Amyloid-like protein mediated long-acting metal organic framework antifouling agent as well as preparation method and application thereof

Abstract

The invention discloses an amyloid-like protein mediated long-acting metal organic framework antifouling agent as well as a preparation method and application thereof. Belongs to the field of marine antifouling material preparation. The anti-fouling agent is based on MOF with an anti-fouling function, and amyloid-like protein is self-assembled on the surface of the MOF to form a compact protective shell layer. According to the preparation method, metal ions and organic ligands react and are connected through coordinate bonds to form an MOF structure, and MOF particles are obtained through centrifugation, collection, precipitation, washing and drying; under the action of a water-soluble organic reducing substance, the protein completely opens a disulfide bond to form an unfolded protein chain, and the protein chain is self-assembled to obtain an amyloid-like protein solution; and placing the MOF particles in an amyloid-like protein solution, and carrying out simple one-step incubation to obtain the amyloid-like protein mediated long-acting metal organic framework antifouling agent. The antifouling agent is prepared by adopting a novel green, high-stability, rapid and efficient mild modification method, and has the advantages of stability, durability, universality and high efficiency.

Description

TECHNICAL FIELD

[0001] The present application belongs to the field of marine antifouling agent material preparation, and particularly relates to a long-acting metal-organic framework antifouling agent mediated by amyloid-like proteins and a preparation method and application thereof. BACKGROUND

[0002] The harm of marine biofouling has been valued by countries around the world for many years, and is a worldwide problem that mankind has faced since engaging in marine activities. In the field of marine industry, the secretions released by marine fouling organisms such as plants, animals and microorganisms cause microbial corrosion, leading to reduced work efficiency and shortened service life of marine equipment. The attachment of marine fouling organisms also increases the resistance of ships during navigation, leading to reduced maneuverability, increased fuel consumption and huge economic losses. Moreover, it also brings problems such as sonar interference, safety hazards, and more seriously, damage to the marine ecosystem. Marine biofouling often causes great harm to coastal industries, marine transportation, marine pipelines and fisheries.

[0003] At present, antifouling agents are the most feasible and effective method to solve the problem of biofouling in terms of technology and economy. The use of marine antifouling agents began with early toxic substances such as arsenic and mercury, but the antifouling effect was limited. The emergence of high-efficiency organotin antifouling agents in the 20th century brought a revolutionary breakthrough, significantly reducing ship resistance. However, with the increasing awareness of environmental protection, people found that toxic antifouling agents such as tributyltin would accumulate in marine organisms, eventually causing harm to the marine ecosystem, so toxic antifouling agents were banned. Thereafter, the industry shifted to copper oxide-based antifouling agents, which reduced environmental risks, but the sudden release of copper ions and high toxicity still threatened the nearshore ecosystem. In recent years, marine antifouling agents have focused on biomimetic design and smart response materials, but the emerging environmentally friendly technology lacks stability in complex marine environments, has poor antifouling effect and high cost, which restricts industrialization. The current core challenge is to develop new materials that can effectively prevent fouling, are uniform and stable, have environmental friendliness and cost control, to balance the needs of marine industry and ecological protection.

[0004] Metal-organic frameworks (MOFs) are composed of metal ions and organic ligands, which can provide abundant active sites due to their tunable porous structure and high specific surface area, and show great potential in the field of antifouling: they can achieve efficient antifouling by releasing metal ions / antifouling ligands or loading antifouling active substances. However, most MOFs are prone to structural decomposition in complex marine environments such as seawater, acid and alkali, and have two major defects of poor stability and excessive release of antifouling components, which seriously restricts their practical application. To break through the short-term bottleneck of MOFs, building a protective shell for slow release is a key strategy. However, existing modification techniques face significant challenges: polymer brush grafting method: low grafting density, large solvent consumption (such as DMF / THF), and biological toxicity caused by catalyst residues; Capsule encapsulation method: MOF structure is prone to collapse, low coating efficiency and unstable interface bonding; Coordination crosslinking method: highly dependent on specific MOF surface metal sites, limited universality. Therefore, developing a green, high-stability, fast and efficient mild modification method has become the core direction of functional modification of MOF antifouling agents.

[0005] Amyloid-like protein assembly system can modify the surface of micro-nano particles, which has the characteristics of mild and controllable assembly conditions, fast speed, and greatly reduced material and process cost, and can successfully adhere to organic, inorganic, metal and living cells and other micro-nano particles. SUMMARY

[0006] In view of the problems existing in the prior art, the present application aims to provide an innovative strategy for functionalizing the surface of MOFs using an amyloid-like protein-mediated surface modification system, and provides an amyloid-like protein-mediated long-acting metal-organic framework antifouling agent, a preparation method and application thereof. The preparation method can prepare low-cost, biocompatible nanoscale protein oligomers, which spontaneously assemble into dense amyloid-like protein aggregates on the surface of MOFs through hydrophobic interaction, thereby successfully modifying the MOF particles. A simple, controllable, long-acting and environmentally friendly MOF antifouling agent is developed, and the preparation method can modify various MOF materials in a green, mild and universal manner, while maintaining high antifouling activity, significantly improving stability, and strengthening environmental friendliness, breaking through the limitations of short-acting and high environmental cost of traditional MOF antifouling agents, and providing a new paradigm for developing long-acting and green marine antifouling materials.

[0007] The purpose of the present application is achieved by the following technical solutions:

[0008] In a first aspect, the present application provides an amyloid-like protein-mediated long-acting metal-organic framework antifouling agent based on MOF with antifouling function, and the amyloid-like protein self-assembles on the surface of MOF to form a dense protective shell.

[0009] Further, the MOF with the anti-fouling function is MOF-5, MOF-74, HKUST-1, Ag-MOF, ZIF-8, UiO-66, PCN-222, or MIL-100, etc.

[0010] In a second aspect, the present application also provides a preparation method of the amyloid-like protein-mediated long-acting metal organic framework anti-fouling agent, comprising the following steps:

[0011] Preparation of the MOF:

[0012] The metal ions and the organic ligand are respectively added into a polar solvent to form a uniform solution by stirring, and then the metal ion solution is added into the organic ligand solution to form a MOF structure by the coordination bond between the metal ions and the organic ligand. After the reaction, the MOF particles are obtained by centrifugation, collection, precipitation, washing, and drying.

[0013] Preparation of the amyloid-like protein (ALP):

[0014] The protein is dissolved in a buffer to form a uniform solution by stirring, and then an excess of water-soluble organic reducing agent is added. After mixing, the natural protein is completely opened by the action of the reducing agent to form an unfolded protein chain, which exposes a large number of chemical groups and self-assembles into a nanoscale oligomer with interfacial activity. Subsequently, the amyloid-like protein solution is obtained by self-assembly.

[0015] Surface modification of the MOF:

[0016] The MOF particles are incubated in the amyloid-like protein solution, and the nanoscale protein oligomer is combined with the MOF particle surface by the strong bond of chemical bonds to realize the modification of the MOF surface. After the reaction, the amyloid-like protein-mediated long-acting metal organic framework anti-fouling agent (hereinafter referred to as MOF@ALP) is obtained by centrifugation, collection, precipitation, washing, and drying.

