Insect neuropeptide analogue and application thereof in pest control

Abstract

The invention discloses an insect neuropeptide analogue and application thereof in pest control. The structural formulas of the compounds are shown as a formula A and a formula B, the insect neuropeptide analogue disclosed by the invention is efficient, broad-spectrum and environment-friendly. The compound provided by the invention has multiple biological activities, has an obvious insecticidal effect on Lepidoptera Asiatic corn borer, Plutella xylostella, hemiptera green peach aphid, pea aphid, soybean aphid and the like, and can be used as a novel green and safe pest control agent. # imgabs0 #

Description

Technical Field

[0001] The present invention belongs to the field of agriculture, and particularly relates to a class of insect neuropeptide analogs and their applications in pest control, and more particularly to the applications of such compounds in controlling Lepidoptera pests such as Asian corn borer, diamondback moth and Hemiptera pests such as green peach aphid, pea aphid and soybean aphid. Background Art

[0002] Various Lepidoptera insects have caused significant losses to crops worldwide. The Asian corn borer (Ostrinia furnacalis) is an important agricultural pest that causes serious damage to cash crops such as corn and sorghum. The diamondback moth (Plutella xylostella) is one of the most destructive pests in the world. They target plants such as broccoli and cabbage, have few natural enemies, reproduce effectively, and have become devastating pests of cruciferous crops due to their strong reproductive ability and extensive resistance to pesticides. Aphids are an important group of economic pests worldwide. As piercing-sucking mouthpart pests, aphids not only directly cause harm by sucking plant sap, but also secrete honeydew, breed molds, induce plant diseases, and are also the primary insect vectors for transmitting plant viruses, causing serious harm to agriculture and the environment (Zhou, Y.-L. et al. Pest Manag. Sci. 2022, 78, 2952 - 2963). For example, the green peach aphid (Myzus persicae) feeds on hundreds of species in more than forty plant families, damaging a wide range of horticultural and food crops, and is a highly harmful polyphagous pest with a global distribution. The pea aphid (Acyrthosiphon pisum) is an important pest worldwide and feeds almost entirely on leguminous plants. The soybean aphid (Aphis glycines) is a herbivorous pest in many soybean-growing areas, which can cause a serious decline in yields.

[0003] Currently, pesticides are still the main means of pest control. However, with the long-term and large-scale use of chemical pesticides, serious problems such as pest resistance and toxicity to non-target organisms have emerged (Woodcock B A et al. Science. 2017, 356: 1393–1395). For example, some neonicotinoid pesticides such as imidacloprid and thiamethoxam have been successively banned due to bee toxicity problems (Butler D et al. Nature. 2018, 557: 14). In addition, with the aggravation of environmental pollution, residues and other problems, how to better control pests has attracted the attention of many scientific workers. Therefore, on the premise of ecological friendliness, developing new, efficient and safe insecticides is of great significance for protecting the ecology and slowing down resistance.

[0004] Insect neuropeptides are a group of brain neuromodulators that play very important roles in insect growth and development, molting and metamorphosis, as well as mating and reproduction (Cui H.-Y. et al. J. Integr. Agric. 2020, 19(6), 1429-1438.). Due to these series of important physiological functions of insect neuropeptides, they are considered as a class of potential pest control agents. However, due to the inherent disadvantages of natural insect neuropeptides, such as easy degradation, poor transport function, and large molecular flexibility, etc., the application of natural neuropeptides in pest control is limited. To overcome these defects, the structures of natural neuropeptides have been modified, and some neuropeptide analogs have been disclosed in the following literatures: such as Zubrzak, P. et al. Biopolymers. 2007, 88, 76-82.; Smagghe, G. et al. Peptides. 2010, 31, 498-505.; Nachman, R. J. et al. Peptides. 2012, 34, 262-265; Zhang C.-L. et al. Peptides. 2015, 68, 233-238; Wang M.-Z. Bioorganic Med. Chem. Lett. 2019, 29, 890-895. In the above literatures, there are mainly two characteristics of the modification of neuropeptide structures: 1) Most use natural amino acids such as alanine, or unnatural amino acids such as 4-amino-5-imidazolecarboxamide and aromatic acids, etc., to replace the amino acids in natural neuropeptides to obtain analogs with very similar structures. 2) Most compounds retain the original in vitro biological activities of neuropeptides. However, there are still the following deficiencies: The structures of some compounds are complex (simulating bioactive peptides with more than five peptides), and the synthesis cost is high; The in vivo stability of the analogs is not ideal, the in vivo biological activities are still not very prominent, and the spectrum of action is relatively narrow, mainly concentrated on Blattella germanica and Aphis glycines. Therefore, there are still certain limitations in directly applying them as pesticide molecules in agricultural production. In view of these deficiencies, the present invention discloses a class of novel insect neuropeptide analogs with simple structures, good stability, and broad spectrum of action, as well as their applications in pest control. Summary of the Invention

