Carbon nanotube protein composite hydrogel as well as preparation method and application thereof

Abstract

The invention relates to the technical field of biomedical materials, in particular to carbon nanotube protein composite hydrogel and a preparation method and application thereof, and preparation raw materials comprise hydrophilic carbon nanotubes and protein; the protein is characterized in that A, the protein comprises one or more of serum albumin, acellular matrix protein or derivatives thereof; and B, the quantity ratio of aromatic ring-containing amino acids or derivatives thereof in the protein structure is greater than or equal to 4%. According to the method, the hydrophilic nanotubes are dispersed and are fully and uniformly mixed with the protein, so that the formed compound has good stability, and near-infrared light induced gel forming can be realized within 5 minutes after the near-infrared light is used for irradiation. The preparation method provided by the invention is rapid, simple and good in repeatability, can be suitable for various proteins, and can be applied to the fields of biomedical materials, flexible electronic devices and the like.

Description

Technical Field

[0001] This invention relates to the field of biomedical materials technology, specifically to a carbon nanotube protein composite hydrogel, its preparation method, and its application. Background Technology

[0002] Hydrogels, as biocompatible materials, are a class of three-dimensional network polymers with hydrophilic groups. Due to the physical and chemical cross-linking between polymer chains, hydrogels can swell in water but remain insoluble while maintaining a certain shape. In medicine, hydrogels are used for wound dressings, postoperative anti-adhesion, surgical hemostasis, tissue filling, and preventing tissue fluid leakage or gas leakage. Based on their formation mechanism, hydrogels are divided into two main categories: chemically cross-linked hydrogels and physically cross-linked hydrogels. Physically cross-linked hydrogels can be further divided into thermosensitive hydrogels and molecularly self-assembled hydrogels. Physically cross-linked hydrogels are bonded together by physical forces, such as electrostatic interactions, hydrogen bonds, and chain entanglement. Physically cross-linked hydrogels have attracted widespread attention due to their significant advantages, including simple materials, controllable processes, and avoidance of the potential toxicity of cross-linking agents or unreacted functional groups.

[0003] Proteins, as biomaterials, have received continuous research and attention in tissue repair and disease treatment due to their high bioactivity, low toxicity, and roles in cell regulation and metabolism. For example, Lee et al. used protein hydrogels (containing 20-30 wt% bovine serum albumin (BSA)) for drug release and 3D cell culture, supporting heart / bone tissue regeneration with a cell viability >95%. The gelation of simple proteins often involves temperature-driven self-assembly to form three-dimensional chain entanglements, resulting in hydrogels. However, this process is time-consuming, the loose chain entanglements lead to weak hydrogel mechanics, and degradation is too rapid, limiting their biomedical applications. Currently, proteins often require the addition of cross-linking agents (such as glutaraldehyde), chemical modification (such as grafting methacryloyl groups), or repeated freeze-thaw cycles to form protein hydrogels. However, these methods all have drawbacks, such as the inability to completely remove residual cross-linking agents leading to excessive material toxicity, unreacted functional groups inhibiting cell growth, or poor compatibility between the pre-fabricated hydrogel and the application environment.

[0004] Carbon nanotubes are carbon-based tubular crystals with high specific surface area, strong chemical stability, non-specific adsorption capacity, biomembrane permeability, and biosafety, showing promising applications in drug delivery, tumor therapy, and biosensing. Studies have shown that carbon nanotubes can bind to bacterial cell membranes through electrostatic adsorption, thereby penetrating the bacterial cell wall to achieve antibacterial effects. Their antibacterial mechanism may be related to damage to the bacterial cell membrane, oxidative stress, and loss of DNA and proteins. Functionalized carbon nanotubes (single-stranded DNA-modified carbon nanotubes) do not damage normal cells under near-infrared light irradiation but exhibit targeted killing effects on malignant tumor cells. In the materials science field, carbon nanotubes can enhance the conductivity of polyethylene glycol hydrogels, showing potential in nerve repair. They may also be used in conjunction with sericin to prepare flexible electronic devices. However, the above studies may only focus on the conductivity and photothermal therapeutic effects of carbon nanotubes on cells, without exploring the photothermal-induced gelation effect of carbon nanotube materials. Furthermore, as an inorganic nanomaterial, carbon nanotubes inherently exhibit insolubility and solution aggregation, leading to uneven distribution in aqueous solutions or sedimentation before use. This often necessitates prolonged sonication or agitation before application, and the resulting composite solutions suffer from poor homogeneity, making it difficult to maintain suspension for extended periods, severely limiting their applications. Additionally, existing research, such as Chinese invention patent application CN116688955A, primarily focuses on protein-modified carbon nanotubes or the adsorption of small amounts of protein by carbon nanotubes. There are no patent reports on using the photothermal effect of carbon nanotubes to induce gelation of high-concentration proteins, nor are there any studies on the performance and applications of using the photothermal effect of carbon nanotubes to induce protein hydrogels. Summary of the Invention