[0017] Further, the metal ions in the preparation of the MOF are Zn 2+ , Cu 2+ , Ag + , Fe 3+ , or Zr 4+ .

[0018] The organic ligand is 2-methylimidazole (2-MI), terephthalic acid (H2BDC), porphyrin tetracarboxylic acid (H4TCPP), 2,5-dihydroxyterephthalic acid (H4DHBDC), or 1,3,5-benzene tricarboxylic acid (H3BDC).

[0019] The solvent is H2O, ethanol, or N,N-dimethylformamide (DMF).

[0020] Further, the molar ratio of metal ions and organic ligands in the preparation of MOF is 1:(4-12), the reaction time is 4h-36h, the reaction temperature is 20℃-120℃, the centrifugation condition is 8000rpm-12000rpm for 5min-20min, and the drying temperature is 60℃-120℃.

[0021] Further, the protein in the preparation of amyloid-like protein is serum albumin, lysozyme, alpha-lactalbumin, insulin, beta-lactoglobulin, oat protein or soybean protein, etc.

[0022] The buffer is Hepes buffer or Tris buffer.

[0023] The water-soluble organic reducing substance is tris(2-carboxyethyl)phosphonium hydrochloride (TCEP) or L-cysteine (L-Cysteine).

[0024] Further, the concentration of the protein in the preparation of amyloid-like protein is 0.1mg / mL-40mg / mL.

[0025] The concentration of the buffer is 10mM-50mM.

[0026] Further, the incubation in the surface modification of MOF adopts a simple one-step method.

[0027] The mass-volume ratio mg:mL of MOF particles to amyloid-like protein is 10:(1-10).

[0028] The reaction time of incubation in the surface modification of MOF is 10min-120min.

[0029] The centrifugation condition is 8000rpm-12000rpm for 5min-20min.

[0030] The drying temperature is 60℃-120℃.

[0031] In a third aspect, the application further provides a use of the amyloid-like protein-mediated long-acting metal-organic framework antifouling agent in the field of marine antifouling.

[0032] Further, when the addition amount of the amyloid-like protein-mediated long-acting metal-organic framework antifouling agent is ≥150mg / L, the bacterial survival rate of anti-Vietnamese Bacillus and anti-Pseudomonas aeruginosa is <9%.

[0033] Compared with the prior art, the application has the following beneficial effects:

[0034] 1、The MOF has antifouling performance, and the MOF is modified by the amyloid-like protein after being synthesized, so that the amyloid-like protein provides a natural armor for the MOF, and the stability of the antifouling agent in a complex marine environment is greatly improved.

[0035] 2、The amyloid-like protein system is used for modifying the MOF, a universal modification method is developed, and the method is suitable for MOF-5, MOF-74, HKUST-1, Ag-MOF, ZIF-8, UiO-66, PCN-222, MIL-100 and other MOFs, and the crystal type is broken through.

[0036] 3、The amyloid-like protein is selected for modifying the MOF, and the amyloid-like protein spontaneously assembles into a dense protective shell on the surface of the MOF, and the method has the characteristics of mild and controllable assembly conditions, fast speed and greatly reduced material and process cost.

[0037] 4、The amyloid-like protein-mediated long-acting metal organic framework antifouling agent provided by the application adopts a green, high-stability, rapid and efficient mild modification method, has stability, durability, universality and high efficiency, and provides a path for the development of a high-efficiency and stable green antifouling agent in marine engineering. BRIEF DESCRIPTION OF DRAWINGS

[0038] Figure 1 A scanning electron microscope (SEM) image of ZIF-8 particles prepared in Example 1;

[0039] Figure 2 A scanning electron microscope (SEM) image of ZIF-8@ALP prepared in Example 1;

[0040] Figure 3 A transmission electron microscope (TEM) image of ZIF-8 particles prepared in Example 1;

[0041] Figure 4 A transmission electron microscope (TEM) image of ZIF-8@ALP prepared in Example 1;

[0042] Figure 5 An element distribution (TEM-EDS) image of ZIF-8 particles prepared in Example 1;

[0043] Figure 6 An element distribution (TEM-EDS) image of ZIF-8@ALP prepared in Example 1;

[0044] Figure 7 X-ray diffraction (XRD) images of ZIF-8 particles and ZIF-8@ALP prepared in Example 1;

[0045] Figure 8Infrared spectrum of ZIF-8 particles and ZIF-8@ALP prepared for Example 1;

[0046] Figure 9 Comparison chart of sustained-release effect of ZIF-8 particles and ZIF-8@ALP prepared for Example 1;

[0047] Figure 10 Scanning electron microscope (SEM) images of ZIF-8 particles prepared for Example 1 for stability test, wherein: (a) is the SEM image under pH = 5 environment, (b) is the SEM image under pH = 7 environment, (c) is the SEM image under pH = 13 environment;

[0048] Figure 11 Scanning electron microscope (SEM) images of ZIF-8@ALP prepared for Example 1 for stability test, wherein: (a) is the SEM image under pH = 5 environment, (b) is the SEM image under pH = 7 environment, (c) is the SEM image under pH = 13 environment;

[0049] Figure 12 Bacterial survival rate change chart of ZIF-8 particles and ZIF-8@ALP prepared for Example 1 for Bacillus vietnamiensis antibacterial effect test;

[0050] Figure 13 Bacterial survival rate change chart of ZIF-8 particles and ZIF-8@ALP prepared for Example 1 for Pseudomonas aeruginosa antibacterial effect test. DETAILED DESCRIPTION

[0051] The specific embodiments of the present application will be further described in detail below with reference to the accompanying drawings and examples.

[0052] A long-acting metal-organic framework antifouling agent mediated by amyloid-like proteins, based on MOF with antifouling function, including MOF-5, MOF-74, HKUST-1, Ag-MOF, ZIF-8, UiO-66, PCN-222 or MIL-100, and the amyloid-like proteins self-assemble on the surface of the MOF to form a dense protective shell.

