CN111458391B - Multi-mechanism driven amyloid peptide detection sensor and construction method thereof - Google Patents
Multi-mechanism driven amyloid peptide detection sensor and construction method thereof Download PDFInfo
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- CN111458391B CN111458391B CN202010294697.3A CN202010294697A CN111458391B CN 111458391 B CN111458391 B CN 111458391B CN 202010294697 A CN202010294697 A CN 202010294697A CN 111458391 B CN111458391 B CN 111458391B
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Abstract
The inventionA multi-mechanism driven amyloid peptide detection sensor and a construction method thereof are disclosed, which make full use of the characteristics of amyloid protein to realize the specific detection of amyloid protein. Amyloid can be simultaneously reacted with Cu2+Binding to Heme forms a complex that can produce H2O2。C3N4At low concentration H2O2If present, promotes ECL luminescence. High concentrations of amyloid can cause steric hindrance to the sensor, contributing to a decrease in ECL signal. The sensor has better specificity to amyloid, and can quickly and sensitively realize early detection of the amyloid.
Description
Technical Field
The invention belongs to the field of detection of amyloid protein, and particularly relates to a novel method for detecting amyloid protein peptide, so that early detection of the amyloid protein is realized.
Background
Alzheimer's Disease (AD) is an irreversible neurodegenerative disease that can lead to synaptic dysfunction and alterations in human behavioral ability. It usually brings about The deposition of Toxic amyloid fibrils (amyloid aggregates) in The subcortical space and cortex of The human brain and thus enables The detection of AD (Taylor, j.p.; Hardy, j.; Fischbeck, k.h. biomedicine-Toxic proteins in neuro-genic disorders, science 2002,296,1991-1995. sacchethei, j.c.; Kelly, j.w. therapeutic variants for human amyloid disorders, nat. rev. drive, Discovery 2002,1,267-275.Holtzman, d.m.; Morris, j.c.; urate, a.m. alzheimer's disorders: change of The connected center, science trans.2011.2011.3577, 75). However, recent research activities have shown that soluble oligomeric intermediates are the most neurotoxic species and are key factors for neuronal cell death in AD patients (Lesne, S.; Koh, M.T.; Kotilinek, L.; Kayed, R.; Glabe, C.G.; Yang, A.; Gallagher, M.; Ashe, K.H.A specific amyloid-beta protein assay in the branched antigens memory. Nature 2006,440, 352;). Beta-amyloid is a major component of age spots and is highly associated with neuronal dysfunction and memory deficits (Ross, c.a.; poinier, m.a. protein Aggregation and neuro-generative disease, nat. med.2004,10(Suppl), S10-7.). A β is a hydrophobic, fixedly disordered and easily aggregated peptide, which usually consists of 39-43 amino acid residues (Qiang, W., Yau, W.M., Lu, J.X., Colling, J., and Tycko, R. (2017) Structural variation in amino-beta fibers from Alzheimer's disease closed amino groups. Nature 541, 217-221.). The symptoms of AD present in the elderly present a great challenge to the medical system and associated policies due to the lack of methods by which AD can be rapidly recovered and treated (Gregersen, n.; Bross, p.; Vang, s.; Christensen, j.h. protein mixing and Human disease.annu.rev. genomics hum. gene.2006, 7,103-124.).
Electrochemiluminescence (ECL) is enjoyed by researchers as an emerging detection technology, and thus, various ECL biosensors have been created. Recent studies have mainly used metal complexes, luminol and nanomaterials as ECL luminophores (Yuan, j., Li, t., Yin, x.b., Guo, l., Jiang, x., Jin, w., Yang, x., Wang, e.,2006, anal.chem.78, 2934-2938. Qiao, y., Li, y., Fu, w., Guo, z., Zheng, x.,2018.anal.chem.90, 9629-9636. Zhou, y., Chen, m., Zhuo, y., Chai, y., Xu, w., Yuan, r.,2017.anal.chem.89, 6787-6793. Li, x., Lu, p., Wu, b., Wang h, Wang, b., leg, r, 2017. ampere.7, 11, bio-47. In recent years, carbon nitride nanosheets have been favored by researchers due to their excellent properties (Wang, y.z., Hao, n., Feng, q.m., Shi, h.w., Xu, j.j., Chen, h.y.,2016.biosens, bioelectrron.77, 76-82.).
