Insect neuropeptide analog and use thereof in pest control

Abstract

Provided are an insect neuropeptide analog and the use thereof in pest control. The insect neuropeptide analog is highly effective, broad-spectrum, and environmentally friendly. The provided insect neuropeptide analog has multiple biological activities, and exhibits significant insecticidal effects against lepidoptera pests such as Ostrinia furnacalis and Plutella xylostella, and Hemiptera pests such as Myzus persicae, Acyrthosiphon pisum and Aphis glycines, and can be used as a new, environmentally-friendly and safe pest control agent.

Description

Insect neuropeptide analogs and their application in pest control Technical Field

[0001] This invention belongs to the agricultural field, specifically relating to a class of insect neuropeptide analogs and their application in pest control, and more specifically to the application of such compounds in controlling Lepidoptera Asian corn borer, diamondback moth, and Hemiptera peach aphid, pea aphid, and soybean aphid. Background Technology

[0002] Various lepidopteran insects cause significant losses to crops worldwide. The Asian corn borer (Ostrinia furnacalis) is a major agricultural pest, severely damaging cash crops such as corn and sorghum. The diamondback moth (Plutella xylostella) is one of the world's most destructive pests. Targeting plants like broccoli and cabbage, they have virtually no natural enemies, reproduce efficiently, and are a devastating pest of cruciferous crops due to their high reproductive rate and widespread resistance to pesticides. Aphids are a major economic pest globally. As piercing-sucking insects, aphids not only directly damage plants by sucking sap but also secrete honeydew, fostering mold growth and inducing plant diseases. They are also primary insect vectors for plant viruses, posing serious threats to agriculture and the environment. For example, the peach aphid (Myzus persicae) feeds on hundreds of species from over forty plant families, causing widespread damage to horticultural and food crops; it is a globally distributed, highly destructive, polyphagous pest. The pea aphid (Acyrthosiphon pisum) is a significant global pest that feeds almost entirely on legumes. The soybean aphid (Aphis glycines) is a herbivorous pest in many soybean-growing areas, causing severe yield reductions.

[0003] Currently, pesticides remain the primary means of pest control. However, the long-term and extensive use of chemical pesticides has led to severe resistance problems in pests and toxicity issues to non-target organisms. For example, some neonicotinoid pesticides, such as imidacloprid and thiamethoxam, have been banned due to bee venom issues. Furthermore, with increasing environmental pollution and residue problems, how to better control pests has attracted the attention of many scientists. Therefore, developing new, highly effective, and safe insecticides based on eco-friendliness is of great significance for protecting the ecosystem and mitigating pesticide resistance.

[0004] Insect neuropeptides are a group of neuroregulatory factors that play a crucial role in insect growth, development, molting, metamorphosis, mating, and reproduction. Due to these important physiological functions, insect neuropeptides are considered a potential class of pest control agents. However, the inherent drawbacks of natural insect neuropeptides, such as easy degradation, poor transport function, and high molecular flexibility, limit their application in pest control. To overcome these shortcomings, the structure of natural neuropeptides has been modified. The characteristics of neuropeptide structural modification are mainly twofold: 1) Most use natural amino acids such as alanine, or non-natural amino acids such as 4-amino-5-imidazolium carboxamide and aromatic acids, to replace the amino acids in the natural neuropeptide, resulting in structurally very similar analogs. 2) Most compounds retain the original in vitro biological activity of the neuropeptides. However, the following shortcomings remain: some compounds have complex structures (simulating active peptides with more than five peptides), resulting in high synthesis costs; the in vivo stability of the analogs is not ideal, their in vivo biological activity is not very prominent, and their spectrum of action is relatively narrow, mainly concentrated in the Pacific cockroach and soybean aphid. Therefore, their direct application as pesticide molecules in agricultural production still has certain limitations. To address these shortcomings, this invention discloses a new class of insect neuropeptide analogs with simple structure, good stability, and broad spectrum of action, as well as their applications in pest control.

[0005] Invention Overview

[0006] One of the objectives of this invention is to provide a class of insect neuropeptide analogs.

[0007] The insect neuropeptide analogs provided by this invention have the structural formulas shown in Formula A and Formula B:

[0008] In formula A:

[0009] R1 is selected from cinnamic acid, 4-nitrocinnamic acid, or R1 is not present.

[0010] R2, R3, R4, and R5 are all amino acids;

[0011] Specifically, R2 can be selected from any one of glycine, L-aspartic acid, D-aspartic acid, D-tert-leucine, L-tert-leucine, D-homogeneous alanine, L-homogeneous alanine, D-2-aminobutyric acid, L-2-aminobutyric acid, D-4-trifluoromethylphenylalanine, L-4-trifluoromethylphenylalanine, D-valine, L-valine, D-cyclohexylalanine, L-cyclohexylalanine, and L-phenylalanine.

[0012] R3 can be selected from any one of L-phenylalanine, D-phenylalanine, and β-alanine;

[0013] R4 can be selected from any one of glycine, D-tryptophan, and L-tryptophan;

[0014] R5 can be selected from any one of L-leucine, D-leucine, and glycine;

[0015] The carboxyl group in R1 forms an amide bond with the amino group of the amino acid shown in R2;

[0016] The carboxyl group of the amino acid shown in R2 forms an amide bond with the amino group of the amino acid shown in R3.

[0017] The carboxyl group of the amino acid shown in R3 forms an amide bond with the amino group of the amino acid shown in R4.