[0005] To address the problems in the prior art, the first aspect of the present invention provides a carbon nanotube-protein composite hydrogel, the raw materials of which include hydrophilic carbon nanotubes and proteins; The protein includes the following characteristics: A. The protein includes one or more of serum albumin, decellularized matrix protein, or derivatives thereof; B. The protein contains ≥4% aromatic ring amino acids or their derivatives in its structure.

[0006] This invention utilizes hydrophilic carbon nanotubes to bind with proteins containing aromatic cyclic amino acids via π-π interactions, forming a stable complex. This addresses the problem of carbon nanotubes easily agglomerating and settling in aqueous solutions, significantly improving dispersion stability. Furthermore, controlling the proportion of aromatic cyclic amino acids or their derivatives in the protein structure to ≥4% ensures effective binding between carbon nanotubes and proteins, enabling rapid gelation induced by near-infrared light. Aromatic cyclic amino acids provide binding sites; insufficient proportions result in weak binding forces, preventing carbon nanotubes from stably anchoring to the protein surface and hindering the subsequent photothermal-induced self-assembly process.

[0007] In some embodiments, the derivative includes at least one of recombinant human serum albumin, albumin-drug conjugates, oxidized or glycosylated derivatives, fatty acid-binding derivatives, and protein nanoparticles.

[0008] In some embodiments, the purity of the serum albumin is ≥90%.

[0009] In some embodiments, the serum albumin includes bovine serum albumin, wherein the bovine serum albumin contains ≥8% aromatic ring amino acids or their derivatives in its structure.

[0010] In some embodiments, the serum albumin comprises gamma-ray treated bovine serum albumin; the irradiation dose is 25 kGy to 35 kGy.

[0011] In some embodiments, the aromatic ring amino acid or its derivative is selected from at least one of phenylalanine, tyrosine, and tryptophan.

[0012] In some embodiments, the mass concentration of the protein in the carbon nanotube protein composite hydrogel is 0.04% to 40%.

[0013] Optionally, the mass concentration of the protein in the carbon nanotube protein composite hydrogel is 5% to 40%. For example, 5%, 10%, 20%, 40%, etc., or any value within the range of 5% to 40%.

[0014] In some embodiments, the hydrophilic carbon nanotubes satisfy at least one of the following conditions: A. The hydrophilic carbon nanotubes include one or more of aminated carbon nanotubes and carboxylated carbon nanotubes; B. The hydrophilic carbon nanotubes are at least one of single-walled carbon nanotubes, multi-walled carbon nanotubes, or their functionalized derivatives.

[0015] Optionally, the hydrophilic carbon nanotubes include at least one of carboxylated multi-walled carbon nanotubes, carboxylated single-walled carbon nanotubes, and aminated multi-walled carbon nanotubes.

[0016] In some embodiments, the hydrophilic carbon nanotubes have a diameter of 1 nm to 5 nm and a length of 1 μm to 30 μm.

[0017] In some embodiments, the mass concentration of the hydrophilic carbon nanotubes in the carbon nanotube-protein composite hydrogel is 0.01% to 20%.

[0018] Optionally, the mass concentration of the hydrophilic carbon nanotubes in the carbon nanotube-protein composite hydrogel is 0.05% to 1%. For example, 0.05%, 0.5%, 1%, etc., or any value within the range of 0.05% to 1%.

[0019] In some embodiments, the mass ratio of the protein to the hydrophilic carbon nanotubes is (5~40):(0.05~1).

[0020] In some embodiments, the carbon nanotube protein composite hydrogel has an electrical conductivity ≥1 μS / cm at room temperature.

[0021] A second aspect of this invention provides a method for preparing a carbon nanotube-protein composite hydrogel, comprising at least the following steps: S1. Provide a dispersion containing hydrophilic carbon nanotubes; S2. Disperse the protein in the dispersion to obtain a carbon nanotube protein complex; S3. The carbon nanotube protein complex is irradiated with near-infrared light to obtain the carbon nanotube protein complex hydrogel.