[0053] A preparation method of a long-acting metal-organic framework antifouling agent mediated by amyloid-like proteins, including the following steps:

[0054] Preparation of MOF:

[0055] The metal ion and the organic ligand are added into a polar solvent respectively, stirred to form a uniform solution, then the metal ion solution is added into the organic ligand solution, the molar ratio of the metal ion and the organic ligand is 1:(4-12), stirred uniformly, reacted at 20-120℃ for 4-36h, the metal ion and the organic ligand are connected through coordination bond to form a MOF structure, after the reaction is completed, centrifuged at 8000-12000rpm for 5-20min, then collected, precipitated, washed, and dried at 60-120℃ to obtain MOF particles;

[0056] Preparation of amyloid-like proteins:

[0057] The protein (0.1-40mg / mL) is dissolved in Hepes buffer (10-50mM) or Tris buffer (10-50mM), the protein includes serum albumin, lysozyme, alpha-lactalbumin, insulin, beta-lactoglobulin, oat protein or soybean protein, stirred to form a uniform solution, then an excess of water-soluble organic reducing agent tris (2-carboxyethyl) phosphonium hydrochloride or L-cysteine is added, after the two are mixed, the natural protein is completely opened in the presence of the reducing agent, the disulfide bond is opened, the unfolded protein chain is exposed to abundant chemical groups, self-assembled into an interface-active nanoscale oligomer, and then self-assembled to obtain an amyloid-like protein solution;

[0058] Surface modification of MOF:

[0059] The MOF particles are placed in the amyloid-like protein solution for simple one-step incubation for 10-120min, the mass-volume ratio mg:mL of the MOF particles and the amyloid-like protein is 10:1-10, the unfolded nanoscale protein oligomer is combined with the surface of the MOF particles through the strong bond of chemical bonds, the surface of the MOF is modified, after the reaction is completed, centrifuged at 8000-12000rpm for 5-20min, then collected, precipitated, washed, and dried at 60-120℃ to obtain an amyloid-like protein-mediated long-acting metal organic framework antifouling agent, hereinafter referred to as MOF@ALP.

[0060] The application of the amyloid-like protein-mediated long-acting metal organic framework antifouling agent in the field of marine antifouling, when the addition amount is ≥150mg / L, the bacterial survival rate of anti-Vietnamese bacillus and Pseudomonas aeruginosa is <9%.

[0061] The MOF-based marine antifouling agent can select different metal ions and organic ligands, design the morphology and size of the MOF by exploring the reaction conditions and reactants, and then realize the controllable regulation of the MOF; the amyloid-like protein is selected to modify the surface of the MOF, the amyloid-like protein (ALP) is combined with the surface of the MOF particle through the strong bond of various chemical bonds, which provides a natural armor for the MOF, and greatly improves the stability of the antifouling agent in the complex marine environment.

[0062] Based on this, the structure and function of the MOF itself are designed, metal ions or organic ligands with bactericidal properties are selected, and the release of the metal and the ligand has an antifouling effect. The amyloid-like protein is used to modify the surface of the MOF, and a large number of groups are exposed after the unfolding of the protein, which is combined with the MOF particle through the strong bond between these chemical bonds, and the amyloid-like protein is spontaneously assembled into a dense amyloid-like protein aggregate on the surface of the MOF.

[0063] Example 1

[0064] An amyloid-like protein-mediated long-acting metal organic framework antifouling agent, the amyloid-like protein is self-assembled on the surface of ZIF-8 to form a dense protective shell.

[0065] A preparation method of an amyloid-like protein-mediated long-acting metal organic framework antifouling agent, specifically comprising the following steps:

[0066] Preparation of MOF:

[0067] Zn 2+ and 2-methylimidazole are added to deionized water respectively, and stirred to form a uniform solution, wherein the molar ratio of Zn 2+ and 2-methylimidazole is 1:8, then the Zn 2+ solution is added to the 2-methylimidazole solution and magnetically stirred, and stirred uniformly, and reacted at 20℃ for 4h, after the reaction is completed, centrifuged at 8000rpm for 5min, collect the precipitate and wash with deionized water three times, and dry at 60℃ to obtain ZIF-8 particles.

[0068] Preparation of amyloid-like protein:

[0069] 0.1mg / mL of bovine serum albumin is dissolved in 10mM of Hepes buffer, magnetically stirred to form a uniform solution, and 50mM of reducing agent tris (2-carboxyethyl) phosphonium hydrochloride is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0070] Surface modification of MOF:

[0071] 10mg of ZIF-8 particles were placed in 10mL amyloid-like protein solution for simple one-step incubation, the amyloid-like protein was combined with the surface of ZIF-8 particles through strong bonding of various chemical bonds, after 120min of reaction, centrifugation was performed at 8000rpm for 5min, the precipitate was collected and washed with deionized water three times, and dried at 60℃ to obtain ZIF-8@ALP.

[0072] Characterization test:

[0073] The ZIF-8 particles and ZIF-8@ALP prepared in this embodiment 1 were subjected to scanning electron microscope test, as shown in Figure 1 , the ZIF-8 with clear morphology was successfully synthesized, and the particle size was uniform; as shown in Figure 2 , the ZIF-8@ALP was completely wrapped by nano-sized small particles, the combination was firm, and the amyloid-like protein was spontaneously assembled on the surface of ZIF-8.

[0074] The ZIF-8 particles and ZIF-8@ALP prepared in this embodiment 1 were subjected to transmission electron microscope test, as shown in Figure 3 , the morphology of the synthesized ZIF-8 was rhombic dodecahedron, and the boundary was clear; as shown in Figure 4 , compared with the TEM image of ZIF-8 in Figure 3 , it can be observed that the amyloid-like protein formed a stable shell layer on the surface of ZIF-8.

[0075] The ZIF-8 particles and ZIF-8@ALP prepared in this embodiment 1 were subjected to element distribution test, as shown in Figure 5 , the element distribution of ZIF-8 was uniform; as shown in Figure 6 , the element distribution of ZIF-8@ALP was also uniform, indicating that the amyloid-like protein was uniformly distributed on the surface of ZIF-8.

[0076] The ZIF-8 particles and ZIF-8@ALP prepared in this embodiment 1 were subjected to X-ray diffraction test, as shown in Figure 7 , compared with the diffraction peaks on the standard XRD diffraction card of ZIF-8, it can be seen that ZIF-8 and ZIF-8@ALP both showed characteristic diffraction peaks at 7.5°, 10.5° and 12°, proving that the modification of amyloid-like protein did not change the crystal form of ZIF-8.

[0077] The ZIF-8 particles, ALP and ZIF-8@ALP prepared in this embodiment 1 were subjected to infrared spectrum test, as shown in Figure 8 , the ZIF-8 particles and ZIF-8@ALP showed absorption peaks at 3133cm -1 and 2921cm -1The absorption peaks at 424 cm⁻¹ are attributed to the stretching vibrations of the CH bonds in the methyl and imidazole rings, respectively. -1 The absorption peak at 1640 cm⁻¹ belongs to the Zn-N stretching band, and ALP and ZIF-8@ALP have absorption peaks at 1640 cm⁻¹. -1 The absorption peak at this location is a characteristic peak of the β-sheet of amyloid protein, indicating that ZIF-8 and ZIF-8@ALP were successfully synthesized.

[0078] Performance testing:

[0079] The sustained-release performance of ZIF-8@ALP prepared in Example 1 was evaluated, and the Zn content was investigated using the dialysis bag method. 2+ The release rate of Zn was determined using the following experimental steps: ZIF-8 and ZIF-8@ALP were dispersed separately in dialysis bags containing 20 mL of H2O with a molecular weight cutoff of 3500, and immediately transferred to clean beakers. 480 mL of H2O was added to submerge the dialysis bags. The mixture was magnetically stirred at room temperature. Three parallel experiments were conducted (the average value of the test results was taken). At fixed time intervals, 10 mL of the solution was pipetted and stored for later testing. Inductively coupled plasma mass spectrometry (ICP-MS) was used to measure the Zn content. 2+ Release concentration, such as Figure 9 As shown, the results indicate that ZIF-8@ALP has a significantly improved sustained-release effect compared to ZIF-8.