[0018] The carboxyl group of the amino acid shown in R4 forms an amide bond with the amino group of the amino acid shown in R5.

[0019] The rightmost amino group in Formula A is provided by the solid-phase resin used in the solid-phase synthesis of the polypeptide; the carboxyl group of the amino acid shown in R5 forms -CONH2 with the amino group.

[0020] In formula B:

[0021] R6 is selected from any one of L-phenylalanine, nicotinic acid, piperic acid, sinapic acid, naphthaleneacetic acid, vanillic acid, syringic acid, gallic acid, protocatechuic acid, coumaric acid, furoic acid, cinnamic acid, salicylic acid, and β-alanine, or R6 is absent.

[0022] R7 and R8 are both amino acids;

[0023] R7 is selected from either glycine or L-tryptophan;

[0024] R8 is selected from any one of L-leucine, L-histidine, and glycine.

[0025] The carboxyl group in R6 forms an amide bond with the amino group of the amino acid shown in R7;

[0026] The carboxyl group of the amino acid shown in R7 forms an amide bond with the amino group of the amino acid shown in R8.

[0027] The rightmost amino group in Formula B is provided by the solid-phase resin used in the solid-phase synthesis of the polypeptide, and the carboxyl group of the amino acid shown in R8 forms -CONH2 with this amino group.

[0028] The compounds shown in Formula A and Formula B provided in this invention were all prepared according to the peptide solid-phase synthesis method (Reference: W Chan, Peter White. Fmoc solid phase peptide synthesis: A Practical Approach, Oxford University Press, 2000; pp. 9-74.).

[0029] The second objective of this invention is to provide the application of the compounds shown in Formula A or Formula B in pest control.

[0030] The third objective of this invention is to provide a pest control agent.

[0031] The pest control agent contains an insect neuropeptide analogue as shown in Formula A or Formula B above.

[0032] The pests mentioned are Lepidoptera and Hemiptera pests.

[0033] The Lepidoptera pests may specifically be at least one of the Asian corn borer and the diamondback moth, and the Hemiptera pests may specifically be at least one of the peach aphid, the pea aphid, and the soybean aphid.

[0034] The insecticidal activity of the compounds of this invention against the Asian corn borer was determined by feeding method (Reference: Jin X.-Y. et al. J. Agr. Food Chem. 2023, 71, 8345-8355). The insecticidal activity against the diamondback moth and aphids was determined by leaf dipping method (Reference: Jin X.-Y. et al., J. Agr. Food Chem. 2023, 71, 8345-8355; Zhou, Y.-L. et al. Pest Manag. Sci. 2022, 78, 2952-2963). Bioassay results showed that the compounds of this invention have very significant insecticidal activity against the Asian corn borer and diamondback moth, and also exhibit good activity against the peach aphid, pea aphid, and soybean aphid. Some compounds show superior activity compared to commercially available pesticides phenoxycarb and pymetrozine, demonstrating their potential for further development and application as green pest control agents.

[0035] The beneficial effects of this invention are as follows: This invention adopts a strategy of mimicking peptides to invent a class of insect neuropeptide analogs, that is, by introducing hydrogen, acid, natural amino acids or non-natural amino acids at different sites for substitution modification, a series of small peptide analogs with novel structures and more stable performance are obtained. The insecticidal activity of many new compounds is very significant, which is superior to commercial pesticides phenoxycarb and pymetrozine, and is expected to be applied to the green control of agricultural pests. Embodiments of the present invention

[0036] The present invention will now be described in further detail with reference to specific embodiments. The given embodiments are merely illustrative of the invention and not intended to limit its scope. The embodiments provided below can serve as a guide for further improvements by those skilled in the art and do not constitute a limitation on the invention in any way.

[0037] Unless otherwise specified, the experimental methods used in the following examples are conventional methods, performed according to the techniques or conditions described in the literature in this field or according to the product instructions. Unless otherwise specified, the materials and reagents used in the following examples are commercially available.

[0038] Using compound A-1 as a representative compound (but not limited to this compound), describe the preparation process of compounds A-1 to A-30.

[0039] Example 1: Preparation of the compound shown in A-1 (R1 from 4-nitrocinnamic acid, R2 from glycine, R3 from D-phenylalanine, R4 from glycine, R5 from L-leucine)

[0040] Rink Amide-Am resin (0.3 mmol) was activated in 5 mL of DCM for 2 h, then washed 5 times with DMF, and then reacted with 5 mL of 20% piperidine DMF solution for 20 min to remove the Fmoc protecting groups on the resin. A 5 mL DMF solution containing Fmoc-L-leucine-OH (1.2 mmol), HBTU (1.2 mmol), HOBt (1.2 mmol), and DIEA (1.2 mmol) was prepared, activated for 5 min, and then reacted with the resin at room temperature for 2 h to obtain Fmoc-L-leucine with Rink Amide-Am resin. Further removal of Fmoc groups was performed by sequentially inoculating Fmoc-glycine-OH, Fmoc-D-phenylalanine-OH, Fmoc-glycine-OH, and 4-nitrocinnamic acid using the same method. Finally, the target compound was obtained by reacting the resin with a mixed solution of trifluoroacetic acid:phenol: anisole sulfide:water = 90:5:2.5:2.5 for 4 h. The TFA was removed by filtration, and an appropriate amount of frozen diethyl ether was added to precipitate the product. The supernatant was removed by centrifugation, and the resulting solid was freeze-dried to obtain the crude product. The crude product was purified by reversed-phase C18 semi-preparative high-performance liquid chromatography (HPLC). The chromatographic conditions were: mobile phase of 45% acetonitrile aqueous solution (containing 0.1% TFA), flow rate of 10 mL / min, detection wavelength of 215 nm, and HPLC retention time of approximately 29.0 min. The structural identification data are shown in Table 1, and the structure was confirmed to be correct by high-resolution mass spectrometry.