Disclosure of Invention
The invention aims to overcome the defects in the prior art and prepare a biosensor for detecting amyloid by utilizing the characteristics of the biosensor. The biosensor is prepared by utilizing the dual effects of the intrinsic characteristics and the steric hindrance of the compound, and the specific detection of amyloid protein is realized.
The term "a β" refers to: beta-amyloid protein (1-40). The term "Hemin" refers to: hemin. The term "Heme" refers to: heme. The term "g-C3N4"means that: carbon nitride nanosheets.
A multi-mechanism driven amyloid peptide detection sensor comprises a gold electrode and g-C3N4Au nanoparticles, DNA-immobilized strand having thiol group at end, beta-precipitatePowder-like protein, copper sulfate solution and heme. g-C3N4Assembled on the surface of the gold electrode, and Au nanoparticles assembled on g-C3N4The surface, the DNA fixed chain with the sulfhydryl at the tail end is loaded on the surface of the gold nanoparticle, the surface of the DNA fixed chain with the sulfhydryl at the tail end captures beta-amyloid, and the surface of the beta-amyloid captures copper ions and heme to form a complex.
A construction method of a multi-mechanism driven amyloid peptide detection sensor specifically comprises the following steps:
(1) polishing a gold electrode on polishing cloth by using 0.05 mu M aluminum powder, sequentially performing ultrasonic treatment on the polished electrode in ultrapure water, ethanol and ultrapure water for three minutes, then blow-drying by using nitrogen, and placing the electrode at 4 ℃ for later use;
(2) g to C3N4Sonicating the sonicated g-C prior to use3N4Dropwise adding the DNA immobilized chain with sulfydryl at the tail end to the electrode assembled layer by layer after the drying of the Au nano particles, and putting the DNA immobilized chain into a 37 ℃ oven for overnight reaction;
(3) soluble copper salt solution and heme were added to β -amyloid (a β) solutions of different concentrations for two hours, and then the electrodes treated in step (2) were washed with PBS buffer solution (0.1M, pH 7.4) and separately placed in PBS buffer solution.
Further, the soluble copper salt in step (3) includes, but is not limited to, one or more of copper sulfate and copper chloride.
Further, the g-C3N4The preparation method specifically comprises the following steps:
(101) adding 10g urea into a crucible, placing into a muffle furnace, heating at 20 deg.C/min, heating to 550 deg.C, maintaining for two hours, and naturally cooling to room temperature to obtain block C3N4。
(102) 100mg of the block C obtained in the above step was taken3N4Dispersing in 100mL of ultrapure water, and ultrasonically pulverizing the dispersed suspension for two hours by using a cell pulverizer to obtain g-C3N4And placing the suspension liquid after ultrasonic treatment at 4 ℃ for later use.
The preparation method of the Au nanoparticles comprises the following steps:
(201) aqua regia (HNO) for glassware used in the experimental process3HCl 1:3) overnight, washed with ultrapure water and dried.
(202) 50mL of 1% HAuCl were added under vigorous stirring at 220 deg.C4Into a round bottom flask. After the solution boiled, sodium citrate was added rapidly and the solution slowly turned purple indicating the formation of gold nanoparticles.
(203) The solution was stirred at 220 ℃ for 1h in the dark. Finally, the solution was allowed to react overnight at room temperature with a color change from purple to wine-red.
Preferably, the beta-amyloid and Cu in the solution of the step (3)2+The molar ratio of (1: 0.4) - (1: 1.6); most preferably, the optimal reaction ratio is 1: 1.2.
Preferably, the molar ratio of beta-amyloid to Heme in the solution of step (3) is 1:0.4-1: 1.6; most preferably, the optimal reaction ratio is 1: 0.8.
Preferably, the pH of the solution of beta-amyloid in the solution of step (3) is: 5.9-8.4; most preferably, the optimal reaction pH is 7.4.
Preferably, the amyloid beta and Cu in the solution obtained in the step (3)2+And the reaction times for Heme were: 1-7 h; most preferably, the optimal reaction time is 3 h.
Preferably, the wavelength screening range of the biosensor is: 400nm, 425nm, 440nm, 460nm, 490nm, 535nm, the optimum wavelength is about 460 nm.
