Polypeptide for modifying nanometal-based energetic material and preparation method and application thereof

Abstract

This invention discloses a polypeptide for modifying nano-metallic energetic materials, its preparation method, and its application, belonging to the field of energetic materials technology. The purpose of this invention is to improve the thermal properties of nano-metallic energetic materials and to specifically target and modify them. This invention provides a polypeptide for monomodifying nano-metallic energetic materials, the amino acid sequence of which is shown in SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4, SEQ ID NO.5, or SEQ ID NO.6. It can be used in the preparation of nano-metallic energetic materials.

Description

Technical Field

[0001] This invention belongs to the field of energetic materials technology, specifically relating to a polypeptide modified with nano-metal energetic materials, its preparation method and application. Background Technology

[0002] Nano-aluminothermic agents, composed of nano-metal oxidants and nano-metal reductants, are a novel energetic material with broad application prospects. They not only maintain the high energy density of composite energetic materials but also significantly shorten the mass transfer distance between the oxidant and fuel and increase the mass transfer interface contact area by reducing the particle size of the reactants to the nanoscale, thereby greatly improving the energy release efficiency and combustion rate of energetic materials. However, because high-energy nanoparticles are prone to aggregation, it is difficult to significantly improve or precisely control their high-energy performance. The effective interaction between the components of nano-aluminothermic agents is key to achieving improved energy release efficiency and rate.

[0003] Achieving precise assembly of nano-oxidants and reductants is a pressing issue that needs to be addressed. Chemical experimental methods are used, but these require stringent experimental conditions and equipment. For example, layered vapor deposition utilizes high-vacuum conditions to deposit oxidants and reductants into layers; core-shell structure preparation methods involve multiple steps, including nano-core preparation and nano-shell coating, requiring the integration of solution chemistry, magnetron sputtering, and surface modification. Furthermore, these methods inevitably use large amounts of organic solvents.

[0004] Utilizing the targeted assembly characteristics of biomolecules to prepare nano-aluminothermic agents is a novel preparation method. Peptide functional molecules possess unique advantages such as ease of solid-phase synthesis, easy specific modification, and easy functionalization. Furthermore, compared to other biomolecules (DNA, proteins) used in the assembly of energetic nanomaterials via biological methods, peptide functional molecules also offer advantages such as small molecular weight (introducing fewer non-energetic components into the system), low cost, no need for pretreatment, and simple preparation process.

[0005] However, the prerequisite for assembling nano-oxidants and reductants using peptide functional molecules is the design of monofunctional peptide molecules that modify nano-oxidants and reductants. Currently, there are no monofunctional peptides available for assembling nano-metallic oxidants and reductants. Summary of the Invention

[0006] The purpose of this invention is to improve the thermal properties of nano-metallic energetic materials and to specifically target and modify them.

[0007] This invention provides a polypeptide of a single-modified nanometallic energetic material, wherein the amino acid sequence of the polypeptide is shown in SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4, SEQ ID NO.5 or SEQ ID NO.6.

[0008] Further specifying, SEQ ID NO.1-3 are polypeptides modified with nano-metal reducing agents; SEQ ID NO.4-6 are polypeptides modified with nano-metal oxidizing agents.

[0009] Further specifying, the energetic materials of the nano-metal type are nano-metal oxidants and nano-metal reducing agents, the nano-metal oxidants are nano-Al; the nano-metal reducing agents are nano-Fe2O3, nano-CuO, nano-Bi2O3 or nano-Co3O4; the nanoscale is 5-1000nm.

[0010] This invention provides a polypeptide for a dual-modified nanometallic energetic material, which uses linking peptides to connect any one of SEQ ID NO. 1-3 with any one of SEQ ID NO. 4-6.

[0011] This invention provides a gene encoding the aforementioned polypeptide.

[0012] The present invention provides a recombinant vector containing the above-mentioned genes.

[0013] The present invention provides a recombinant microbial cell containing the above-mentioned genes.