[0041] Other target compounds A-2 to A-30 were prepared according to the above method.

[0042] Example 2: Preparation of the compound shown in A-2 (R1 from 4-nitrocinnamic acid, R2 from glycine, R3 from L-phenylalanine, R4 from glycine, R5 from D-leucine)

[0043] Compound A-2 was prepared following the same steps as in Example 1, except that R3 was replaced with L-phenylalanine and R5 with D-leucine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0044] Example 3: Preparation of the compound shown in A-3 (R1 from 4-nitrocinnamic acid, R2 from glycine, R3 from D-phenylalanine, R4 from glycine, R5 from D-leucine)

[0045] Compound A-3 was prepared following the same steps as in Example 1, except that R5 was replaced with D-leucine. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0046] Example 4: Preparation of the compounds shown in A-4 (R1 from 4-nitrocinnamic acid, R2 from D-aspartic acid, R3 from L-phenylalanine, R4 from glycine, R5 from L-leucine)

[0047] Compound A-4 was prepared following the same steps as in Example 1, except that R2 was replaced with D-aspartic acid and R3 with L-phenylalanine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0048] Example 5: Preparation of the compounds shown in A-5 (R1 from 4-nitrocinnamic acid, R2 from L-aspartic acid, R3 from D-phenylalanine, R4 from glycine, R5 from L-leucine)

[0049] Compounds shown in A-5 were prepared following the same procedures as in Example 1, except that R2 was replaced with L-aspartic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0050] Example 6: Preparation of the compounds shown in A-6 (R1 from 4-nitrocinnamic acid, R2 from L-aspartic acid, R3 from L-phenylalanine, R4 from glycine, R5 from D-leucine)

[0051] Compounds shown in A-6 were prepared following the same procedures as in Example 1, except that R2 was replaced with L-aspartic acid, R3 with L-phenylalanine, and R5 with D-leucine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0052] Example 7: Preparation of the compounds shown in A-7 (R1 from 4-nitrocinnamic acid, R2 from D-aspartic acid, R3 from D-phenylalanine, R4 from glycine, R5 from L-leucine)

[0053] Compounds shown in A-7 were prepared following the same procedures as in Example 1, except that R2 was replaced with D-aspartic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0054] Example 8: Preparation of the compounds shown in A-8 (R1 from 4-nitrocinnamic acid, R2 from D-aspartic acid, R3 from L-phenylalanine, R4 from glycine, R5 from D-leucine)

[0055] Compounds shown in A-8 were prepared following the same procedures as in Example 1, except that R2 was replaced with D-aspartic acid, R3 with L-phenylalanine, and R5 with D-leucine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0056] Example 9: Preparation of the compounds shown in A-9 (R1 from 4-nitrocinnamic acid, R2 from L-aspartic acid, R3 from D-phenylalanine, R4 from glycine, R5 from D-leucine)

[0057] Compounds shown in A-9 were prepared following the same procedures as in Example 1, except that R2 was replaced with L-aspartic acid and R5 with D-leucine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0058] Example 10: Preparation of the compounds shown in A-10 (R1 from 4-nitrocinnamic acid, R2 from D-aspartic acid, R3 from D-phenylalanine, R4 from glycine, R5 from D-leucine)

[0059] Compound A-10 was prepared following the same steps as in Example 1, except that R2 was replaced with D-aspartic acid and R5 with D-leucine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0060] Example 11: Preparation of the compound shown in A-11 (R1 is from cinnamic acid, R2 is from D-tert-leucine, R3 is from β-alanine, R4 is from L-tryptophan, R5 is from glycine)

[0061] Compound A-11 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-tert-leucine, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0062] Example 12: Preparation of the compound shown in A-12 (R1 from cinnamic acid, R2 from D-homophylline, R3 from β-alanine, R4 from L-tryptophan, R5 from glycine)

[0063] Compound A-12 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-homophylline, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0064] Example 13: Preparation of the compound shown in A-13 (R1 from cinnamic acid, R2 from D-2-aminobutyric acid, R3 from β-alanine, R4 from L-tryptophan, R5 from glycine)

[0065] Compound A-13 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-2-aminobutyric acid, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0066] Example 14: Preparation of the compound shown in A-14 (R1 from cinnamic acid, R2 from D-4-trifluoromethylphenylalanine, R3 from β-alanine, R4 from L-tryptophan, R5 from glycine)

[0067] Compound A-14 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-4-trifluoromethylphenylalanine, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0068] Example 15: Preparation of the compounds shown in A-15 (R1 from cinnamic acid, R2 from D-valine, R3 from β-alanine, R4 from L-tryptophan, R5 from glycine)

[0069] Compound A-15 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-valine, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0070] Example 16: Preparation of the compound shown in A-16 (R1 from cinnamic acid, R2 from D-cyclohexylalanine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0071] Compound A-16 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-cyclohexylalanine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0072] Example 17: Preparation of the compound shown in A-17 (R1 from cinnamic acid, R2 from D-cyclohexylalanine, R3 from β-alanine, R4 from L-tryptophan, R5 from glycine)

