing chip of test obtain
The coefficient of variation CV value of fluorescence signal out is 14.3%.
Embodiment 3
The aldehyde group modified method based on chip surface that the present embodiment provides a kind of, it with it is almost the same in embodiment 1, no
With: in step (a), the volume ratio of amino silane and ethyl alcohol is 1:400.Same batch 10 groups of same treatment processing chip of test obtain
The coefficient of variation CV value of fluorescence signal out is 13.6%.
Embodiment 4
The aldehyde group modified method based on chip surface that the present embodiment provides a kind of, it with it is almost the same in embodiment 1, no
With: in step (b), the volume ratio of glutaraldehyde and ethyl alcohol is 1:200.Same batch 10 groups of same treatment processing chip of test obtain
Fluorescence signal coefficient of variation CV value be 14.1%.
Embodiment 5
The aldehyde group modified method based on chip surface that the present embodiment provides a kind of, it with it is almost the same in embodiment 1, no
With: in step (b), the volume ratio of glutaraldehyde and ethyl alcohol is 1:50.Same batch 10 groups of same treatment processing chip of test obtain
Fluorescence signal coefficient of variation CV value be 13.2%.
Comparative example 1
The present embodiment uses solwution method, and chip is impregnated in the concentrated sulfuric acid and hydrogen peroxide and reaches surface active, is then transferred to
In the solution of amino acid solution and the molecule containing aldehyde radical, so that chip surface grafts aldehyde groups.
The step of verifying proteopexy effect is consistent with embodiment 1.
The concentrated sulfuric acid in comparative example 1 generates direct destruction to chip, can not carry out subsequent grafting and test with effect
Card.
Comparative example 2
Chip does not do aldehyde group modified, and the step of verifying proteopexy effect is consistent with embodiment 1.
Test is 20% with the coefficient of variation CV value of batch 10 groups of fluorescence signals obtained of same treatment processing chip.
The stability for the fluorescence intensity that ten groups of parallel laboratory tests of embodiment 1 and ten groups of parallel laboratory tests of comparative example 2 are calculated
Data are listed in table 1.
| Chip number | Fluorescence intensity -- it is aldehyde group modified | Fluorescence intensity -- it does not modify |
| 1 | 347571 | 52359 |
| 2 | 361810 | 64976 |
| 3 | 372677 | 197709 |
| 4 | 374680 | 203521 |
| 5 | 378886 | 207049 |
| 6 | 395992 | 235372 |
| 7 | 405594 | 262913 |
| 8 | 423945 | 286883 |
| 9 | 432541 | 303807 |
| 10 | 450977 | 333005 |
| Mean | 394467.3 | 253782.4 |
| STD | 33354.84 | 50921.63 |
| CV | 8.45% | 20% |
Table 1
As shown in table 1, aldehyde group modified chip and the CV value for not doing modification chip are respectively 8.45% and 20%, it is seen that aldehyde radical
Chip is substantially better than the chip for not making to modify in the effect of proteopexy after modification.Coefficient of variation CV value is as judge chip fluorescence
The standard of signal strength generally believes that it is just obtained with the chip CV of batch same treatment technique lower than 15% on the market and recognizes to market
It can.
Conventional modification is not modified or done to chip in comparative example, and consuming time is long and low output, to chip meeting
Generate direct destruction structure.Therefore the qualification rate of chip is low, in substrate detection disease and pesticide residue etc. fastly inspection product
Using bad.And it is aldehyde group modified to use method of the invention to carry out, verifying proteopexy effect is good.By table 1, we can be sent out
It now finishes difference in the chip batch of aldehyde radical processing and is significantly less than the chip not dealt with.
The above embodiments merely illustrate the technical concept and features of the present invention, and its object is to allow person skilled in the art
Scholar cans understand the content of the present invention and implement it accordingly, and it is not intended to limit the scope of the present invention.It is all according to the present invention
Equivalent change or modification made by Spirit Essence, should be covered by the protection scope of the present invention.
Claims (10)
1. a kind of aldehyde group modified method based on substrate surface, which is characterized in that it the following steps are included:
(a) after clean substrate being carried out corona treatment, it is transferred to the vacuum chamber of the gasification of amino silane and ethyl alcohol, is protected
Pressure maintains, and modifies to obtain the first modification substrate, and the volume ratio of the amino silane and ethyl alcohol is 1:50-1:400；
(b) take out the gas of the vacuum chamber and access the ethyl alcohol diluent gas of glutaraldehyde, pressure maintaining maintains, modify the
The volume ratio of two modification substrates, the glutaraldehyde and the ethyl alcohol is 1:50-1:200:.