[0005] One object of the present invention is to provide a class of insect neuropeptide analogs.

[0006] The insect neuropeptide analogs provided by the present invention have structural formulas as shown in Formula A and Formula B:

[0007]

[0008] In Formula A:

[0009] wherein R1 is selected from any one of cinnamic acid and 4-nitrocinnamic acid or R1 does not exist;

[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-homophenylalanine, L-homophenylalanine, 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 contained in R1 forms an amide bond with the amino group of the amino acid represented by R2;

[0016] The carboxyl group of the amino acid represented by R2 forms an amide bond with the amino group of the amino acid represented by R3;

[0017] The carboxyl group of the amino acid represented by R3 forms an amide bond with the amino group of the amino acid represented by R4;

[0018] The carboxyl group of the amino acid represented by R4 forms an amide bond with the amino group of the amino acid represented by R5;

[0019] The rightmost amino group in formula A is provided by the solid-phase resin used in solid-phase peptide synthesis; the carboxyl group of the amino acid represented by R5 forms -CONH2 with this 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, β-alanine or R6 does not exist;

[0022] R7 and R8 are both amino acids;

[0023] R7 is selected from any one of glycine and L-tryptophan;

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

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

[0026] The carboxyl group of the amino acid represented by R7 and the amino group of the amino acid represented by R8 form an amide bond;

[0027] The rightmost amino group in formula B is provided by the solid-phase resin used in solid-phase peptide synthesis. The carboxyl group of the amino acid represented by R8 and this amino group form -CONH2.

[0028] The compounds represented by formula A and formula B provided by the present invention are all prepared according to the solid-phase peptide synthesis method (References: W Chan, Peter White. Fmoc solid phase peptide synthesis: A Practical Approach, Oxford University Press, 2000; pp. 9 - 74.)

[0029] The second object of the present invention is to provide the application of the compound represented by the above formula A or formula B in pest control.

[0030] The third object of the present invention is to provide a pest control agent.

[0031] The pest control agent contains the insect neuropeptide analog represented by the above formula A or formula B.

[0032] The pests are Lepidoptera and Hemiptera pests.

[0033] The Lepidoptera pests can specifically be at least one of Ostrinia furnacalis and Plutella xylostella, and the Hemiptera pests can specifically be at least one of Myzus persicae, Acyrthosiphon pisum, and Aphis glycines.

[0034] The insecticidal activity of the compounds of the present invention against Ostrinia furnacalis was determined by the feeding method (References: Jin X.-Y. et al. J. Agr. Food Chem. 2023, 71, 8345 - 8355). The insecticidal activity against Plutella xylostella and aphids was determined by the leaf-dipping method (References: 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). The bioassay results show that: the compounds of the present invention have very obvious insecticidal activity against Ostrinia furnacalis and Plutella xylostella, and also have good activity against Myzus persicae, Acyrthosiphon pisum, and Aphis glycines. The activities of some compounds are better than those of the commercial agents fenoxycarb and pymetrozine, and have the value of further application and development as green pest control agents.