[0073] Compound A-17 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-cyclohexylalanine, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0074] Example 18: Preparation of the compound shown in A-18 (R1 from cinnamic acid, R2 from D-valine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0075] Compound A-18 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-valine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0076] Example 19: Preparation of the compound shown in A-19 (R1 from cinnamic acid, R2 from D-tert-leucine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0077] Compound A-19 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-tert-leucine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0078] Example 20: Preparation of the compounds shown in A-20 (R1 from cinnamic acid, R2 from D-homophylline, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0079] Compound A-20 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-homophylline, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0080] Example 21: Preparation of the compound shown in A-21 (R1 from cinnamic acid, R2 from D-2-aminobutyric acid, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0081] Compound A-21 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-2-aminobutyric acid, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0082] Example 22: Preparation of the compound shown in A-22 (R1 from cinnamic acid, R2 from D-4-trifluoromethylphenylalanine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0083] Compound A-22 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with D-4-trifluoromethylphenylalanine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0084] Example 23: Preparation of the compound shown in A-23 (R1 from cinnamic acid, R2 from L-2-aminobutyric acid, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0085] Compound A-23 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-2-aminobutyric acid, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0086] Example 24: Preparation of the compounds shown in A-24 (R1 from cinnamic acid, R2 from L-tert-leucine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0087] Compound A-24 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-tert-leucine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0088] Example 25: Preparation of the compounds shown in A-25 (R1 from cinnamic acid, R2 from L-valine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0089] Compound A-25 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-valine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0090] Example 26: Preparation of the compounds shown in A-26 (R1 from cinnamic acid, R2 from L-cyclohexylalanine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0091] Compound A-26 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-cyclohexylalanine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0092] Example 27: Preparation of the compounds shown in A-27 (R1 from cinnamic acid, R2 from L-homophenylalanine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0093] Compound A-27 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-homophenylalanine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0094] Example 28: Preparation of the compounds shown in A-28 (R1 from cinnamic acid, R2 from L-4-trifluoromethylphenylalanine, R3 from β-alanine, R4 from D-tryptophan, R5 from glycine)

[0095] Compound A-28 was prepared following the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 with L-4-trifluoromethylphenylalanine, R3 with β-alanine, R4 with D-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0096] Example 29: Preparation of the compound shown in A-29 (R1 is empty, R2 is from L-aspartic acid, R3 is from L-phenylalanine, R4 is from glycine, R5 is from L-leucine)

[0097] Compound A-29 was prepared following the same steps as in Example 1, except that R1 was left blank, R2 was replaced with L-aspartic acid, and R3 was replaced with L-phenylalanine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0098] Preparation of compounds shown in Examples 30 and A-30 (R1 is empty, R2 is from L-phenylalanine, R3 is from β-alanine, R4 is from L-tryptophan, R5 is from glycine)

[0099] Compound A-30 was prepared following the same steps as in Example 1, except that R1 was left blank, R2 was replaced with L-phenylalanine, R3 with β-alanine, R4 with L-tryptophan, and R5 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0100] Using compound B-1 as a representative compound (but not limited to this compound), describe the preparation process of compounds B-1 to B-26.

[0101] Example 31: Preparation of the compound shown in B-1 (R6 is from L-phenylalanine, R7 is from glycine, and R8 is from L-leucine)

[0102] Rink Amide-Am resin (0.3 mmol) was activated in 5 mL of DCM for 2 h, then washed 5 times with DMF, and then reacted with 5 mL of 20% piperidine DMF solution for 20 min to remove the Fmoc protecting groups on the resin. A 5 mL DMF solution containing Fmoc-L-leucine-OH (1.2 mmol), HBTU (1.2 mmol), HOBt (1.2 mmol), and DIEA (1.2 mmol) was prepared, activated for 5 min, and then reacted with the resin at room temperature for 2 h to obtain Fmoc-L-leucine with Rink Amide-Am resin. The Fmoc groups were further removed by sequentially inoculating Fmoc-glycine-OH and Fmoc-L-phenylalanine-OH using the same method. Finally, the target compound was obtained by reacting the resin with a mixed solution of trifluoroacetic acid:phenol: anisole:water = 90:5:2.5:2.5 for 4 h. The TFA was removed by filtration, and an appropriate amount of frozen diethyl ether was added to precipitate the product. The supernatant was removed by centrifugation, and the resulting solid was freeze-dried to obtain the crude product. The crude product was purified by reversed-phase C18 semi-preparative high-performance liquid chromatography (HPLC). The chromatographic conditions were: mobile phase of 45% acetonitrile aqueous solution (containing 0.1% TFA), flow rate of 10 mL / min, detection wavelength of 215 nm, and HPLC retention time of approximately 8.6 min. The structural identification data are shown in Table 1, and the structure was confirmed by high-resolution mass spectrometry.

[0103] Other target compounds B-2 to B-26 were prepared according to the above method.