The invention has the beneficial effects that:
(1) the biosensor prepared by the invention can be used for detecting amyloid protein with the detection speed of 1.0 multiplied by 10 respectively-13mol/L to 1.0X 10-11mol/L range and 1.0X 10-11mol/L to 1.0X 10-8Good linearity in the mol/L range.
(2) The beta-amyloid protein can be mixed with Cu2+Binding with Heme to form a complex, which can exist in the presence of dissolved oxygenGeneration of H2O2。
(3) When the content of beta-amyloid is low, a small amount of H is produced2O2Small amount of H2O2Can promote C3N4ECL signal of (c).
(4) When the content of beta-amyloid is high, a large amount of complexes are captured on the electrode due to the capture effect of the electrode, so that large steric hindrance is brought, and C is enabled to be contained3N4The ECL signal of (c) decreases.
Drawings
FIG. 1 is a diagram for verifying the feasibility of the biosensor constructed according to the present invention. Panel A shows the ECL signal at small amyloid concentrations (a: 1.0X 10)-11mol/L, b: blank), panel B shows ECL signal at large amyloid concentrations (a: 1.0X 10- 8mol/L,b：1.0×10-11mol/L), panel C shows EIS signals at small concentrations of amyloid (a: 1.0X 10-11mol/L, b: blank), panel D shows EIS signals at large amyloid concentrations (a: 1.0X 10-3mol/L,b：1.0×10-11mol/L)。
FIG. 2 shows g-C in the present invention3N4Infrared characterization graph of (1).
FIG. 3 shows g-C in the present invention3N4And ultraviolet absorption spectrum of Au nanoparticles (a is g-C)3N4And b is Au nanoparticles).
FIG. 4 is an electrochemical luminescence detection graph of a biosensor constructed according to the present invention for different concentrations of amyloid beta (where a: 1.0X 10)-13mol/L、b：5.0×10-13mol/L、c：1.0×10-12mol/L、d：5.0×10-12mol/L、e：1.0×10-11mol/L)。
FIG. 5 is an electrochemical luminescence test chart of a biosensor constructed according to the present invention for various concentrations of amyloid beta (wherein a: 1.0X 10)-11mol/L、b：5.0×10-11mol/L、c：1.0×10-10mol/L d：5.0×10-10mol/L、e:1.0×10-9mol/L、f：5.0×10-9mol/L、g:1.0×10-8mol/L)。
FIG. 6 is a standard curve of electrochemiluminescence detection of various concentrations of amyloid beta by the biosensor constructed according to the present invention.
FIG. 7 is an optimization of biosensing constructed according to the present invention for different wavelengths.
Detailed Description
The technical scheme of the invention is further explained by the specific implementation mode in combination with the attached drawings.
This section generally describes the materials used in the testing of the present invention, as well as the testing methods. Although many materials and methods of operation are known for the purpose of carrying out the invention, the invention is nevertheless described herein in detail as is practicable.
The beta-amyloid used in the following examples was purchased from Shanghai Biopsis GmbH, unless otherwise specified. The beta-amyloid sequence is: DAEFR HDSGY EVHHQ KLVFF AEDVG SNKGA ILGLM VGGVV are provided.
Unless otherwise indicated, the DNA used in the following examples was purchased from shanghai bio-gaku corporation and has a DNA sequence of 5' -HS-GCC TGT GGT GTT GGG GCG GGT GCG.
The solvents of the aqueous solutions used in the following examples were all ultrapure water unless otherwise specified.
All reagents used in the following examples were analytical reagents unless otherwise specified.
The reagents and instrumentation used in the following examples are as follows:
reagent:
urea, Hemin (Hemin), copper sulfate (CuSO)4) Potassium chloride, sodium hydroxide, sodium chloride, chloroauric acid (HAuCl)4) Disodium hydrogen phosphate, sodium citrate, sodium dihydrogen phosphate, potassium persulfate, and Hexafluoroisopropanol (HFIP) were all available from alatin reagent limited.
The instrument comprises:
infrared absorption Spectroscopy, model FT-IR Nicolet iS 10.
Ultraviolet absorption spectrometer, model BIOMATE 160.