[0022] In some embodiments, S1 includes: placing hydrophilic carbon nanotubes in a solvent for vortexing or ultrasonic treatment to obtain a dispersion containing hydrophilic carbon nanotubes.

[0023] In some embodiments, the solvent includes a phosphate buffer solution having a pH of 7.2 to 7.4.

[0024] In some embodiments, the vortex oscillation treatment time is 5 min to 100 min; the ultrasonic treatment power is 100 W to 1000 W and the treatment time is 5 min to 100 min.

[0025] In some embodiments, the wavelength of the near-infrared light is 780nm~2526nm, and the illumination power is 10mW / cm². 2 ~1000mW / cm 2 The illumination time is 10s to 1000s.

[0026] In this invention, during near-infrared light irradiation, the temperature of the carbon nanotube protein complex rises to 37°C~50°C, and the gelation time does not exceed 5 minutes.

[0027] The third aspect of this invention provides an application of carbon nanotube protein composite hydrogels in the preparation of biomedical materials and flexible electronic devices.

[0028] Before near-infrared light irradiation, the present invention can inject or extrude the carbon nanotube protein complex into the target application environment, and then perform infrared-triggered gelation to achieve in-situ gelation.

[0029] Beneficial effects 1. In this invention, hydrophilic carbon nanotubes are combined with proteins containing aromatic amino acids through π-π interactions to form a stable complex, which solves the problem of easy aggregation and sedimentation of carbon nanotubes in aqueous solution and significantly improves dispersion stability.

[0030] 2. This invention controls the proportion of aromatic cyclic amino acids or their derivatives in the protein structure to ≥4%, ensuring effective binding of carbon nanotubes to proteins and achieving rapid gelation induced by near-infrared light. Aromatic cyclic amino acids provide binding sites; insufficient proportions result in weak binding forces, causing carbon nanotubes to fail to stably anchor on the protein surface and preventing the subsequent photothermal-induced self-assembly process from being triggered.

[0031] 3. The carbon nanotube protein composite hydrogel provided by this invention is irradiated with near-infrared light. After the carbon nanotubes absorb the near-infrared light, they generate a local photothermal effect, which raises the temperature of the system to 37~50℃, triggering the thermal self-assembly of high-concentration protein molecular chain segments to form a three-dimensional network structure. This allows the system to achieve rapid gelation within 5 minutes without the need for chemical cross-linking agents or chemical modification of the main protein material, thus avoiding toxic residues.

[0032] 4. The carbon nanotube protein composite hydrogel provided by the present invention has the characteristic of cyclic heating and cooling, and can maintain a stable gel morphology under the conditions of 37℃~50℃.

[0033] 5. The carbon nanotube-protein composite hydrogel provided by this invention has an electrical conductivity of ≥1μS / cm, and the carbon nanotubes form a continuous conductive network, which is suitable for the fabrication of flexible electronic devices.

[0034] 6. The carbon nanotube protein composite hydrogel provided by the present invention can be injected or extruded into the target application environment, and then infrared-triggered gelation can be performed to achieve in-situ gelation, which can be applied to the preparation of biomaterials. Attached Figure Description

[0035] Figure 1 This is the amino acid sequence diagram of BSA in Example 1.

[0036] Figure 2 This is a comparison of the stability of carbon nanotube protein complexes in Examples 1-3. From left to right in the figure, they represent Example 2, Example 1, and Example 3.

[0037] Figure 3Figures show the gelation performance test results of Examples 1, 2, and Comparative Example 1. Figure a is a schematic diagram of the gelation of carbon nanotube protein complexes irradiated with near-infrared light; b and d correspond to Comparative Example 1, Example 2, and Example 1, respectively.

[0038] Figure 4 The graphs show the gelation performance test results for Examples 4-6. In the graphs, a and b, from left to right, correspond to the states of Examples 4-6 before near-infrared light irradiation; c, from left to right, corresponds to the gelation state of Examples 4-6 after near-infrared light irradiation.

[0039] Figure 5 The graphs show the gelation performance test results for Examples 7 and 8. In the graphs, a and b, from left to right, correspond to the states of Examples 7 and 8 before near-infrared light irradiation, respectively; c, from left to right, corresponds to the gelation state of Examples 7 and 8 after near-infrared light irradiation, respectively.