[0104] Example 32: Preparation of the compound shown in B-2 (R6 from nicotinic acid, R7 from glycine, R8 from L-leucine)

[0105] Compound B-2 was prepared following the same steps as in Example 31, except that R6 was replaced with nicotinic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0106] Example 33: Preparation of the compound shown in B-3 (R6 from piperic acid, R7 from glycine, R8 from L-leucine)

[0107] Compound B-3 was prepared following the same steps as in Example 31, except that R6 was replaced with piperic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0108] Example 34: Preparation of the compounds shown in B-4 (R6 from sinapic acid, R7 from glycine, R8 from L-leucine)

[0109] Compound B-4 was prepared following the same steps as in Example 31, except that R6 was replaced with sinapic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0110] Example 35: Preparation of the compounds shown in B-5 (R6 from naphthaleneacetic acid, R7 from glycine, R8 from L-leucine)

[0111] Compound B-5 was prepared following the same steps as in Example 31, except that R6 was replaced with naphthaleneacetic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0112] Example 36: Preparation of the compounds shown in B-6 (R6 from vanillic acid, R7 from glycine, R8 from L-leucine)

[0113] Compound B-6 was prepared following the same steps as in Example 31, except that R6 was replaced with vanillic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0114] Example 37: Preparation of the compounds shown in B-7 (R6 from syringic acid, R7 from glycine, R8 from L-leucine)

[0115] Compound B-7 was prepared following the same steps as in Example 31, except that R6 was replaced with syringic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0116] Example 38: Preparation of the compounds shown in B-8 (R6 is from gallic acid, R7 is from glycine, and R8 is from L-leucine).

[0117] Compound B-8 was prepared following the same steps as in Example 31, except that R6 was replaced with gallic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0118] Example 39, Preparation of the compounds shown in B-9 (R6 from protocatechuic acid, R7 from glycine, R8 from L-leucine)

[0119] Compound B-9 was prepared following the same steps as in Example 31, except that R6 was replaced with protocatechuic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0120] Preparation of compounds shown in Examples 40 and B-10 (R6 from coumaric acid, R7 from glycine, R8 from L-leucine)

[0121] Compound B-10 was prepared following the same steps as in Example 31, except that R6 was replaced with coumaric acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0122] Example 41: Preparation of the compound shown in B-11 (R6 from furoic acid, R7 from glycine, R8 from L-leucine)

[0123] Compound B-11 was prepared following the same steps as in Example 31, except that R6 was replaced with furoic acid. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0124] Example 42: Preparation of the compound shown in B-12 (R6 is from L-phenylalanine, R7 is from glycine, and R8 is from L-histidine)

[0125] Compound B-12 was prepared following the same steps as in Example 31, except that R8 was replaced with L-histidine. Structural identification data are shown in Table 1, and the structure was verified to be correct.

[0126] Example 43: Preparation of the compound shown in B-13 (R6 from nicotinic acid, R7 from glycine, R8 from L-histidine)

[0127] Compound B-13 was prepared following the same steps as in Example 31, except that R6 was replaced with nicotinic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0128] Example 44, Preparation of the compound shown in B-14 (R6 from piperic acid, R7 from glycine, R8 from L-histidine)

[0129] Compound B-14 was prepared following the same steps as in Example 31, except that R6 was replaced with piperic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0130] Example 45: Preparation of the compounds shown in B-15 (R6 from sinapic acid, R7 from glycine, R8 from L-histidine)

[0131] Compound B-15 was prepared following the same steps as in Example 31, except that R6 was replaced with sinapic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0132] Example 46: Preparation of the compound shown in B-16 (R6 from naphthaleneacetic acid, R7 from glycine, R8 from L-histidine)

[0133] Compound B-16 was prepared following the same steps as in Example 31, except that R6 was replaced with naphthaleneacetic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0134] Example 47, Preparation of the compound shown in B-17 (R6 from vanillic acid, R7 from glycine, R8 from L-histidine)

[0135] Compound B-17 was prepared following the same steps as in Example 31, except that R6 was replaced with vanillic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0136] Example 48, Preparation of the compound shown in B-18 (R6 from syringic acid, R7 from glycine, R8 from L-histidine)

[0137] Compound B-18 was prepared following the same steps as in Example 31, except that R6 was replaced with syringic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0138] Preparation of compounds shown in Examples 49 and B-19 (R6 derived from cinnamic acid, R7 from glycine, R8 from L-histidine)

[0139] Compound B-19 was prepared following the same steps as in Example 31, except that R6 was replaced with cinnamic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0140] Preparation of compounds shown in Examples 50 and B-20 (R6 from furoic acid, R7 from glycine, R8 from L-histidine)

[0141] Compound B-20 was prepared following the same steps as in Example 31, except that R6 was replaced with furoic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0142] Example 51, Preparation of the compound shown in B-21 (R6 from coumaric acid, R7 from glycine, R8 from L-histidine)

[0143] Compound B-21 was prepared following the same steps as in Example 31, except that R6 was replaced with coumaric acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0144] Preparation of compounds shown in Examples 52 and B-22 (R6 from salicylic acid, R7 from glycine, R8 from L-histidine)

[0145] Compound B-22 was prepared following the same steps as in Example 31, except that R6 was replaced with salicylic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0146] Preparation of compounds shown in Examples 53 and B-23 (R6 derived from gallic acid, R7 from glycine, and R8 from L-histidine)

[0147] Compound B-23 was prepared following the same steps as in Example 31, except that R6 was replaced with gallic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0148] Preparation of compounds shown in Examples 54 and B-24 (R6 derived from protocatechuic acid, R7 from glycine, and R8 from L-histidine)

[0149] Compound B-24 was prepared following the same steps as in Example 31, except that R6 was replaced with protocatechuic acid and R8 with L-histidine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0150] Preparation of compounds shown in Examples 55 and B-25 (R6 from β-alanine, R7 from L-tryptophan, R8 from glycine)

[0151] Compound B-25 was prepared following the same steps as in Example 31, except that R6 was replaced with β-alanine, R7 with L-tryptophan, and R8 with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0152] Example 56, Preparation of the compound shown in B-26 (R6 is left blank, R7 is from L-tryptophan, R8 is from glycine)

[0153] Compound B-26 was prepared following the same steps as in Example 31, except that R6 was left empty, R7 was replaced with L-tryptophan, and R8 was replaced with glycine. The structural identification data are shown in Table 1, and the structure was verified to be correct.