Electrochemiluminescence analyzer, available from sienna ruimmy, model MPI-E.
Example 1
g-C in the present example3N4The preparation method specifically comprises the following steps:
(1) adding 10g urea into a crucible, placing into a muffle furnace, heating at 20 deg.C/min, heating to 550 deg.C, maintaining for two hours, and naturally cooling to room temperature to obtain block C3N4。
(2) Taking 100mg of the block C obtained in the previous step3N4Dispersing in 100mL of ultrapure water, and ultrasonically pulverizing the dispersed suspension for two hours by using a cell pulverizer to obtain g-C3N4And placing the suspension liquid after ultrasonic treatment at 4 ℃ for later use.
Example 2
The preparation method of the Au nanoparticle related to this embodiment specifically includes the following steps:
(1) aqua regia (HNO) for glassware used in the experimental process3HCl 1:3) overnight, washed with ultrapure water and dried.
(2) 50mL of 1% HAuCl were added under vigorous stirring at 220 deg.C4Into a round bottom flask. After the solution is boiled, sodium citrate is added rapidly, and the solution slowly turns purple, which indicates that gold nanoparticles are generated.
(3) The solution was stirred at 220 ℃ for 1h in the dark. Finally, the solution was allowed to react overnight at room temperature, changing color from purple to wine-red.
As shown in FIG. 1, for g-C3N4Performing infrared characterization, and analyzing each peak position of the infrared spectrogram to show that g-C3N4The successful preparation. Then for g-C3N4And Au nano-particles are subjected to ultraviolet characterization, and the graph of the ultraviolet characterization is contrasted with the reported literature, so that g-C is shown3N4And the successful preparation of Au nanoparticles.
Example 3
Preparation of a β solution:
(1) the A beta powder was dissolved in Hexafluoroisopropanol (HFIP) to prepare a 1.0mg/mL Hexafluoroisopropanol (HFIP) solution, and the prepared solution was freeze-dried using a freeze-dryer to form an A beta layered film on the bottom of the tube.
(2) The lyophilized a β layered film was dissolved in PBS buffer (0.1M, pH 7.4) to prepare 1.0 × 10-6mol/L of A beta solution at-20 ℃ for standby.
Detection of A beta:
(1) before experimental test, a gold electrode is polished on polishing cloth by using 0.05 mu M aluminum powder, the polished electrode is respectively subjected to ultrasonic treatment for three minutes in ultrapure water, ethanol and ultrapure water in sequence, the electrode subjected to ultrasonic treatment is dried by using nitrogen, and the electrode is placed at 4 ℃ for later use;
(2) the DNA reagent was allowed to stand at room temperature for 2 minutes, centrifuged at 10000 rpm for 10 minutes, and added with PBS buffer (0.1M, pH 7.4) to prepare a solution of a predetermined concentration. The prepared DNA solution is mixed with a TCEP solution to cut the disulfide bonds in the DNA solution, and a DNA fixed chain with a thiol group at the end is obtained.
(3) G to C to be prepared3N4Ultrasonic treatment is carried out for 30 minutes before the suspension is used to ensure that the suspension is uniformly dispersed, and a certain amount of g-C is taken3N4Dripping the DNA fixed chain with the mercapto at the tail end onto the electrode treated in the process after the natural drying is finished, and putting the electrode into an oven at 37 ℃ for overnight reaction.
(4) Taking a clean EP tube, adding different amounts of beta-amyloid and CuSO into the tube4And Heme, prepared as a standard solution at a certain concentration with PBS buffer solution (0.1M, pH 7.4). The treated electrode was washed with PBS buffer (0.1M, pH 7.4), then placed in a test tube, and placed in a constant temperature oven at 37 ℃ for 3 hours. And after incubation, putting the electrode into a detection pool filled with potassium persulfate detection liquid to carry out electrochemiluminescence signal detection, and obtaining a standard curve of the concentration of Abeta and the electrochemiluminescence intensity. Wherein the concentration of the potassium persulfate detection solution is 0.1 mol/L.