[0035] The beneficial effects of the present invention are as follows: The present invention adopts the strategy of mimotope, and invents a class of insect neuropeptide analogs, that is, hydrogen, acid, natural amino acids or unnatural amino acids are introduced at different sites for substitution modification to obtain a series of small peptide analogs with novel structures and more stable properties. The insecticidal activities of multiple new compounds are very obvious, superior to the commercial agents fenoxycarb and pymetrozine, and are expected to be applied to the green prevention and control of agricultural pests. Detailed implementation manners

[0036] The present invention will be further described in detail below in conjunction with the specific implementation manners. The examples given are only for clarifying the present invention, rather than limiting the scope of the present invention. The following examples can be used as a guide for those of ordinary skill in the art to make further improvements, and do not limit the present invention in any way.

[0037] The experimental methods in the following examples are all conventional methods unless otherwise specified, and are carried out according to the techniques or conditions described in the literature in this field or according to the product instructions. The materials, reagents, etc. used in the following examples can be obtained from commercial sources unless otherwise specified.

[0038] Taking compound A-1 as a representative compound (but not limited to this compound), the preparation processes of compounds A-1 to A-30 are described.

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

[0040] Take Rink Amide-Am resin (0.3 mmol) and activate it in 5 mL of DCM for 2 h. Then wash it 5 times with DMF, and add 5 mL of a DMF solution containing 20% piperidine and react for 20 min to remove the Fmoc protecting group on the resin. Prepare 5 mL of a DMF solution containing Fmoc-L-leucine-OH (1.2 mmol), HBTU (1.2 mmol), HOBt (1.2 mmol), and DIEA (1.2 mmol). After activation for 5 min, react with the resin at room temperature for 2 h to obtain Fmoc-L-leucine with Rink Amide-Am resin. Continue to remove the Fmoc group, and successively introduce Fmoc-glycine-OH, Fmoc-D-phenylalanine-OH, Fmoc-glycine-OH, and 4-nitrocinnamic acid in the same method. Finally, react the resin with a mixed solution of trifluoroacetic acid:phenol:benzyl methyl sulfide:water = 90:5:2.5:2.5 for 4 h to obtain the target product. Filter, remove TFA, add an appropriate amount of frozen ether to precipitate, centrifuge to remove the supernatant, and the obtained solid is freeze-dried to obtain the crude product. The crude product is separated by reversed-phase C18 semi-preparative high-performance liquid chromatography to obtain the pure product. The chromatographic conditions are: the mobile phase is an aqueous solution of 45% acetonitrile (containing 0.1% TFA), the flow rate is 10 mL / min, the detection wavelength is 215 nm, and the HPLC retention time is about 29.0 min. The structure identification data are shown in Table 1, and the structure is confirmed to be correct by high-resolution mass spectrometry.

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

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

[0043] Prepare the compound shown in A-2 according to the same steps as in Example 1, only replacing R3 with L-phenylalanine and R5 with D-leucine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0045] Prepare the compound shown in A-3 according to the same steps as in Example 1, only replacing R5 with D-leucine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

[0046] Example 4. Preparation of the compound shown as A-4 (R1 is from 4-nitrocinnamic acid, R2 is from D-aspartic acid, R3 is from L-phenylalanine, R4 is from glycine, and R5 is from L-leucine)

[0047] The compound shown as A-4 was prepared according to the same procedure as in Example 1, except that R2 was replaced with D-aspartic acid and R3 was replaced with L-phenylalanine. The structure identification data are shown in Table 1, and after verification, the structure was correct.

[0048] Example 5. Preparation of the compound shown as A-5 (R1 is from 4-nitrocinnamic acid, R2 is from L-aspartic acid, R3 is from D-phenylalanine, R4 is from glycine, and R5 is from L-leucine)

[0049] The compound shown as A-5 was prepared according to the same procedure as in Example 1, except that R2 was replaced with L-aspartic acid. The structure identification data are shown in Table 1, and after verification, the structure was correct.