[0154] The structures, high-resolution or mass spectrometry data, and purities of the compounds shown in Formula A are listed in Table 1.

[0155] Table 1. Structures, high-resolution mass spectrometry data, and purities of the compounds shown in Formula A.

[0156] The structures, high-resolution or mass spectrometry data, and purities of the compounds shown in Formula B are listed in Table 2.

[0157] Table 2 shows the structure, high-resolution mass spectrometry data, and purity of the compounds represented by Formula B.

[0158] Example 57: Bioactivity of compounds of formulas A and B against the Asian corn borer (Ostrinia furnacalis)

[0159] This embodiment uses representative compounds (but not limited to) of Formulas A and B to test the insecticidal activity against the Asian corn borer. The bioactivity of the target compounds against the Asian corn borer was determined using the feed method (Jin, X.-Y. et al. J. Agric. Food Chem. 2023, 71, 8345-8355). The specific steps are as follows: The target compound was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a 200 mg / L stock solution. The stock solution was continuously diluted to different concentrations with the buffer solution. Artificial feed was mixed with the test solution and placed in 9 cm petri dishes. Each group contained 15 second-instar larvae, and each concentration was repeated three times. Finally, the petri dishes were stored in an incubator at 25±2℃, 70% RH (relative humidity), and a 16:8h (light:dark photocycle). The results were checked after 96h, 120h, 144h, and 168h. The formula for calculating the adjusted mortality rate is shown in Figure 1. Adjusted mortality rate (%) = (TC) × 100 / (100% - C) (1)

[0160] The corrected mortality rate was assessed using formula (1), where T represents the mortality rate of the test compound group and C represents the mortality rate of the blank control group (T and C are expressed as percentages). Data on the insecticidal activity of some compounds from formulas A and B against the Asian corn borer are shown in Table 3.

[0161] Table 3. Insecticidal activity (200 mg / L) of representative compounds of formulas A and B against the Asian corn borer (Ostrinia furnacalis)

[0162] As shown in Table 3, some of the compounds of formula A and formula B provided by this invention exhibit excellent insecticidal activity against the tested Asian corn borer. At 168 h, at a concentration of 200 mg / L, 23 target compounds (A-1 to A-10, B-1 to B-7, B10, B13 to B15, B20, and B23) showed insecticidal activity of over 80%, and 6 target compounds (A-5, A-7 to A-10, and B18) showed 100% insecticidal activity, comparable to the positive control phenoxycarb, demonstrating promising potential as insecticides for controlling the agricultural pest, the Asian corn borer.

[0163] Example 58: Bioactivity of compounds of formulas A and B against the diamondback moth (Plutella xylostella).

[0164] This embodiment uses representative compounds (but not limited to) of Formulas A and B to test the insecticidal activity against diamondback moth. The bioactivity was evaluated using the leaf-dipping method proposed by the International Resistant Pesticides Action Committee (IRAC). The specific steps are as follows: The target compound was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a 200 mg / L stock solution. The stock solution was continuously diluted to different concentrations with the buffer solution. Cabbage leaves were immersed in solutions with different insecticide concentrations for 3 seconds. Control leaves were treated with 0.05% Triton X-100 and DMSO solutions. After drying at room temperature for 2 hours, the leaves were placed in petri dishes (9 cm in diameter). Each concentration was repeated three times (15 second-instar larvae per repeat). Finally, the petri dishes were stored in an incubator at 25±2℃, 70±20% RH (relative humidity), and a 14:10h (light:dark photoperiod). Results were checked at 72h, 96h, 120h, and 144h. The insect was considered dead if it could not crawl normally when gently touched with a needle. The corrected mortality rate was calculated using the formula shown in Figure 1. Corrected mortality rate (%) = (TC) × 100 / (100% - C) (1)

[0165] The corrected mortality rate was assessed using formula (1), where T represents the mortality rate of the test compound group and C represents the mortality rate of the blank control group (T and C are expressed as percentages). Data on the insecticidal activity of some compounds from formulas A and B against the diamondback moth are shown in Table 4.

[0166] Table 4. Insecticidal activity (200 mg / L) of representative compounds of formula A and B against diamondback moth (Plutella xylostella).

[0167] As shown in Table 4, some of the compounds of formula A and formula B provided by this invention exhibit moderate to good insecticidal activity against the tested diamondback moth. At 144 h, at a concentration of 200 mg / L, 10 compounds (A-2, A-3, A-5 to A-8, A-10, B6, B17, and B18) showed insecticidal activity exceeding 80% against the diamondback moth, and 4 compounds (A-6, A-7, A-8, and A-10) showed insecticidal activity exceeding 90%, which is superior to the activity of the positive control phenoxycarb, demonstrating its potential as an insecticide for controlling the agricultural pest, the diamondback moth.