[0014] This invention provides the application of the above-mentioned single-modified nano-metallic energetic material polypeptide, the above-mentioned double-modified nano-metallic energetic material polypeptide, the above-mentioned recombinant carrier, or the above-mentioned recombinant microbial cell in modifying nano-metallic energetic materials or improving the thermal properties of nano-metallic energetic materials.

[0015] This invention provides a method for improving the thermal properties of nano-metallic energetic materials, which involves using a linker peptide to link any one of SEQ ID NO. 1-3 with any one of SEQ ID NO. 4-6, followed by N-terminal acetylation and C-terminal amidation.

[0016] This invention provides a modified nanomaterial containing energetic metals, the modified nanomaterial containing energetic metals being as follows: Ac-YPSSGPQDTTRTTGGGGQMDTSTSLAPSR-NH2 and Ac-YSPDTRPWSSRYGGGGDMCHTKSSYNPS-NH2.

[0017] Beneficial Effects: This patent proposes a peptide design method for modifying energetic metal-based materials. This method utilizes the high hydroxyl content and hydrophilicity of the surface of energetic metal-based materials, and designs peptide functional molecules that can specifically bind to nano-metal oxides and reducing agents based on the hydrophilic and hydrophobic functions of different amino acids constituting the peptide functional molecules. The peptide functional molecules designed and synthesized based on this method can simultaneously and specifically bind to nano-oxidants and nano-reducants, and can be used in the preparation of nano-aluminothermic agents. Furthermore, it helps in screening for more superior, more affinity-rich, and more specific targeted peptide molecules. Attached Figure Description

[0018] Figure 1 Al / CuO DSC curves for the assembly of peptides 5, 6, and 7.

[0019] Figure 2 DSC curves of Al / Fe2O3 and physical mixtures for polypeptide 12 assembly.

[0020] Figure 3 DSC curves of Al / Fe2O3 and physical mixtures for polypeptide 13 assembly. Detailed Implementation

[0021] Example 1. Peptides that can modify nano-metal reducing agents and peptides that can modify nano-metal oxidizing agents. 1. Peptide sequences that can modify nano-metal reducing agents: SY-15 (STEARATTLTACDAY, SEQ ID NO.1), YT-12 (YPSSGPQDTRTT, SEQ ID NO.2), and YY-12 (YSPDTRPWSSRY, SEQ ID NO.3). A polypeptide sequence HH-6 (HHHHHH, SEQ ID NO.4), RQ-12 (QMDTSTSLAPSR, SEQ ID NO.5), and DS-12 (DMCHTKSSYNPS) that can modify nano-metal oxidants is provided.

[0022] 2. Preparation method of dual-modified materials: 1) Design short peptide chains that specifically target metallic fuels (nano Al) and verify their specific targeting effect through ultraviolet adsorption. The peptide chains should contain several amino acids that interact with the fuel through hydrogen bonding, such as hydroxyl, thiol, and carbonyl groups, with a total number of 6-15 amino acids. 2) Design an intermediate linker sequence. The intermediate linker sequence is glycine (G), with 2-10 amino acids. 3) Design specific targeting peptides for metal oxidants (one or more of the oxidants such as Fe2O3, CuO, Bi2O3, Co3O4, etc.), and verify the specific targeting effect by ultraviolet adsorption. The peptides should contain several amino acids that interact with the fuel by hydrogen bonding, such as hydroxyl, thiol, and carbonyl groups, or one or more amino acids that coordinate with the metal oxidant, such as histidine (H). The number of amino acids should be 6-15. 4) Construct and assemble metal-based energetic material peptide chains, verify specific targeting effects through ultraviolet adsorption, and link the peptides screened in step 1 with the glycine short peptides screened in step 2 and step 3, with the number of amino acids controlled between 15 and 30. For the design of new sequences, in order to be closer to the parent protein, the peptide ends need to be blocked, the N-terminus acetylated, and the C-terminus amidated.