[0040] Figure 6 The graphs show the gelation performance test results for Comparative Examples 2-6. In the graphs, a and b, from left to right, correspond to the state of Comparative Examples 2-4 before near-infrared light irradiation; c, from left to right, corresponds to the gelation state of Comparative Examples 2-4 after near-infrared light irradiation; d and e, from left to right, correspond to the state of Comparative Examples 5-6 before near-infrared light irradiation; and f, from left to right, corresponds to the gelation state of Comparative Examples 5-6 after near-infrared light irradiation.

[0041] Figure 7 The graphs show the gelation performance of Comparative Examples 7-14. In the graphs, a and b, from left to right, correspond to the state of Comparative Examples 7-10 before near-infrared light irradiation; c, from left to right, corresponds to the gelation state of Comparative Examples 7-10 after near-infrared light irradiation; d and e, from left to right, correspond to the state of Comparative Examples 11-14 before near-infrared light irradiation; and f, from left to right, corresponds to the gelation state of Comparative Examples 11-14 after near-infrared light irradiation.

[0042] Figure 8 The amino acid sequence diagram of RCC in Comparative Example 7 is shown.

[0043] Figure 9 This is a conductivity test diagram for Example 4. Detailed Implementation

[0044] To make the objectives, technical solutions, and advantages of this invention clearer, the invention will be further described in detail below with reference to embodiments and accompanying drawings. It should be understood that the specific embodiments described herein are merely illustrative of the invention and are not intended to limit the invention. Experimental methods not specifying specific conditions in the embodiments were performed under conventional conditions or conditions recommended by the manufacturer. Reagents not specifying manufacturers are all commercially available conventional products.

[0045] Example 1 The first aspect of this example provides a carbon nanotube protein composite hydrogel, the raw materials of which include carboxylated multi-walled carbon nanotubes and bovine serum albumin (BSA). The bovine serum albumin contains 8.89% aromatic ring amino acids.

[0046] The bovine serum albumin has a purity of >96%, a molecular weight of 66.4 kDa, is derived from Aladdin, and is of biotechnology grade.

[0047] The carboxylated multi-walled carbon nanotubes in the composite hydrogel have a mass concentration of 0.5% and are sourced from Shenzhen Suiheng Technology Co., Ltd., with a purity of 99%.

[0048] The bovine serum albumin concentration in the composite hydrogel is 10%.

[0049] The second aspect of this example provides a method for preparing a carbon nanotube protein composite hydrogel, including the following steps: S1. Carboxylated multi-walled carbon nanotubes were placed in phosphate buffer (PBS, pH 7.3) to prepare a solution with a mass concentration of 0.5% CNT; then dispersed under ultrasonic treatment at a power of 500W and a frequency of 40kHz for 10 minutes at room temperature to obtain a carboxylated multi-walled carbon nanotube dispersion. S2. Disperse bovine serum albumin in the carboxylated multi-walled carbon nanotube dispersion to obtain a carbon nanotube protein complex with a BSA mass concentration of 10%. S3. Irradiate the carbon nanotube protein complex with near-infrared light at 808 nm for 60 s to obtain the carbon nanotube protein complex hydrogel.

[0050] The third aspect of this example provides an application of carbon nanotube protein composite hydrogels in the fabrication of biomedical materials and flexible electronic devices.

[0051] Figure 1 The image shows the amino acid sequence of BSA in Example 1. BSA contains a total of 607 amino acids: 30 phenylalanine (code F, highlighted in yellow in the image); 21 tyrosine (code Y, highlighted in green in the image); and 3 tryptophan (code W, highlighted in red in the image). The proportion of amino acids containing aromatic rings is 8.89%.

[0052] Example 2 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 0.1%.

[0053] Example 3 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 1%.

[0054] Example 4 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 0.05%.

[0055] The bovine serum albumin concentration in the composite hydrogel is 5%.

[0056] Example 5 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 0.05%.

[0057] The bovine serum albumin concentration in the composite hydrogel is 10%.

[0058] Example 6 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 0.05%.

[0059] The bovine serum albumin concentration in the composite hydrogel is 20%.

[0060] Example 7 The specific implementation method in this example is the same as in Example 5, except that the protein is bovine serum albumin treated with gamma rays; the irradiation dose is 25 kGy.