[0168] Example 59: Bioactivity of compounds of formulas A and B against the peach aphid (Myzus persicae)

[0169] This embodiment uses representative compounds (but not limited to) of Formulas A and B to test the insecticidal activity against peach aphids. The insecticidal activity against peach aphids was determined using the leaf immersion method. The target compound was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a 200 mg / L stock solution. The stock solution was continuously diluted to different concentrations with the buffer solution. Cabbage leaves were immersed in solutions with different insecticide concentrations for 3 seconds. Control leaves were treated with 0.05% Triton X-100 and DMSO solutions. After drying at room temperature for 2 hours, the leaves were placed in petri dishes (3 cm in diameter), with 1.5% agar added to the bottom for humidification. Each concentration was repeated three times (twenty peach aphids per repeat). Finally, the petri dishes were stored in an incubator at 25±3℃, 70±10% RH (relative humidity), and a 16:8h (light:dark) photoperiod. After 48 hours, the results were checked; if the aphid could not crawl normally when gently touched with a needle, it was considered dead. The formula for calculating the adjusted mortality rate is shown in Figure 1. Adjusted mortality rate (%) = (TC) × 100 / (100% - C) (1)

[0170] The corrected mortality rate was assessed using formula (1), where T represents the mortality rate of the test compound group and C represents the mortality rate of the blank control group (T and C are expressed as percentages). Data on the insecticidal activity of some compounds from formulas A and B against peach aphids are shown in Table 5.

[0171] Table 5. Insecticidal activity (200 mg / L) of representative compounds of formulas A and B against the peach aphid (Myzus persicae).

[0172] As shown in Table 5, some of the compounds of formula A and formula B provided by this invention exhibit moderate to good insecticidal activity against the tested peach aphid. At 48 h, at a concentration of 200 mg / L, 10 compounds (B-2, B-7, B-8, B-10 to B-13, B-16, B-17, and B-20) showed insecticidal activity exceeding 80% against the peach aphid, and 8 compounds (B-2, B-7, B-10, B-11, B-13, B-16, B-17, and B-20) showed insecticidal activity exceeding 90%, which is superior to the activity of the positive control pymetrozine. Therefore, they show promise as insecticides for controlling the agricultural pest, the peach aphid.

[0173] Example 60: Bioactivity of the compounds shown in Formula A and Formula B against the pea aphid (Acyrthosiphon pisum)

[0174] This embodiment uses representative compounds (but not limited to) of Formulas A and B to test the insecticidal activity against pea aphids. The activity against pea aphids was also determined using the leaf immersion method. The target compound was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a 200 mg / L stock solution. The stock solution was continuously diluted to different concentrations with the buffer solution. Broad bean leaves were immersed in solutions with different insecticide concentrations for 3 seconds. Control leaves were treated with 0.05% Triton X-100 and DMSO solutions. After drying at room temperature for 2 hours, the leaves were placed in petri dishes (3 cm in diameter), with 1.5% agar added to the bottom for humidification. Each concentration was repeated three times (twenty pea aphids per repeat). Finally, the petri dishes were stored in an incubator at 25±3℃, 70±10% RH (relative humidity), and a 16:8h (light:dark) photoperiod. After 48 hours, the results were checked; if the insect could not crawl normally when gently touched with a needle, it was considered dead. The formula for calculating the adjusted mortality rate is shown in Figure 1. Adjusted mortality rate (%) = (TC) × 100 / (100% - C) (1)

[0175] The corrected mortality rate was assessed using formula (1), where T represents the mortality rate of the test compound group and C represents the mortality rate of the blank control group (T and C are expressed as percentages). Data on the insecticidal activity of some compounds from formulas A and B against pea aphids are shown in Table 6.

[0176] Table 6. Insecticidal activity (200 mg / L) of representative compounds of formulas A and B against pea aphid (Acyrthosiphon pisum)

[0177] As shown in Table 6, some of the compounds of formula A and formula B provided by this invention exhibit moderate to good insecticidal activity against the tested pea aphid. At 48 h, at a concentration of 200 mg / L, 10 compounds (A-2, A-3, A-6, A-8, B-7, B-9, B-10, B-13, B-18, and B-19) showed insecticidal activity exceeding 70% against the pea aphid, and 3 compounds (A-6, B-10, and B-19) showed insecticidal activity exceeding 80%, comparable to the activity of the positive control pymetrozine, demonstrating promising potential as insecticides for controlling the agricultural pest, the pea aphid.

[0178] Example 61: Bioactivity of compounds of formula A and formula B against soybean aphid (Aphis glycines)

[0179] This embodiment uses representative compounds (but not limited to) of the compounds shown in Formulas A and B to test the insecticidal activity against soybean aphids. The activity against soybean aphids was determined using the leaf immersion method. The target compound was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a 200 mg / L stock solution. The stock solution was continuously diluted to different concentrations with the buffer solution. Soybean leaves were immersed in solutions with different insecticide concentrations for 3 seconds. Control leaves were treated with 0.05% Triton X-100 and DMSO solutions. After drying at room temperature for 2 hours, the leaves were placed in petri dishes (3 cm in diameter), with 1.5% agar added to the bottom for humidification. Each concentration was repeated three times (twenty soybean aphids per repeat). Finally, the petri dishes were stored in an incubator at 25±3℃, 70±10% RH (relative humidity), and a 16:8h (light:dark) photoperiod. After 48 hours, the results were checked; the insects were considered dead if they could not crawl normally when gently touched with a needle. The formula for correcting the mortality rate is as shown in Figure 1. Corrected mortality rate (%) = (TC) × 100 / (100% - C) (1)

[0180] The corrected mortality rate was assessed using formula (1), where T represents the mortality rate of the test compound group and C represents the mortality rate of the blank control group (T and C are expressed as percentages). Data on the insecticidal activity of some compounds from formulas A and B against soybean aphids are shown in Table 7.