[0080] The stability of ZIF-8@ALP prepared in Example 1 was evaluated. The specific experimental steps are as follows: ZIF-8 and ZIF-8@ALP were dispersed in solutions with pH values ​​of 5, 7, and 13, respectively, and soaked. After reacting at 100 rpm for 24 h in a shaker, the mixture was centrifuged at 8000 rpm for 5 min, washed three times with ultrapure water, and the precipitate was collected and observed under a scanning electron microscope. Figure 10 , Figure 11 As shown, under harsh conditions, ZIF-8@ALP can still maintain morphological integrity and stability compared to ZIF-8, exhibiting superior stability.

[0081] The antibacterial properties of ZIF-8@ALP prepared in Example 1 were evaluated. The antibacterial performance of ZIF-8@ALP was assessed by examining bacterial survival rate. Bacillus vietnamese and Pseudomonas aeruginosa, typical Gram-positive bacteria from the marine environment, were selected as experimental strains. Single colonies were isolated using the streak plate method and cultured at 37°C for 12-16 hours in 2216 E or Luria-Bertani liquid medium until the bacteria reached the logarithmic growth phase. The specific steps of the antibacterial experiment are as follows: Bacteria (initial concentration 10) were... 6ZIF-8 and ZIF-8@ALP at different concentrations (25 mg / L, 50 mg / L, 100 mg / L, 125 mg / L, and 150 mg / L) were co-cultured for 24 h in simulated seawater medium containing yeast extract (1 g / L) and tryptone (1 g / L), respectively. A control group without ZIF-8 and ZIF-8@ALP was used. During the entire culture period, the optical density (OD) at 600 nm was measured. 600 Characterize bacterial growth and explore bacterial survival rate based on the following expression:

[0082] Bacterial survival rate ;

[0083] in OD of the sample processing group 600 value, OD representing the control group 600 value, and These represent the initial OD values ​​of the sample treatment group and the control group, respectively. 600 value.

[0084] like Figure 12 As shown, both ZIF-8 and ZIF-8@ALP in Example 1 exhibited antibacterial effects against Bacillus vivax. Furthermore, the bacterial survival rate decreased with increasing concentration, but ZIF-8@ALP showed superior antibacterial activity compared to ZIF-8. At a concentration of 150 mg / L, the bacterial survival rate of ZIF-8@ALP decreased to 7.57%, while that of ZIF-8 was 11.3%. Figure 13 As shown, both ZIF-8 and ZIF-8@ALP in Example 1 can exert antibacterial effects against Pseudomonas aeruginosa. As the concentration increases, the bacterial survival rate decreases, but the antibacterial effect of ZIF-8@ALP is better than that of ZIF-8. When the concentration is 150 mg / L, the bacterial survival rate of ZIF-8@ALP decreases to 8.95%, while the bacterial survival rate of ZIF-8 is 11.79%.

[0085] Example 2

[0086] A long-lasting metal-organic framework antifouling agent mediated by amyloid protein, wherein amyloid protein self-assembles on the surface of MOF-5 to form a dense protective shell.

[0087] A method for preparing a long-acting metal-organic framework antifouling agent mediated by amyloid protein specifically includes the following steps:

[0088] Preparation of MOFs:

[0089] Zn 2+and terephthalic acid were added into N,N-dimethylformamide, stirred to form a uniform solution, wherein Zn 2+ and terephthalic acid were added into N,N-dimethylformamide, stirred to form a uniform solution, wherein Zn 2+ solution was added into 2-methylimidazole solution, stirred magnetically, stirred uniformly, reacted at 120℃ for 24h, after the reaction was completed, centrifuged at 8000rpm for 10min, collected the precipitate and washed with N,N-dimethylformamide for three times, dried at 80℃ to obtain MOF-5 particles.

[0090] Preparation of amyloid-like protein:

[0091] 25mg / mL of bovine serum albumin was dissolved in 30mM Tris buffer, stirred magnetically to form a uniform solution, 50mM reducing agent L-cysteine was added to completely open the disulfide bond of the protein, and the two were mixed to obtain ALP.

[0092] Surface modification of MOF:

[0093] 10mg of MOF-5 particles were placed in 4mL of amyloid-like protein solution for simple one-step incubation, the amyloid-like protein was combined with the MOF-5 particle surface through strong bonding of various chemical bonds, after 60min of reaction, centrifuged at 8000rpm for 15min, collected the precipitate and washed with deionized water for three times, dried at 80℃ to obtain MOF-5@ALP.

[0094] Characterization test:

[0095] Using the same characterization test method as in Example 1, the MOF-5 with clear morphology and uniform particle size was successfully synthesized in this Example 2, and the MOF-5@ALP was completely wrapped by the nano-sized small particles, the combination was firm, and the amyloid-like protein was spontaneously assembled on the surface of MOF-5; the morphology of the synthesized MOF-5 was octahedral structure with clear boundary, and it could be observed that the amyloid-like protein formed a stable shell layer on the surface of MOF-5; the element distribution of MOF-5 and MOF-5@ALP was uniform, and the amyloid-like protein was uniformly distributed on the surface of MOF-5; compared with the diffraction peaks on the standard XRD diffraction card of MOF-5, both MOF-5 and MOF-5@ALP showed characteristic diffraction peaks at 6.8°, 9.7° and 3.7°, and the modification of amyloid-like protein did not change the crystal form of MOF-5; the absorption peaks of MOF-5 and MOF-5@ALP at 1580cm -1 and 1390cm -1 belonged to the asymmetric and symmetric stretching vibration of the terephthalic acid ligand coordinated with Zn, the peak at 750cm -1 belonged to the out-of-plane bending vibration of the benzene ring ortho-substituted C-H, and the peaks of ALP and MOF-5@ALP at 1640cm -1The absorption peak at that location is a characteristic protein peak of the β-sheet of amyloid protein.

[0096] Performance testing:

[0097] Using the same performance testing methods as in Example 1, the sustained-release effect of MOF-5@ALP in Example 2 was significantly improved compared to MOF-5. Under harsh conditions, MOF-5@ALP maintained its morphological integrity and stability compared to MOF-5, exhibiting superior stability. Both MOF-5 and MOF-5@ALP demonstrated antibacterial effects against Bacillus vivax, and while bacterial survival decreased with increasing concentration, MOF-5@ALP showed superior antibacterial efficacy at a concentration of 150 mg. At a concentration of 150 mg / L, the bacterial survival rate of MOF-5@ALP decreased to 6.98%, while that of MOF-5 was 11.03%. Both MOF-5 and MOF-5@ALP exhibited antibacterial effects against Pseudomonas aeruginosa, and the bacterial survival rate decreased with increasing concentration. However, MOF-5@ALP showed better antibacterial effects than MOF-5. At a concentration of 150 mg / L, the bacterial survival rate of MOF-5@ALP decreased to 7.07%, while that of MOF-5 was 11.37%.