[0023] 3. Preparation method of reducing agent-modified materials: Design short peptide chains specifically targeting metallic fuels (nano-Al) and verify their specific targeting effect through ultraviolet adsorption. The peptide chains need to contain several amino acids that interact with the fuel through hydrogen bonding, such as hydroxyl, thiol, and carbonyl groups, with 6-15 amino acids in total. The peptide ends need to be blocked by N-terminal acetylation and C-terminal amidation.

[0024] 4. Preparation method of oxidant-modified materials: Design specific targeting peptides for metal oxidants (one or more of the oxidants such as Fe2O3, CuO, Bi2O3, Co3O4, etc.), and verify the specific targeting effect by ultraviolet adsorption. The peptides should contain several amino acids that interact with the fuel by hydrogen bonding, such as hydroxyl, thiol, and carbonyl groups, or one or more amino acids that coordinate with the metal oxidant, such as histidine (H). The number of amino acids should be 6-15. In step 1, the peptide ends need to be blocked, the N-terminus acetylated, and the C-terminus amidated.

[0025] Example 2. 1. The short peptide Ac-STEARATTLTACDAY-NH2 (peptide 1):SY-15 (STEARATTLTACDAY) was designed and obtained by N-terminal acetylation and C-terminal amidation.

[0026] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg Al powder and add 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide (peptide 1). Sonicate for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 18.5 μM, indicating that the peptide interacts with Al.

[0027] Example 3. 1. Design of short peptide Ac-STEARAGGLGAGVAG-NH2 (peptide 2): Ac-STEARAGGLGAGVAG is obtained by N-terminal acetylation and C-terminal amidation of STEARAGGLGAGVAG.

[0028] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg Al powder and add 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide (peptide 2). Sonicate for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times, and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 27.0 μM. Under the same conditions, the peptide in Example 2 adsorbed more. By comparing the peptide structure, it can be found that the peptide contains more amino acids such as hydroxyl and thiol groups that are easy to form hydrogen bonds with Al, and the binding effect with Al is stronger.

[0029] Example 4. 1. The short peptide Ac-HHHHHH-NH2 (peptide 3) and HH-6 (HHHHHH) that interact with CuO were designed and then N-terminally acetylated and C-terminally amidated.

[0030] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg CuO powder and add 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide (peptide 3). Sonicate for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 20.4 μM, indicating that the peptide interacts with CuO.

[0031] Example 5. 1. The short peptide Ac-HHGGGG-NH2 (peptide 4) that interacts with CuO was designed and obtained by N-terminal acetylation and C-terminal amidation of HHGGGG.

[0032] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg CuO powder and add 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide (peptide 4). Sonicate for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times, and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 26.5 μM. Under the same conditions, the peptide in Example 4 adsorbed more. By comparing the peptide structure, it can be seen that the peptide contains more amino acids that can coordinate with CuO, and the binding effect is better.

[0033] Example 6. 1. A short peptide Ac-STEARATTLTACDAYGGGGHHHHHH-NH2 (peptide 5) was designed to interact with Al / CuO. SY-15 (STEARATTLTACDAY) and HH-6 (HHHHHH) were linked using GGGG, followed by N-terminal acetylation and C-terminal amidation.

[0034] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg CuO powder and 5 mg Al powder, add 0.01 M pH 7.0 phosphate buffer solution to prepare 5 mL of 30 μM peptide (peptide 5), sonicate for 5 min with a probe (100 W, sonication for 2 s, pause for 1 s), incubate for 2 h, centrifuge at 10000 rpm for 10 min after incubation, take the supernatant, dilute it 3 times and measure the absorbance. Compare it with the peptide standard prepared in the same buffer solution to draw a UV absorption standard curve to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 15.1 μM, indicating that the peptide interacts with Al / CuO.

[0035] Example 7. 1. A short peptide Ac-STEARAGGLGAGVAGGGGGHHHHHH-NH2 (peptide 6) interacting with Al / CuO was designed. STEARAGGLGAGVA was linked to HH-6 (HHHHHH) using GGGG, followed by N-terminal acetylation and C-terminal amidation to obtain the peptide.