[0181] Table 7. Insecticidal activity (200 mg / L) of representative compounds of formula A and formula B against soybean aphid (Aphis glycines)

[0182] As shown in Table 7, some of the compounds of formula A and formula B provided by this invention exhibit moderate to good insecticidal activity against the tested soybean aphid. At a concentration of 200 mg / L, 11 compounds (A-11 to A-14, A-16, A-21, A-24 to A-28) showed insecticidal activity exceeding 70% against soybean aphid, and one compound, A-21, showed insecticidal activity exceeding 90%, which is superior to the activity of the positive control pymetrozine, demonstrating its potential as an insecticide for controlling the agricultural pest, soybean aphid.

[0183] Cross-reference to related applications

[0184] This application claims the benefit and priority of Chinese Patent 202510372279.4, filed on March 27, 2025. The entire disclosure of that earlier application is incorporated herein by reference. Industrial applicability

[0185] This invention employs a peptide-mimicking strategy, introducing hydrogen, acid, natural amino acids, or non-natural amino acids at different sites for substitution modification. The insecticidal activity of several new compounds is very significant, superior to commercial pesticides phenoxycarb and pymetrozine, and is expected to be applied to the green control of agricultural pests.

Claims

1. Insect neuropeptide analogs, the structural formulas of which are shown in Formula A and Formula B: In formula A: R1 is selected from cinnamic acid, 4-nitrocinnamic acid, or R1 is not present. R2, R3, R4, and R5 are all amino acids; The rightmost amino group in Formula A is provided by the solid-phase resin used in the solid-phase synthesis of the polypeptide; the carboxyl group of the amino acid shown in R5 forms -CONH2 with the amino group. In formula B: R6 is selected from any one of L-phenylalanine, nicotinic acid, piperic acid, sinapic acid, naphthaleneacetic acid, vanillic acid, syringic acid, gallic acid, protocatechuic acid, coumaric acid, furoic acid, cinnamic acid, salicylic acid, and β-alanine, or R6 is absent. R7 and R8 are both amino acids; The rightmost amino group in Formula B is provided by the solid-phase resin used in the solid-phase synthesis of the polypeptide, and the carboxyl group of the amino acid shown in R8 forms -CONH2 with this amino group.

2. The insect neuropeptide analogue according to claim 1, characterized in that, In Formula A, R2 is selected from any one of glycine, L-aspartic acid, D-aspartic acid, D-tert-leucine, L-tert-leucine, D-homogeneous alanine, L-homogeneous alanine, D-2-aminobutyric acid, L-2-aminobutyric acid, D-4-trifluoromethylphenylalanine, L-4-trifluoromethylphenylalanine, D-valine, L-valine, D-cyclohexylalanine, L-cyclohexylalanine, and L-phenylalanine. R3 is selected from any one of L-phenylalanine, D-phenylalanine, and β-alanine; R4 is selected from any one of glycine, D-tryptophan, and L-tryptophan; R5 is selected from any one of L-leucine, D-leucine, and glycine; In this case, the carboxyl group in R1 forms an amide bond with the amino group of the amino acid shown in R2; The carboxyl group of the amino acid shown in R2 forms an amide bond with the amino group of the amino acid shown in R3. The carboxyl group of the amino acid shown in R3 forms an amide bond with the amino group of the amino acid shown in R4. The carboxyl group of the amino acid shown in R4 forms an amide bond with the amino group of the amino acid shown in R5.

3. The insect neuropeptide analogue according to claim 1, characterized in that, In formula B, R7 is selected from either glycine or L-tryptophan; R8 is selected from any one of L-leucine, L-histidine, and glycine; Among them, the carboxyl group contained in R6 forms an amide bond with the amino group of the amino acid shown in R7; The carboxyl group of the amino acid shown in R7 forms an amide bond with the amino group of the amino acid shown in R8.

4. The use of the insect neuropeptide analogue according to any one of claims 1-3 in pest control.

5. The application according to claim 4, characterized in that, The pests mentioned are Lepidoptera and Hemiptera pests.

6. The application according to claim 5, characterized in that, The lepidopteran pest is at least one of the Asian corn borer and the diamondback moth, and the hemiptera pest is at least one of the peach aphid, the pea aphid, and the soybean aphid.

7. A pest control agent comprising the insect neuropeptide analogue of any one of claims 1-3.

8. The pest control agent according to claim 7, characterized in that, The pests mentioned are Lepidoptera and Hemiptera pests.

9. The pest control agent according to claim 8, characterized in that, The lepidopteran pest is at least one of the Asian corn borer and the diamondback moth, and the hemiptera pest is at least one of the peach aphid, the pea aphid, and the soybean aphid.

10. The pest control agent according to claim 7, characterized in that, The pest control agent is an insecticide.

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