[0098] Example 3

[0099] A long-lasting metal-organic framework antifouling agent mediated by amyloid protein, wherein amyloid protein self-assembles on the surface of HKUST-1 to form a dense protective shell.

[0100] A method for preparing a long-acting metal-organic framework antifouling agent mediated by amyloid protein specifically includes the following steps:

[0101] Preparation of MOFs:

[0102] Cu 2+ 1,3,5-Benzotricarboxylic acid and ethanol were added separately and stirred to form a homogeneous solution, wherein Cu 2+ The molar ratio of Cu to 1,3,5-benzenetricarboxylic acid is 1:12, then Cu 2+ The solution was added to a 1,3,5-benzenetricarboxylic acid solution and magnetically stirred until homogeneous. The mixture was then reacted at 100°C for 12 hours. After the reaction was completed, the mixture was centrifuged at 10,000 rpm for 10 minutes. The precipitate was collected, washed three times with ethanol, and dried at 60°C to obtain HKUST-1 particles.

[0103] Preparation of amyloid proteins:

[0104] Dissolve 15 mg / mL of lysozyme in 20 mM Hepes buffer, stir magnetically to form a homogeneous solution, add 50 mM of the reducing agent L-cysteine ​​to completely open the disulfide bonds of the protein, and mix the two to obtain ALP.

[0105] Surface modification of MOF:

[0106] 10 mg of HKUST-1 particles were placed in 6 mL of amyloid protein solution and incubated in a simple one-step method. The amyloid protein binds to the surface of HKUST-1 particles through strong chemical bonds. After reacting for 40 min, the mixture was centrifuged at 12000 rpm for 15 min, the precipitate was collected and washed three times with deionized water, and then dried at 60 °C to obtain HKUST-1@ALP.

[0107] Characterization tests:

[0108] Using the same characterization and testing methods as in Example 1, Example 3 successfully synthesized HKUST-1 with clear morphology and uniform particle size. HKUST-1@ALP was completely encapsulated by nanoscale particles, exhibiting strong binding, and amyloid proteins spontaneously assembled on the HKUST-1 surface. The synthesized HKUST-1 had an octahedral structure with clear boundaries, and a stable shell of amyloid proteins could be observed forming on the HKUST-1 surface. HKUST-1 and HKUST-1@ALP showed uniform elemental distribution, and amyloid proteins were uniformly distributed on the HKUST-1 surface. Comparison with the diffraction peaks on the standard XRD diffraction card for HKUST-1 showed characteristic diffraction peaks at 6.7°, 9.5°, and 11.6°, indicating that amyloid protein modification did not alter the crystal form of HKUST-1. HKUST-1 and HKUST-1@ALPP showed characteristic diffraction peaks at 1580 cm⁻¹. -1 and 1390cm -1 The absorption peaks at 750 cm⁻¹ are attributed to the asymmetric and symmetric stretching vibrations of the 1,3,5-benzenetricarboxylic acid ligand coordinated with Cu, respectively. -1 The peak at 1640 cm⁻¹ belongs to the out-of-plane bending vibration of CH4 associated with ortho-substituted benzene ring in 1,3,5-benzenetricarboxylic acid. ALP and HKUST-1@ALP peaks at 1640 cm⁻¹ are also observed. -1 The absorption peak at that location is a characteristic protein peak of the β-sheet of amyloid protein.

[0109] Performance testing:

[0110] The HKUST-1@ALP of the present embodiment 3 has a significantly improved slow-release effect compared with HKUST-1 by using the same performance test method as in embodiment 1; compared with HKUST-1, the MOF-5@ALP can still maintain a complete and stable morphology in a harsh environment, and has more excellent stability; both HKUST-1 and HKUST-1@ALP can have an antibacterial effect on Bacillus vietnamensis, and as the concentration increases, the bacterial survival rate shows a downward trend, but the antibacterial effect of HKUST-1@ALP is better than that of HKUST-1, when the concentration is 150 mg / L, the bacterial survival rate of HKUST-1@ALP decreases to 7.83%, while the bacterial survival rate of HKUST-1 is 12.05%; both HKUST-1 and HKUST-1@ALP can also have an antibacterial effect on Pseudomonas aeruginosa, and as the concentration increases, the bacterial survival rate shows a downward trend, but the antibacterial effect of HKUST-1@ALP is better than that of HKUST-1, when the concentration is 150 mg / L, the bacterial survival rate of HKUST-1@ALP decreases to 6.91%, while the bacterial survival rate of HKUST-1 is 11.78%.

[0111] Embodiment 4

[0112] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent, amyloid-like protein is self-assembled on the surface of Ag-MOF to form a dense protective shell layer.

[0113] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent preparation method, specifically includes the following steps:

[0114] Preparation of MOF:

[0115] Ag + And 1,3,5-benzene tricarboxylic acid are added to N,N-dimethylformamide, stirred to form a uniform solution, wherein the molar ratio of Ag + And 1,3,5-benzene tricarboxylic acid is 1:6, then Ag + Solution is added to 1,3,5-benzene tricarboxylic acid solution and magnetically stirred, stirred uniformly, reacted at 120 DEG C for 24 h, after the reaction, centrifuged at 8000 rpm for 20 min, collected the precipitate and washed with N,N-dimethylformamide three times, dried at 60 DEG C to obtain Ag-MOF particles.

[0116] Preparation of amyloid-like protein:

[0117] 35 mg / mL of oat protein is dissolved in 40 mM Hepes buffer, magnetically stirred to form a uniform solution, 50 mM reducing substance L-cysteine is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0118] Surface modification of MOF:

[0119] 10 mg of Ag-MOF particles were placed in 2 mL of amyloid-like protein solution for simple one-step incubation, and the amyloid-like protein was combined with the Ag-MOF particle surface through strong bonding of various chemical bonds. After 20 min of reaction, centrifugation was performed at 8000 rpm for 5 min, the precipitate was collected and washed with deionized water three times, and drying was performed at 60°C to obtain Ag-MOF@ALP.