[0050] Example 6. Preparation of the compound shown as A-6 (R1 is from 4-nitrocinnamic acid, R2 is from L-aspartic acid, R3 is from L-phenylalanine, R4 is from glycine, and R5 is from D-leucine)

[0051] The compound shown as A-6 was prepared according to the same procedure as in Example 1, except that R2 was replaced with L-aspartic acid, R3 was replaced with L-phenylalanine, and R5 was replaced with D-leucine. The structure identification data are shown in Table 1, and after verification, the structure was correct.

[0052] Example 7. Preparation of the compound shown as A-7 (R1 is from 4-nitrocinnamic acid, R2 is from D-aspartic acid, R3 is from D-phenylalanine, R4 is from glycine, and R5 is from L-leucine)

[0053] The compound shown as A-7 was prepared according to the same procedure as in Example 1, except that R2 was replaced with D-aspartic acid. The structure identification data are shown in Table 1, and after verification, the structure was correct.

[0054] Example 8. Preparation of the compound shown as A-8 (R1 is from 4-nitrocinnamic acid, R2 is from D-aspartic acid, R3 is from L-phenylalanine, R4 is from glycine, and R5 is from D-leucine)

[0055] The compound shown as A-8 was prepared according to the same procedure as in Example 1, except that R2 was replaced with D-aspartic acid, R3 was replaced with L-phenylalanine, and R5 was replaced with D-leucine. The structure identification data are shown in Table 1, and after verification, the structure was correct.

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

[0057] The compound shown as A-9 was prepared according to the same procedure as in Example 1, except that R2 was replaced with L-aspartic acid and R5 was replaced with D-leucine. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0059] The compound shown as A-10 was prepared according to the same procedure as in Example 1, except that R2 was replaced with D-aspartic acid and R5 was replaced with D-leucine. The structure identification data are shown in Table 1. After verification, the structure was correct.

[0060] Example 11. Preparation of the compound shown as 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] The compound shown as A-11 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-tert-leucine, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0063] The compound shown as A-12 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-homophenylalanine, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0065] The compound shown in A-13 was prepared according to the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-2-aminobutyric acid, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is 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] The compound shown in A-14 was prepared according to the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-4-trifluoromethylphenylalanine, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0069] The compound shown in A-15 was prepared according to the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-valine, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is 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] The compound shown in A-16 was prepared according to the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-cyclohexylalanine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is 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] The compound shown in A-17 was prepared according to the same steps as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-cyclohexylalanine, R3 was replaced with β-alanine, R4 was replaced with L-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0075] The compound shown as A-18 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-valine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0077] The compound shown as A-19 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-tert-leucine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0079] The compound shown as A-20 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-homophenylalanine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0081] The compound shown as A-21 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-2-aminobutyric acid, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0083] The compound shown in A-22 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with D-4-trifluoromethylphenylalanine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure was 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] The compound shown in A-23 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with L-2-aminobutyric acid, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure was correct.

[0086] Example 24, Preparation of the compound 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] The compound shown in A-24 was prepared according to the same procedure as in Example 1, except that R1 was replaced with cinnamic acid, R2 was replaced with L-tert-leucine, R3 was replaced with β-alanine, R4 was replaced with D-tryptophan, and R5 was replaced with glycine. The structure identification data are shown in Table 1, and after verification, the structure was correct.

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

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

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

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

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

[0093] The compound shown as A-27 was prepared according to the same procedure as in Example 1, except that R1 was replaced by cinnamic acid, R2 was replaced by L-homophenylalanine, R3 was replaced by β-alanine, R4 was replaced by D-tryptophan, and R5 was replaced by glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0095] The compound shown as A-28 was prepared according to the same procedure as in Example 1, except that R1 was replaced by cinnamic acid, R2 was replaced by L-4-trifluoromethylphenylalanine, R3 was replaced by β-alanine, R4 was replaced by D-tryptophan, and R5 was replaced by glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

[0096] Example 29. Preparation of the compound shown as 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] The compound shown as A-29 was prepared according to the same procedure as in Example 1, except that R1 was set to be empty, R2 was replaced by L-aspartic acid, and R3 was replaced by L-phenylalanine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

[0098] Example 30. Preparation of the compound shown as 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] The compound shown as A-30 was prepared according to the same procedure as in Example 1, except that R1 was set to be empty, R2 was replaced by L-phenylalanine, R3 was replaced by β-alanine, R4 was replaced by L-tryptophan, and R5 was replaced by glycine. The structure identification data are shown in Table 1, and after verification, the structure is correct.