[0036] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg CuO powder and 5 mg Al powder, add 0.01 M pH 7.0 phosphate buffer solution to prepare 5 mL of 30 μM peptide (peptide 6), sonicate for 5 min with a probe (100 W, sonication for 2 s, pause for 1 s), incubate for 2 h, centrifuge at 10000 rpm for 10 min after incubation, take the supernatant, dilute it 3 times and measure the absorbance. Compare it with the peptide standard prepared in the same buffer solution to draw a UV absorption standard curve to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 20.3 μM, indicating that the peptide has a weak interaction with Al / CuO.

[0037] Example 8. 1. A short peptide Ac-STEARAGGLGAGVAGGGGGHHGGGGG-NH2 (peptide 7) was designed to interact with Al / CuO. STEARAGGLGAGVA and HHGGGG were linked by GGGG, followed by N-terminal acetylation and C-terminal amidation.

[0038] 2. UV adsorption verification of specific targeting effect: Weigh 5 mg CuO powder and 5 mg Al powder, add 0.01M pH7.0 phosphate buffer solution to prepare 5 mL of 30 μM peptide (peptide 7), sonicate for 5 min with a probe (100W, sonication for 2 s, pause for 1 s), incubate for 2 h, centrifuge at 10000 rpm for 10 min after incubation, take the supernatant, dilute it 3 times and measure the absorbance. Compare it with the peptide standard prepared in the same buffer solution to draw a UV absorption standard curve to determine the adsorption amount. The peptide concentration in the supernatant decreased from the original 30 μM to 26.2 μM, indicating that the peptide has a weak interaction with Al / CuO. Combined with Examples 6 and 7, it can be concluded that the peptide contains amino acids that form hydrogen bonds with energetic metal materials, which is more conducive to specific targeting effect.

[0039] Example 9. Performance verification of peptide assembly using Al and CuO: Appropriate amounts of Al and CuO were weighed into 10 mL centrifuge tubes (5.00 mmol / L Al and 7.50 mmol / L CuO). Peptide solutions (30 μmol / L, peptide 5) were prepared by adding 0.01 M PBS. The solutions were sonicated for 5 min in the same sonication environment (100 W, 2 s sonication, 1 s pause). After sonication, assembly was performed for 30 min. The samples were then centrifuged at 10000 rpm for 10 min, the supernatant was removed, and the samples were incubated in a water-jacketed incubator for 30 minutes. o Drying at C. After drying, thermal properties were tested using DSC. The results for peptides 5, 6, and 7 showed thermal properties of 1072 J / g, 697 J / g, and 632 J / g, respectively, indicating strong interactions between the peptides and Al and CuO, which are more conducive to assembly. Figure 1 As shown.

[0040] Physical mixing: Weigh the corresponding amounts of Al and CuO into 10 mL centrifuge tubes (5.00 mmol / L Al and 7.50 mmol / L CuO), and sonicate for 5 min in the same ultrasonic environment (100 W, sonication for 2 s, pause for 1 s). After sonication, assemble for 30 min, centrifuge at 10000 rpm for 10 min, remove the supernatant, and incubate the sample in a water-jacketed incubator for 30 minutes. o Drying at C. After drying, perform DSC thermal property testing. The physical mixture thermal property is 576 J / g.

[0041] Example 10. Design of the short peptide Ac-YPSSGPQDTRTT-NH2 (peptide 8, SEQ ID NO.2): obtained by N-terminal acetylation and C-terminal amidation of YPSSGPQDTRTT to interact with Al.

[0042] UV adsorption verification of specific targeting effect: Weigh 5 mg Al powder and add 0.01 M pH 7.0 phosphate buffer solution to prepare 5 mL of 30 μM peptide. Sonicate for 5 min with probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. After dilution, the peptide concentration in the supernatant was calculated to decrease from the original 30 μM to 20.1 μM, indicating that the peptide interacts with Al.