[0120] Characterization test:

[0121] Using the same characterization test method as in Example 1, the Ag-MOF with clear morphology and uniform particle size was successfully synthesized in this embodiment 4, and the Ag-MOF@ALP was completely wrapped by the nano-sized small particles, and the combination was firm, and the amyloid-like protein was spontaneously assembled on the surface of the Ag-MOF; the morphology of the synthesized Ag-MOF was a cubic structure with clear boundaries, and it could be observed that the amyloid-like protein formed a stable shell layer on the surface of the Ag-MOF; the element distribution of the Ag-MOF and the Ag-MOF@ALP was uniform, and the amyloid-like protein was uniformly distributed on the surface of the Ag-MOF; compared with the diffraction peaks on the standard XRD diffraction card of Ag-MOF, both the Ag-MOF and the Ag-MOF@ALP showed characteristic diffraction peaks at 5.9°, 10.2° and 13.8°, and the modification of the amyloid-like protein did not change the crystal form of the Ag-MOF; the absorption peaks of the Ag-MOF and the Ag-MOF@ALP at 1570 cm -1 and 1370 cm -1 The absorption peaks of the Ag-MOF and the Ag-MOF@ALP at 1570 cm -1 The absorption peaks of the Ag-MOF and the Ag-MOF@ALP at 1570 cm -1 The absorption peaks of the Ag-MOF and the Ag-MOF@ALP at 1570 cm

[0122] Performance test:

[0123] The same performance test method as in Example 1 is adopted, the slow release effect of Ag-MOF@ALP of this embodiment 4 is significantly improved compared with Ag-MOF; compared with Ag-MOF, Ag-MOF@ALP can still keep the morphology complete and stable in harsh environment, and has more excellent stability; both Ag-MOF and Ag-MOF@ALP can play the antibacterial effect of Bacillus vietnamensis, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of Ag-MOF@ALP is better than that of Ag-MOF, when the concentration is 150mg / L, the survival rate of bacteria of Ag-MOF@ALP decreases to 6.58%, while the survival rate of bacteria of Ag-MOF is 10.98%; both Ag-MOF and Ag-MOF@ALP can also play the antibacterial effect of Pseudomonas aeruginosa, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of Ag-MOF@ALP is better than that of Ag-MOF, when the concentration is 150mg / L, the survival rate of bacteria of Ag-MOF@ALP decreases to 6.63%, while the survival rate of bacteria of Ag-MOF is 11.35%.

[0124] Example 5

[0125] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent, amyloid-like protein is self-assembled on the surface of UiO-66 to form a dense protective shell layer.

[0126] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent preparation method, specifically includes the following steps:

[0127] Preparation of MOF:

[0128] Zr 4+ and terephthalic acid are added to N,N-dimethylformamide, stirred to form a uniform solution, wherein the molar ratio of Zr 4+ and terephthalic acid is 1:4, then the Zr 4+ solution is added to the terephthalic acid solution and magnetically stirred, stirred uniformly, reacted at 120℃ for 36h, after the reaction is completed, centrifuged at 12000rpm for 10min, the precipitate is collected and washed with N,N-dimethylformamide three times, dried at 60℃ to obtain UiO-66 particles.

[0129] Preparation of amyloid-like protein:

[0130] 20mg / mL of α-lactalbumin is dissolved in 20mM of Hepes buffer, magnetically stirred to form a uniform solution, 50mM of reducing substance L-cysteine is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0131] Surface modification of MOF:

[0132] 10 mg of UiO-66 particles were placed in 5 mL of amyloid protein solution and incubated in a simple one-step method. The amyloid protein was strongly bonded to the surface of UiO-66 particles through various chemical bonds. After reacting for 80 min, the mixture was centrifuged at 8000 rpm for 20 min, the precipitate was collected and washed three times with deionized water, and then dried at 60 °C to obtain UiO-66@ALP.

[0133] Characterization tests:

[0134] Using the same characterization and testing methods as in Example 1, Example 5 successfully synthesized UiO-66 with clear morphology and uniform particle size. UiO-66@ALP was completely encapsulated by nanoscale particles, exhibiting strong binding, and amyloid protein spontaneously assembled on the UiO-66 surface. The synthesized UiO-66 had an octahedral structure with clear boundaries, and a stable shell of amyloid protein was observed forming on the UiO-66 surface. The elemental distribution of UiO-66 and UiO-66@ALP was uniform, and the amyloid protein was evenly distributed on the UiO-66 surface. Comparison with the diffraction peaks on the standard XRD diffraction card of UiO-66 showed characteristic diffraction peaks at 7.3°, 8.4°, and 25.6°, indicating that the amyloid protein modification did not change the crystal form of UiO-66. UiO-66 and UiO-66@ALP showed characteristic diffraction peaks at 1580 cm⁻¹. -1 and 1390cm -1 The absorption peaks at 665 cm⁻¹ are attributed to the asymmetric and symmetric stretching vibrations of the coordination between the terephthalic acid ligand and Zr, respectively. -1 The peak at 1640 cm⁻¹ belongs to the stretching vibration of the Zr-O-Zr bridge bond. ALP and UiO-66@ALP are at 1640 cm⁻¹. -1 The absorption peak at that location is a characteristic protein peak of the β-sheet of amyloid protein.

[0135] Performance testing:

[0136] Adopting the same performance test method as example 1, the slow-release effect of UiO-66@ALP of this embodiment 5 is significantly improved compared with UiO-66; compared with UiO-66, UiO-66@ALP can still keep the morphology complete and stable under harsh environment, and has more excellent stability; both UiO-66 and UiO-66@ALP can play the antibacterial effect of Bacillus vietnamensis, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of UiO-66@ALP is better than that of UiO-66, when the concentration is 150 mg / L, the survival rate of bacteria of UiO-66@ALP decreases to 7.32%, while the survival rate of bacteria of UiO-66 is 11.55%; both UiO-66 and UiO-66@ALP can also play the antibacterial effect of Pseudomonas aeruginosa, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of UiO-66@ALP is better than that of UiO-66, when the concentration is 150 mg / L, the survival rate of bacteria of UiO-66@ALP decreases to 7.07%, while the survival rate of bacteria of UiO-66 is 11.39%.

[0137] Example 6

[0138] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent, amyloid-like protein is self-assembled on the surface of MOF-74 to form a dense protective shell layer.

[0139] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent preparation method, specifically includes the following steps:

[0140] Preparation of MOF:

[0141] Zn 2+ and 2,5-dihydroxyterephthalic acid are added to N,N-dimethylformamide, and stirred to form a uniform solution, wherein the molar ratio of Zn 2+ and 2,5-dihydroxyterephthalic acid is 1:8, then the Zn 2+ solution is added to the 2,5-dihydroxyterephthalic acid solution and magnetically stirred, stirred uniformly, reacted at 100℃ for 24h, after the reaction is completed, centrifuged at 8000rpm for 10min, collect the precipitate and wash with N,N-dimethylformamide three times, dry at 60℃ to obtain MOF-74 particles.

[0142] Preparation of amyloid-like protein:

[0143] 40mg / mL of β-lactoglobulin is dissolved in 50mM Tris buffer, magnetically stirred to form a uniform solution, 50mM reducing agent L-cysteine is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0144] Surface modification of MOF:

[0145] 10mg MOF-74 particles were placed in 1mL amyloid-like solution for simple one-step incubation, which was combined with MOF-74 particle surface through strong bonding of various chemical bonds, centrifuged at 9000rpm for 15min after 10min reaction, the precipitate was collected and washed with deionized water for three times, dried at 60℃ to obtain MOF-74@ALP.