[0061] Example 8 The specific implementation method in this example is the same as in Example 5, except that the protein is bovine serum albumin treated with gamma rays; the irradiation dose is 35 kGy.

[0062] Comparative Example 1 The specific implementation method in this example is the same as in Example 1, except that the mass concentration of the carboxylated multi-walled carbon nanotubes in the composite hydrogel is 0%.

[0063] Comparative Example 2 This example provides a bovine serum albumin solution, which consists of the following steps: using the bovine serum albumin from Example 1, preparing it with PBS (pH 7.3), vortexing for 10 min (Vortex setting 10), to obtain a BSA solution with a mass concentration of 10%.

[0064] Comparative Example 3 The specific implementation method in this example is the same as that in Comparative Example 2, except that the mass concentration of the BSA solution is 20%.

[0065] Comparative Example 4 The specific implementation method in this example is the same as that in Comparative Example 2, except that the mass concentration of the BSA solution is 40%.

[0066] Comparative Example 5 This example provides a gamma-ray treated bovine serum albumin solution, which consists of the following steps: 1. Raw material: gamma-ray treated bovine serum albumin from Example 7; 2. Weigh the gamma-ray treated bovine serum albumin, prepare it with PBS (pH 7.3), vortex for 10 min (Vortex setting 10) to obtain a gamma-ray treated bovine serum albumin solution with a mass concentration of 10%.

[0067] Comparative Example 6 The specific implementation method in this example is the same as that in Comparative Example 5, except that the irradiation dose of the gamma-ray treated bovine serum albumin is 35 kGy.

[0068] Comparative Example 7 The specific implementation method of this example is the same as that of Example 5, except that the protein is recombinant human type III collagen (RCC), and the proportion of aromatic ring amino acids in the recombinant human type III collagen is 3.07%.

[0069] Figure 8 This is the amino acid sequence diagram of RCC. It contains 23 phenylalanines (code F, highlighted in yellow in the diagram); 15 tyrosines (code Y, highlighted in green in the diagram); and 7 tryptophans (code W, highlighted in red in the diagram). The proportion of amino acids containing aromatic rings in RCC is 3.07%.

[0070] Comparative Example 8 The specific implementation method in this example is the same as that in Comparative Example 7, except that the mass concentration of the carboxylated multi-walled carbon nanotubes is 0.1%.

[0071] Comparative Example 9 The specific implementation method in this example is the same as that in Comparative Example 7, except that the mass concentration of the carboxylated multi-walled carbon nanotubes is 0.5%.

[0072] Comparative Example 10 The specific implementation method in this example is the same as that in Comparative Example 7, except that the mass concentration of the carboxylated multi-walled carbon nanotubes is 1%.

[0073] Comparative Example 11 The specific implementation method in this example is the same as that in Comparative Example 2, except that the protein is recombinant type III collagen with a mass concentration of 5%.

[0074] Comparative Example 12 The specific implementation method in this example is the same as that in Comparative Example 2, except that the protein is recombinant human type III collagen with a mass concentration of 10%.

[0075] Comparative Example 13 The specific implementation method in this example is the same as that in Comparative Example 2, except that the protein is recombinant human type III collagen with a mass concentration of 20%.

[0076] Comparative Example 14 The specific implementation method in this example is the same as that in Comparative Example 2, except that the protein is recombinant human type III collagen with a mass concentration of 40%.

[0077] Performance testing 1. Stability detection of carbon nanotube protein complexes: The state of the carbon nanotube protein complexes prepared in step S2 of Examples 1-3 was observed after standing for 0-12 hours. The results are shown in the figure. Figure 2 .

[0078] The mass concentrations of CNTs in the figure, from left to right, are 0.1% (Example 2), 0.5% (Example 1), and 1% (Example 3), while the mass concentration of BSA is 10% for all cases. As shown in the figure, all CNT solutions remained stably dispersed within 4 hours without stratification; however, at 12 hours, Example 2 showed stratification on the surface (marked in red).

[0079] 2. Gel formation performance test: Take 2 mL of the carbon nanotube-protein complexes prepared in step S2 of Examples 1, 2, 4-8, and Comparative Examples 1-14 respectively into glass vials, stir at 300 rpm for 0.5 h, and then take 100 μL of the solution into an EP tube at room temperature. Irradiate the solution with 808 nm near-infrared light for 60 s. Confirm the gelation of the material by inverting the vial. The test results are shown in […]. Figure 3-7 .