As can be seen from fig. 6: when the content of beta-amyloid is less than 1.0X 10-11Occasionally, heme-Cu2+-a β forming a complex at the electrodeSurface energy generation of H2O2This stage H2O2Predominating in the enhancement of, H2O2Can promote C3N4The ECL signal intensity of the protein is in positive correlation with the content of beta-amyloid. When the content of beta-amyloid is more than 1.0X 10-11In time, the macromolecules formed by beta-amyloid folding more occupy the surface of the electrode, the steric hindrance plays a main role in inhibiting C3N4The ECL signal intensity of (a) is inversely related to the amount of beta-amyloid.
The wavelength screening range of the biosensor is as follows: 400nm, 425nm, 440nm, 460nm, 490nm, 535nm, the optimum wavelength is about 460 nm.
Claims (7)
1. A multi-mechanism driven amyloid peptide detection sensor is characterized by comprising a gold electrode and g-C3N4Au nanoparticles, DNA-immobilized chain with sulfhydryl at end, beta-amyloid, copper sulfate solution and heme, g-C3N4The Au nanoparticles are assembled on the surface of the gold electrode layer by layer, and the g-C nanoparticles are assembled on the surface of the gold electrode layer by layer3N4The surface, the DNA fixed chain with the sulfhydryl at the tail end is loaded on the surface of the Au nanoparticle, the surface of the DNA fixed chain with the sulfhydryl at the tail end captures beta-amyloid, and the surface of the beta-amyloid captures a complex formed by copper ions and heme.
2. A construction method of a multi-mechanism driven amyloid peptide detection sensor is characterized by comprising the following steps:
(1) polishing a gold electrode on polishing cloth by using 0.05 mu M aluminum powder, sequentially performing ultrasonic treatment on the polished electrode in ultrapure water, ethanol and ultrapure water for three minutes, then blow-drying by using nitrogen, and placing the electrode at 4 ℃ for later use;
(2) g to C3N4Ultrasonic treatment before use, ultrasonic treatment of C3N4Dripping the solution on the electrode pretreated in the step (1) for natural drying, dripping Au nanoparticles on the electrode after drying, and continuously dripping DNA fixed chains with sulfydryl at the tail ends after drying the nanoparticlesPutting the mixture on an electrode, and putting the mixture into a constant-temperature oven at 37 ℃ for overnight reaction;
(3) adding copper sulfate solution and heme into beta-amyloid solution with different concentrations for reaction for two hours, and then putting the electrode treated in the step (2) into the solution.
3. The method for constructing a multi-mechanism driven amyloid peptide detection sensor according to claim 2, wherein the Au nanoparticle manufacturing process comprises the following steps:
(201) soaking glassware used in the experimental process in aqua regia overnight, cleaning with ultrapure water and drying;
(202) 50mL of 1% HAuCl were added under vigorous stirring at 220 deg.C4Injecting the solution into a round-bottom flask, quickly adding sodium citrate after the solution is boiled, and slowly turning the solution into purple, which indicates that Au nano-particles are generated;
(203) the solution was stirred at 220 ℃ in the dark for 1h and finally the solution was allowed to react overnight at room temperature with a change in color from purple to wine-red.
4. The method for constructing a multi-mechanism driven amyloid peptide detection sensor according to claim 3, wherein the solution of step (3) contains beta-amyloid and Cu2+The molar ratio of (1: 0.4) - (1: 1.6); the molar ratio of the beta-amyloid to the heme is 1:0.4-1: 1.6; the pH of the beta-amyloid solution is 5.9-8.4; beta-amyloid protein with Cu2+The reaction time of the hemoglobin and the hemoglobin is 1-7 h.
5. The method for constructing a multi-mechanism driven amyloid peptide detection sensor according to claim 4, wherein the solution of step (3) contains beta-amyloid and Cu2+The optimal molar ratio of (1: 1.2); the optimal molar ratio of beta-amyloid to heme is 1: 0.8; the optimal pH for the beta-amyloid solution reaction is: 7.4 of the total weight of the mixture; beta-amyloid protein with Cu2+The optimal reaction time with heme was 3 h.
6. The method for constructing a multi-mechanism driven amyloid peptide detection sensor according to claim 5, wherein the wavelength screening range of the biosensor is as follows: 400nm, 425nm, 440nm, 460nm, 490nm, 535 nm.
7. The method for constructing a multi-mechanism driven amyloid peptide detection sensor according to claim 5, wherein the wavelength of the biosensor is 460 nm.
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