[0146] Characterization test:

[0147] Using the same characterization test method as Example 1, this embodiment 6 successfully synthesized MOF-74 with clear morphology and uniform particle size, and MOF-74@ALP was completely wrapped by nano-sized small particles, combined firmly, and amyloid-like proteins were spontaneously assembled on the surface of MOF-74; the morphology of the synthesized MOF-74 was hexagonal columnar structure with clear boundary, and stable shell layer of amyloid-like proteins on the surface of MOF-74 could be observed; MOF-74 and MOF-74@ALP were uniformly distributed in elements, and amyloid-like proteins were uniformly distributed on the surface of MOF-74; compared with the diffraction peaks on the standard XRD diffraction card of MOF-74, both MOF-74 and MOF-74@ALP showed characteristic diffraction peaks at 6.5°, 11.5° and 12.8°, and the modification of amyloid-like proteins did not change the crystal form of MOF-74; the absorption peaks of MOF-74 and MOF-74@ALP at 1560cm -1 and 1390cm -1 The wide peak at 3450cm -1 belongs to the stretching vibration of ligand hydroxyl, and the absorption peaks of ALP and MOF-74@ALP at 1640cm -1 belong to the protein characteristic peak of amyloid-like protein β-fold.

[0148] Performance test:

[0149] The MOF-74@ALP of the present embodiment 6 has a significantly improved slow-release effect compared with MOF-74 by using the same performance test method as that of embodiment 1; compared with MOF-74, the MOF-74@ALP can still maintain a complete and stable morphology in a harsh environment, and has more excellent stability; both MOF-74 and MOF-74@ALP can have an antibacterial effect on Bacillus vietnamensis, and as the concentration increases, the survival rate of the bacteria shows a downward trend, but the antibacterial effect of MOF-74@ALP is better than that of MOF-74, when the concentration is 150 mg / L, the survival rate of the bacteria of MOF-74@ALP decreases to 6.28%, while the survival rate of the bacteria of MOF-74 is 10.87%; both MOF-74 and MOF-74@ALP can also have an antibacterial effect on Pseudomonas aeruginosa, and as the concentration increases, the survival rate of the bacteria shows a downward trend, but the antibacterial effect of MOF-74@ALP is better than that of MOF-74, when the concentration is 150 mg / L, the survival rate of the bacteria of MOF-74@ALP decreases to 6.47%, while the survival rate of the bacteria of MOF-74 is 11.01%.

[0150] Embodiment 7

[0151] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent, amyloid-like protein is self-assembled on the surface of PCN-222 to form a dense protective shell layer.

[0152] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent preparation method, specifically includes the following steps:

[0153] Preparation of MOF:

[0154] Zr 4+ and porphyrin tetracarboxylic acid are added to N,N-dimethylformamide, stirred to form a uniform solution, wherein the molar ratio of Zr 4+ and porphyrin tetracarboxylic acid is 1:10, then the Zr 4+ solution is added to the porphyrin tetracarboxylic acid solution and magnetically stirred, stirred uniformly, reacted at 120℃ for 24h, after the reaction is completed, centrifuged at 8000rpm for 10min, collect the precipitate and wash with N,N-dimethylformamide three times, dry at 60℃ to obtain PCN-22 particles.

[0155] Preparation of amyloid-like protein:

[0156] 25mg / mL of insulin is dissolved in 20mM of Hepes buffer, magnetically stirred to form a uniform solution, 50mM of reducing agent L-cysteine is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0157] Surface modification of MOF:

[0158] 10 mg of PCN-222 particles were placed in 4 mL of amyloid-like protein solution for simple one-step incubation, which was combined with the PCN-222 particle surface through strong bonding of various chemical bonds. After 80 min of reaction, centrifugation was performed at 9000 rpm for 15 min, the precipitate was collected and washed with deionized water three times, and dried at 60°C to obtain PCN-222@ALP.

[0159] Characterization test:

[0160] Using the same characterization test method as in Example 1, Example 7 successfully synthesized PCN-222 with clear morphology and uniform particle size, and PCN-222@ALP was completely wrapped by nano-sized small particles, with firm bonding, and amyloid-like proteins spontaneously assembled on the surface of PCN-222; the synthesized PCN-222 has a rod-like structure with clear boundaries, and a stable shell layer of amyloid-like proteins on the surface of PCN-222 can be observed; PCN-222 and PCN-222@ALP have uniform element distribution, and amyloid-like proteins are uniformly distributed on the surface of PCN-222; compared with the diffraction peaks on the standard XRD diffraction card of PCN-222, both PCN-222 and PCN-222@ALP show characteristic diffraction peaks at 4.2°, 6.9° and 9.1°, and the modification of amyloid-like proteins does not change the crystal form of PCN-222; the absorption peaks of PCN-222 and PCN-222@ALP at 1600 cm -1 The absorption peak at 1400 cm -1 The peak at 1400 cm -1 The absorption peak at 1640 cm

[0161] Performance test:

[0162] The PCN-222@ALP of the present embodiment 7 has significantly improved slow-release effect compared with PCN-222 by using the same performance test method as that of embodiment 1; compared with PCN-222, the PCN-222@ALP can still maintain complete and stable morphology in harsh environment, and has more excellent stability; both PCN-222 and PCN-222@ALP can have antibacterial effect on Bacillus vietnamensis, and the survival rate of bacteria shows a downward trend with the increase of concentration, but the antibacterial effect of PCN-222@ALP is better than that of PCN-222, when the concentration is 150 mg / L, the survival rate of bacteria of PCN-222@ALP decreases to 7.38%, while the survival rate of bacteria of PCN-222 is 12.04%; both PCN-222 and PCN-222@ALP can also have antibacterial effect on Pseudomonas aeruginosa, and the survival rate of bacteria shows a downward trend with the increase of concentration, but the antibacterial effect of PCN-222@ALP is better than that of PCN-222, when the concentration is 150 mg / L, the survival rate of bacteria of PCN-222@ALP decreases to 7.45%, while the survival rate of bacteria of PCN-222 is 11.59%.

[0163] Embodiment 8

[0164] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent, amyloid-like protein is self-assembled on the surface of MIL-100 to form a dense protective shell layer.

[0165] A kind of amyloid-like protein-mediated long-acting metal organic framework antifouling agent preparation method, specifically includes the following steps:

[0166] Preparation of MOF:

[0167] Fe 3+ and 1,3,5-benzene tricarboxylic acid are added to deionized water respectively, and stirred to form a uniform solution, wherein the molar ratio of Fe 3+ and 1,3,5-benzene tricarboxylic acid is 1:6, then the Fe 3+ solution is added to the 1,3,5-benzene tricarboxylic acid solution and magnetically stirred, stirred uniformly, reacted at 60℃ for 24h, after the reaction is completed, centrifuged at 12000rpm for 10min, collect the precipitate and wash with deionized water for three times, dry at 120℃ to obtain MIL-100 particles.