[0080] As can be seen from the figures, the embodiments of this application can achieve in-situ gelation after near-infrared light irradiation triggering gelation. However, Comparative Examples 1-6 did not add carboxylated multi-walled carbon nanotubes for composite formation, and therefore could not form a stable gel structure under near-infrared light irradiation, remaining in a solution state. In Comparative Examples 7-10, the proportion of aromatic ring amino acids in recombinant human type III collagen was only 3.07%, resulting in insufficient binding force with carbon nanotubes, and thus the photothermal-induced self-assembly process could not be triggered, ultimately failing to form a gel. Comparative Examples 11-14 consisted only of solutions of recombinant human type III collagen, which also could not trigger the photothermal-induced self-assembly process and failed to form a gel.

[0081] 3. Conductivity test: 1 mL of the carbon nanotube-protein complex obtained in step S2 of Example 4 was added to the letter frame of an A4 sheet of paper; it was then placed in a fume hood and dried overnight to obtain a flexible circuit. The resistance of the material was measured using a multimeter (DLX-890D) switched to resistance measurement mode (ohm range, 2MΩ range). A short-circuit probe was used to check if the resistance was 0Ω, and an open probe was used to check if the resistance was infinite. The two probes of the multimeter were connected to the two ends of the sample respectively to test its conductivity. The test results are shown below. Figure 9 See Table 1.

[0082] Table 1

[0083] As can be seen from the data in the table above, the carbon nanotube protein composite hydrogel prepared in Example 4 forms a continuous conductive network with a conductivity ≥1μS / cm, which can be applied to the fabrication of flexible electronic devices.

Claims

1. A carbon nanotube-protein composite hydrogel, characterized in that, The raw materials used in the preparation include hydrophilic carbon nanotubes and proteins; The protein includes the following characteristics: A. The protein includes one or more of serum albumin, decellularized matrix protein, or derivatives thereof; B. The protein contains ≥4% aromatic ring amino acids or their derivatives in its structure.

2. The carbon nanotube protein composite hydrogel according to claim 1, characterized in that, The serum albumin includes bovine serum albumin, wherein the bovine serum albumin contains ≥8% aromatic ring amino acids or their derivatives in its structure.

3. The carbon nanotube protein composite hydrogel according to claim 1, characterized in that, The mass concentration of the protein in the carbon nanotube protein composite hydrogel is 0.04% to 40%.

4. The carbon nanotube protein composite hydrogel according to claim 3, characterized in that, The mass concentration of the hydrophilic carbon nanotubes in the carbon nanotube-protein composite hydrogel is 0.01% to 20%.

5. The carbon nanotube protein composite hydrogel according to claim 1, characterized in that, The hydrophilic carbon nanotubes satisfy at least one of the following conditions: A. The hydrophilic carbon nanotubes include one or more of aminated carbon nanotubes and carboxylated carbon nanotubes; B. The hydrophilic carbon nanotubes are at least one of single-walled carbon nanotubes, multi-walled carbon nanotubes, or their functionalized derivatives.

6. A method for preparing a carbon nanotube protein composite hydrogel according to any one of claims 1-5, characterized in that, At least the following steps are included: S1. Provide a dispersion containing hydrophilic carbon nanotubes; S2. Disperse the protein in the dispersion to obtain a carbon nanotube protein complex; S3. The carbon nanotube protein complex is irradiated with near-infrared light to obtain the carbon nanotube protein complex hydrogel.

7. The method for preparing the carbon nanotube protein composite hydrogel according to claim 6, characterized in that, The near-infrared light has a wavelength of 780nm~2526nm and an illumination power of 10mW / cm². 2 ~1000mW / cm 2 The illumination time is 10s to 1000s.

8. The method for preparing the carbon nanotube protein composite hydrogel according to claim 6, characterized in that, S1 includes: placing hydrophilic carbon nanotubes in a solvent for vortex oscillation or ultrasonic treatment to obtain a dispersion containing hydrophilic carbon nanotubes.

9. The method for preparing the carbon nanotube protein composite hydrogel according to claim 8, characterized in that, The vortex oscillation treatment lasts for 5 to 100 minutes; the ultrasonic treatment has a power of 100W to 1000W and a treatment time of 5 to 100 minutes.

10. An application of the carbon nanotube protein composite hydrogel according to any one of claims 1-5, characterized in that, It is used in the preparation of biomedical materials and flexible electronic devices.

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