2. the aldehyde group modified method according to claim 1 based on substrate surface, it is characterised in that: in step (a), will do
Net substrate carries out corona treatment 5min-10min, and keeps pressure in 30-50Pa or less under the atmosphere of oxygen.
3. the aldehyde group modified method according to claim 1 based on substrate surface, it is characterised in that: described in step (a)
Pressure maintaining be maintained keep pressure maintain 5-15min at 30Pa-50Pa.
4. the aldehyde group modified method according to claim 1 based on substrate surface, it is characterised in that: described in step (b)
Pressure maintaining be maintained keep pressure maintain 10-20min at 30Pa-100Pa.
5. a kind of method of proteopexy effect through aldehyde group modified substrate of verifying as described in claim 1-4, feature exist
In, it the following steps are included:
S1, it is incubated for monoclonal antibody albumen in the point sample area through aldehyde group modified substrate, pipettes point sample to being incubated for area, then carry out constant temperature
It is incubated for the secure bond of the aldehyde radical and monoclonal antibody albumen of completing substrate；
S2, being immersed through the coated substrate of monoclonal antibody albumen in the PBS solution of BSA of will being incubated for, be placed in constant temperature oscillator incubate with
Reach the closing to substrate surface, further takes out repeated flushing, it is spare；
S3, hydrophilic film will be pasted through the closed substrate of S2, then the sample application zone of substrate be added the PBS solution of monoclonal antibody proteantigen into
Row immune response；
S4, the substrate through being immunoreacted is passed through into fluorometric investigation instrument, measures its fluorescence intensity.
6. the method for the proteopexy effect according to claim 5 through aldehyde group modified substrate, it is characterised in that: in S1,
The monoclonal antibody albumen is alpha-fetoprotein antibody, and the concentration of the alpha-fetoprotein antibody is 100-200ng/ml.
7. the method for the proteopexy effect according to claim 5 through aldehyde group modified substrate, it is characterised in that: in S1,
The temperature of constant-temperature incubation is 37 DEG C, time 4-12h.
8. the method for the proteopexy effect according to claim 5 through aldehyde group modified substrate, it is characterised in that: in S2,
The concentration of the PBS solution of BSA is 1mg/ml, is placed in 37 DEG C of constant temperature oscillator and incubates 1 hour to reach the closing to substrate surface.
9. the method for the proteopexy effect according to claim 5 through aldehyde group modified substrate, it is characterised in that: in S3,
The concentration of the PBS solution of monoclonal antibody proteantigen is 2ug/ml.
10. the method for the proteopexy effect according to claim 5 through aldehyde group modified substrate, it is characterised in that: in S4,
Substrate through being immunoreacted is carried out in 10-15min by fluorometric investigation instrument to the test of fluorescence intensity.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111514871A (en) * | 2020-05-27 | 2020-08-11 | 合肥中科易康达生物医学有限公司 | Preparation method and application of solid phase substrate for nucleic acid extraction |
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| US20050176003A1 (en) * | 2001-11-27 | 2005-08-11 | Sumitomo Bakelite Co., Ltd. | Plastic substrate for microchips |
| CN103543081A (en) * | 2013-09-29 | 2014-01-29 | 中国科学院半导体研究所 | Portable sensing system for early diagnosing liver cancer and functional modification method of portable sensing system |
| CN106841629A (en) * | 2015-12-03 | 2017-06-13 | 中国科学院上海微系统与信息技术研究所 | A kind of odor identification biology sensor based on silicon nanowires |
| CN108085314A (en) * | 2016-11-21 | 2018-05-29 | 清华大学 | A kind of amination filter paper/film purified for nucleic acid extraction and preparation method and application |
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- 2019-07-04 CN CN201910599807.4A patent/CN110343182A/en active Pending
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050176003A1 (en) * | 2001-11-27 | 2005-08-11 | Sumitomo Bakelite Co., Ltd. | Plastic substrate for microchips |
| CN103543081A (en) * | 2013-09-29 | 2014-01-29 | 中国科学院半导体研究所 | Portable sensing system for early diagnosing liver cancer and functional modification method of portable sensing system |
| CN106841629A (en) * | 2015-12-03 | 2017-06-13 | 中国科学院上海微系统与信息技术研究所 | A kind of odor identification biology sensor based on silicon nanowires |
| CN108085314A (en) * | 2016-11-21 | 2018-05-29 | 清华大学 | A kind of amination filter paper/film purified for nucleic acid extraction and preparation method and application |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN111514871A (en) * | 2020-05-27 | 2020-08-11 | 合肥中科易康达生物医学有限公司 | Preparation method and application of solid phase substrate for nucleic acid extraction |
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Application publication date: 20191018 |