[0100] Taking compound B-1 as a representative compound (but not limited to this compound), the preparation processes of compounds B-1 to B-26 are described

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

[0102] Take Rink Amide-Am resin (0.3 mmol) and activate it in 5 mL of DCM for 2 h. Then, wash it 5 times with DMF and add 5 mL of a DMF solution containing 20% piperidine to react for 20 min to remove the Fmoc protecting group on the resin. Prepare 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). After activation for 5 min, react it with the resin at room temperature for 2 h to obtain Fmoc-L-leucine with Rink Amide-Am resin. Continue to remove the Fmoc group and sequentially introduce Fmoc-glycine-OH and Fmoc-L-phenylalanine-OH in the same manner. Finally, react the resin with a mixed solution of trifluoroacetic acid:phenol:benzyl mercaptan:water = 90:5:2.5:2.5 for 4 h to obtain the target product. Filter, remove TFA, add an appropriate amount of frozen ether to precipitate, centrifuge to remove the supernatant, and freeze-dry the obtained solid to obtain the crude product. The crude product is separated by reverse-phase C18 semi-preparative high-performance liquid chromatography to obtain the pure product. The chromatographic conditions are as follows: the mobile phase is an aqueous solution of 45% acetonitrile (containing 0.1% TFA), the flow rate is 10 mL / min, the detection wavelength is 215 nm, and the HPLC retention time is about 8.6 min. The structure identification data are shown in Table 1, and the structure is confirmed to be correct by high-resolution mass spectrometry.

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

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

[0105] Prepare the compound shown in B-2 according to the same steps as in Example 31, only replacing R6 with nicotinic acid. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0107] Prepare the compound shown in B-3 according to the same steps as in Example 31, only replacing R6 with piperonylic acid. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0109] Prepare the compound shown in B-4 according to the same steps as in Example 31, only replacing R6 with sinapic acid. The structure identification data are shown in Table 1, and after verification, the structure is correct.

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

[0111] The compound shown in B-5 was prepared according to the same procedure as in Example 31, except that R6 was replaced with naphthaleneacetic acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0113] The compound shown in B-6 was prepared according to the same procedure as in Example 31, except that R6 was replaced with vanillic acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0115] The compound shown in B-7 was prepared according to the same procedure as in Example 31, except that R6 was replaced with syringic acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0117] The compound shown in B-8 was prepared according to the same procedure as in Example 31, except that R6 was replaced with gallic acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0119] The compound shown in B-9 was prepared according to the same procedure as in Example 31, except that R6 was replaced with protocatechuic acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

[0120] Example 40. Preparation of the compound shown in B-10 (R6 is from coumaric acid, R7 is from glycine, and R8 is from L-leucine)

[0121] The compound shown in B-10 was prepared according to the same procedure as in Example 31, except that R6 was replaced with coumaric acid. The structure identification data are shown in Table 1. After verification, the structure was correct.

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

[0123] The compound shown in B-11 was prepared according to the same procedure as in Example 31, except that R6 was replaced with furoic acid. The structure 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 from L-phenylalanine, R7 from glycine, R8 from L-histidine)

[0125] The compound shown in B-12 was prepared according to the same procedure as in Example 31, except that R8 was replaced with L-histidine. The structure 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] The compound shown in B-13 was prepared according to the same procedure as in Example 31, except that R6 was replaced with nicotinic acid and R8 was replaced with L-histidine. The structure 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] The compound shown in B-14 was prepared according to the same procedure as in Example 31, except that R6 was replaced with piperic acid and R8 was replaced with L-histidine. The structure identification data are shown in Table 1, and the structure was verified to be correct.