[0043] Example 11. The short peptide Ac-YSPDTRPWSSRY-NH2 (peptide 9, SEQ ID NO.3) that interacts with Al was obtained by N-terminal acetylation and C-terminal amidation of YSPDTRPWSSRY.

[0044] UV adsorption verification of specific targeting effect: Weigh 5 mg Al powder and add 0.01 M pH 7.0 phosphate buffer to prepare 5 mL of 30 μM peptide. Sonicate for 5 min with probe (100 W, 2 s sonication, 1 s pause) and incubate for 2 h. After incubation, centrifuge at 10000 rpm for 10 min. Take the supernatant, dilute it 3 times and measure the absorbance. Plot a UV absorption standard curve with the peptide standard prepared in the same buffer to determine the adsorption amount. After dilution, the peptide concentration in the supernatant was calculated to decrease from the original 30 μM to 18.2 μM, indicating that the peptide interacts with Al.

[0045] Example 12. Design of a short peptide Ac-QMDTSTSLAPSR-NH2 (peptide 10, SEQ ID NO.5) that interacts with Fe2O3: obtained by N-terminal acetylation and C-terminal amidation of QMDTSTSLAPSR.

[0046] Specific targeting effect verified by UV adsorption: 5 mg of Fe2O3 powder was weighed and added to 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide. The peptide was sonicated for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubated for 2 h. After incubation, the peptide was centrifuged at 10000 rpm for 10 min. The supernatant was diluted 3 times and the absorbance was measured. The absorbance was compared with that of a peptide standard prepared in the same buffer to plot a UV absorption standard curve to determine the adsorption amount. After dilution, the peptide concentration in the supernatant was calculated to decrease from the original 30 μM to 15.7 μM, indicating that the peptide interacts with Fe2O3.

[0047] Example 13. The short peptide Ac-DMCHTKSSYNPS-NH2 (peptide 11, SEQ ID NO.6) that interacts with Fe2O3 was designed and obtained by N-terminal acetylation and C-terminal amidation of DMCHTKSSYNPS.

[0048] Specific targeting effect verified by UV adsorption: 5 mg of Fe2O3 powder was weighed and added to 5 mL of 0.01 M pH 7.0 phosphate buffer to prepare 30 μM peptide. The peptide was sonicated for 5 min with a probe (100 W, 2 s sonication, 1 s pause) and incubated for 2 h. After incubation, the peptide was centrifuged at 10000 rpm for 10 min. The supernatant was diluted 3 times and the absorbance was measured. The absorbance was compared with that of a peptide standard prepared in the same buffer to plot a UV absorption standard curve to determine the adsorption amount. After dilution, the peptide concentration in the supernatant was calculated to decrease from the original 30 μM to 14.7 μM, indicating that the peptide interacts with Fe2O3.

[0049] Example 14. Based on the interaction between peptides and nano-metals and nano-metal oxides, a short peptide Ac-YPSSGPQDTRTTGGGGQMDTSTSLAPSR-NH2 peptide 12 was designed to interact with Al / Fe2O3. YPSSGPQDTRTT was linked to QMDTSTSLAPSR using GGGG, followed by N-terminal acetylation and C-terminal amidation to obtain the peptide.

[0050] Design and assemble Al and Fe2O3 peptides for performance verification: Weigh the corresponding amounts of Al and Fe2O3 into 10 mL centrifuge tubes (Fe2O3 3.735 mmol / L, Al 7.470 mmol / L), add 0.01 M PBS to prepare peptide solutions (30 μmol / L), and sonicate for 5 min in the same sonication environment (100 W, sonication 2 s, pause 1 s). After sonication, assemble for 30 min, centrifuge at 10000 rpm for 10 min, remove the supernatant, and incubate the samples in a water-jacketed incubator for 30 minutes. o Dry at C. After drying, perform DSC thermal performance testing.