[0168] Preparation of amyloid-like protein:

[0169] 5mg / mL of soybean protein is dissolved in 10mM of Hepes buffer, magnetically stirred to form a uniform solution, 50mM of reducing substance L-cysteine is added to completely open the disulfide bond of the protein, and the mixture is obtained.

[0170] Surface modification of MOF:

[0171] 10mg MIL-100 particles were incubated in 8mL amyloid-like protein solution in a simple one-step method. The amyloid-like protein was combined with the MIL-100 particles surface through strong bonding of various chemical bonds. After 80min of reaction, centrifugation was performed at 9000rpm for 10min. The precipitate was collected and washed with deionized water three times, and dried at 120°C to obtain MIL-100@ALP.

[0172] Characterization tests:

[0173] Using the same characterization test method as in Example 1, the MIL-100 with clear morphology and uniform particle size was successfully synthesized in this embodiment 8, and the MIL-100@ALP was completely wrapped by nano-sized small particles, and the combination was firm. The amyloid-like protein was spontaneously assembled on the surface of MIL-100; the morphology of the synthesized MIL-100 was an octahedral structure with clear boundaries, and it could be observed that the amyloid-like protein formed a stable shell layer on the surface of MIL-100; the element distribution of MIL-100 and MIL-100@ALP was uniform, and the amyloid-like protein was uniformly distributed on the surface of MIL-100; compared with the diffraction peaks on the standard XRD diffraction card of MIL-100, both MIL-100 and MIL-100@ALP showed characteristic diffraction peaks at 5.2°, 5.9° and 10.5°, and the modification of amyloid-like protein did not change the crystal form of MIL-100; the absorption peaks of MIL-100 and MIL-100@ALP at 1610cm -1 and 1370cm -1 The absorption peaks of ALP and MIL-100@ALP at 1640cm -1 The absorption peaks of ALP and MIL-100@ALP at 1640cm -1 The absorption peaks of ALP and MIL-100@ALP at 1640cm

[0174] Performance tests:

[0175] Using the same performance test method as in Example 1, the MIL-100@ALP of this embodiment 8 has significantly improved slow-release effect compared with MIL-100; under harsh environment, compared with MIL-100, MIL-100@ALP can still keep the morphology complete and stable, and has more excellent stability; both MIL-100 and MIL-100@ALP can play the antibacterial effect of Bacillus vietnamensis, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of MIL-100@ALP is better than that of MIL-100, when the concentration is 150 mg / L, the survival rate of bacteria of MIL-100@ALP decreases to 7.71%, while the survival rate of bacteria of MIL-100 is 12.12%; both MIL-100 and MIL-100@ALP can also play the antibacterial effect of Pseudomonas aeruginosa, and with the increase of concentration, the survival rate of bacteria shows a downward trend, but the antibacterial effect of MIL-100@ALP is better than that of MIL-100, when the concentration is 150 mg / L, the survival rate of bacteria of MIL-100@ALP decreases to 8.03%, while the survival rate of bacteria of MIL-100 is 11.84%.

Claims

1. A long-lasting metal-organic framework antifouling agent mediated by amyloid protein, characterized in that, Based on MOFs with antifouling properties, amyloid proteins self-assemble on the MOF surface to form a dense protective shell.

2. The amyloid-like protein-mediated long-lasting metal-organic framework antifouling agent as described in claim 1, characterized in that, MOFs with antifouling function are MOF-5, MOF-74, HKUST-1, Ag-MOF, ZIF-8, UiO-66, PCN-222 or MIL-100.

3. A method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein, characterized in that, Includes the following steps: Preparation of MOFs: Metal ions and organic ligands were added separately to a polar solvent and stirred to form a homogeneous solution. Then, the metal ion solution was added to the organic ligand solution and stirred until homogeneous. The metal ions and organic ligands were linked by coordinate bonds to form a MOF structure. After the reaction was completed, the MOF particles were obtained by centrifugation, collection, precipitation, washing and drying. Preparation of amyloid proteins: The protein was dissolved in a buffer solution and stirred to form a homogeneous solution. Then, an excess of water-soluble organic reducing agent was added. After the two were mixed, the natural protein completely opened its disulfide bonds under the action of the reducing agent, forming unfolded protein chains, exposing abundant chemical groups, and self-assembling into nanoscale oligomers with interfacial activity. Subsequently, the amyloid protein solution was obtained through self-assembly. Surface modification of MOF: MOF particles were incubated in an amyloid protein solution. The unfolded nanoscale protein oligomers were bound to the surface of the MOF particles through strong chemical bonds. After the reaction was completed, the particles were centrifuged, collected, precipitated, washed and dried to obtain an amyloid protein-mediated long-lasting metal-organic framework antifouling agent.

4. The method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein as described in claim 3, characterized in that, The metal ion used in the preparation of MOF is Zn. 2+ Cu 2+ Ag + Fe 3+ or Zr 4+ ; The organic ligands are 2-methylimidazolium, terephthalic acid, porphyrin tetracarboxylic acid, 2,5-dihydroxyterephthalic acid, or 1,3,5-benzenetricarboxylic acid; The solvent is H2O, ethanol, or N,N-dimethylformamide.

5. The method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein as described in claim 3, characterized in that, In the preparation of MOF, the molar ratio of metal ions to organic ligands is 1:(4-12), the reaction time is 4h-36h, the reaction temperature is 20℃-120℃, the centrifugation conditions are 8000rpm-12000rpm for 5min-20min, and the drying temperature is 60℃-120℃.

6. The method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein as described in claim 3, characterized in that, The proteins used in the preparation of amyloid protein are serum albumin, lysozyme, α-lactalbumin, insulin, β-lactoglobulin, oat protein, or soy protein. The buffer solution is either Hepes buffer or Tris buffer; The water-soluble organic reducing agent is tris(2-carboxyethyl) phosphate hydrochloride or L-cysteine.

7. The method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein as described in claim 3, characterized in that, In the preparation of amyloid proteins, the protein concentration is 0.1 mg / mL-40 mg / mL; The buffer concentration is 10mM-50mM.

8. The method for preparing a long-lasting metal-organic framework antifouling agent mediated by amyloid protein as described in claim 3, characterized in that, A simple one-step method was used for incubation in the surface modification of MOFs; The mass-to-volume ratio of MOF particles to amyloid protein (mg:mL) is 10:(1-10); The incubation reaction time for MOF surface modification is 10 min-120 min; Centrifugation conditions: 8000rpm-12000rpm for 5min-20min; The drying temperature is 60℃-120℃.

9. The application of the amyloid-like protein-mediated long-lasting metal-organic framework antifouling agent of claim 1 in the field of marine antifouling.

10. The application of the amyloid-like protein-mediated long-acting metal-organic framework antifouling agent as described in claim 9 in the field of marine antifouling, wherein when the amount of the amyloid-like protein-mediated long-acting metal-organic framework antifouling agent added is ≥150mg / L, the bacterial survival rate against Bacillus vivax and Pseudomonas aeruginosa is <9%.

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