[0051] Physical mixing method: Weigh the corresponding amounts of Al and Fe2O3 into 10 mL centrifuge tubes (Fe2O3 3.735 mmol / L, Al 7.470 mmol / L), and sonicate for 5 min in the same ultrasonic environment (100 W, 2 s sonication, 1 s pause). After sonication, assemble for 30 min, centrifuge at 10000 rpm for 10 min, remove the supernatant, and incubate the sample in a water-jacketed incubator for 30 minutes. o C. Drying. After drying, perform DSC thermal performance testing, and the results are as follows. Figure 2 As shown in the figure. The results indicate that the assembly thermal performance is 1437 J / g and the physical mixing thermal performance is 1202 J / g, demonstrating that the designed peptide can achieve Al / Fe2O3 assembly.

[0052] Example 15. Based on the interactions between peptides and nanometals and nanometal oxides, a short peptide Ac-YSPDTRPWSSRYGGGGDMCHTKSSYNPS-NH2 peptide 13 was designed to interact with Al / Fe2O3. YSPDTRPWSSRY was linked to DMCHTKSSYNPS using GGGG, followed by N-terminal acetylation and C-terminal amidation. Al and Fe2O3 peptides were designed and assembled for performance verification: Appropriate amounts of Al or Fe2O3 were weighed into 10 mL centrifuge tubes (Fe2O3 3.246 mM, Al 10.585 mM), and 0.01 M PBS was added to prepare peptide solutions (30 μmol / L). The solutions were sonicated for 5 min in the same sonication environment (100 W, 2 s sonication, 1 s pause). After sonication, assembly was performed for 30 min, followed by centrifugation at 10000 rpm for 10 min. The supernatant was removed, and the samples were incubated in a water-jacketed incubator for 30 minutes. o C. Drying. After drying, perform DSC thermal performance testing, and the results are as follows. Figure 3 As shown.

[0053] The physical mixing and testing methods were the same as described above, but without the addition of peptides. The results showed that the assembly thermal performance was 2613 J / g, while the thermal performance of the physical mixing method was 1961 J / g, indicating that the designed peptides can achieve Al / Fe₂O₃ assembly and increase the heat of reaction.

Claims

1. A polypeptide of a single-modified nano-metallic energetic material, characterized in that, The amino acid sequence of the polypeptide is shown in SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4, SEQ ID NO.5 or SEQ ID NO.

6.

2. The polypeptide according to claim 1, characterized in that, SEQ ID NO.1-3 are polypeptides modified with nano-metal reducing agents; SEQ ID NO.4-6 are polypeptides modified with nano-metal oxidizing agents.

3. The polypeptide according to claim 1, characterized in that, The energetic materials of nano-metals are nano-metal oxidants and nano-metal reducing agents. The nano-metal oxidant is nano-Al; the nano-metal reducing agent is nano-Fe2O3, nano-CuO, nano-Bi2O3 or nano-Co3O4; the nanoscale is 5-1000nm.

4. A polypeptide of a dual-modified nano-metallic energetic material, characterized in that, Connect any one of SEQ ID NO.1-3 to any one of SEQ ID NO.4-6 using a linker peptide.

5. A gene encoding the polypeptide of claim 1 or 4.

6. A recombinant vector containing the gene of claim 5.

7. A recombinant microbial cell containing the gene of claim 5.

8. The application of the polypeptide of the single-modified nano-metal energetic material according to any one of claims 1-3, the polypeptide of the double-modified nano-metal energetic material according to claim 4, the recombinant carrier according to claim 6, or the recombinant microbial cell according to claim 7 in modifying nano-metal energetic materials or improving the thermal properties of nano-metal energetic materials.

9. A method for improving the thermal properties of nano-metallic energetic materials, characterized in that, The peptides of any one of SEQ ID NO.1-3 and any one of SEQ ID NO.4-6 are linked together, followed by N-terminal acetylation and C-terminal amidation.

10. A modified nanomaterial containing metallic energy, characterized in that, The modified nano-metallic materials are as follows: Ac-YPSSGPQDTRTTGGGGQMDTSTSLAPSR-NH2 and Ac-YSPDTRPWSSRYGGGGDMCHTKSSYNPS-NH2.

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