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

[0131] The compound shown in B-15 was prepared according to the same procedure as in Example 31, except that R6 was replaced with sinapic acid and R8 was replaced with L-histidine. The structure 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] The compound shown in B-16 was prepared according to the same procedure as in Example 31, except that R6 was replaced with naphthaleneacetic acid and R8 was replaced with L-histidine. The structure 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] The compound shown in B-17 was prepared according to the same procedure as in Example 31, except that R6 was replaced with vanillic acid and R8 was replaced with L-histidine. The structure identification data are shown in Table 1 and were 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] The compound shown in B-18 was prepared according to the same procedure as in Example 31, except that R6 was replaced with syringic acid and R8 was replaced with L-histidine. The structure identification data are shown in Table 1 and were verified to be correct.

[0138] Example 49, Preparation of the compound shown in B-19 (R6 from cinnamic acid, R7 from glycine, R8 from L-histidine)

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

[0140] Example 50, Preparation of the compound shown in B-20 (R6 from furoic acid, R7 from glycine, R8 from L-histidine)

[0141] The compound shown in B-20 was prepared according to the same procedure as in Example 31, except that R6 was replaced with furoic acid and R8 was replaced with L-histidine. The structure identification data are shown in Table 1 and were 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] The compound shown in B-21 was prepared according to the same procedure as in Example 31, except that R6 was replaced with coumaric acid and R8 was replaced with L-histidine. The structure identification data are shown in Table 1 and were verified to be correct.

[0144] Example 52, Preparation of the compound shown in B-22 (R6 from salicylic acid, R7 from glycine, R8 from L-histidine)

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

[0146] Example 53, Preparation of the compound shown in B-23 (R6 from gallic acid, R7 from glycine, R8 from L-histidine)

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

[0148] Example 54, Preparation of the compound shown in B-24 (R6 from protocatechuic acid, R7 from glycine, R8 from L-histidine)

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

[0150] Example 55, Preparation of the compound shown in B-25 (R6 from β-alanine, R7 from L-tryptophan, R8 from glycine)

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

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

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

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

[0155] Table 1, Structure, high-resolution mass spectrometry data, and purity of the compound shown in Formula A

[0156]

[0157]

[0158]

[0159] The structure, high-resolution or mass spectrometry data, and purity of the compound shown in Formula B are listed in Table 2.

[0160] Table 2, Structure, high-resolution mass spectrometry data, and purity of the compound shown in Formula B

[0161]

[0162]

[0163]

[0164] Example 57, Biological Activity of Compounds Shown in Formula A and Formula B against Asian Corn Borer (Ostrinia furnacalis)

[0165] In this example, the insecticidal activities of representative compounds (but not limited to these compounds) shown in Formula A and Formula B against Asian corn borer were tested. The bioactivity of the target compounds against Asian corn borer was determined by the diet 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 stock solution of 200 mg / L. The stock solution was continuously diluted with the buffer solution to different concentrations. The artificial diet was mixed with the test solution and placed in a 9-cm petri dish. 15 second-instar larvae were placed in each group, and each concentration was repeated three times. Finally, the petri dishes were stored in an incubator at 25 ± 2 °C, 70% RH (relative humidity), and a 16:8 h (light:dark photoperiod). The results were checked at 96 h, 120 h, 144 h, and 168 h. The calculation formula for corrected mortality is as shown in Equation (1).

[0166] Corrected Mortality (%) = (T - C) × 100 / (100% - C) (1)

[0167] The corrected mortality was evaluated by Equation (1), where T represents the mortality of the test compound group and C represents the mortality of the blank control group (T and C are expressed as percentages). The insecticidal activity data of some compounds in Formula A and Formula B against Asian corn borer are shown in Table 3

[0168] Table 3, Insecticidal Activities of Representative Compounds in Formula A and Formula B against Asian Corn Borer (Ostrinia furnacalis) (200 mg / L)

[0169]

[0170]

[0171]

[0172] As can be seen from Table 3, the partial compounds of Formula A and Formula B provided by the present invention have 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, B23) showed insecticidal activity of more than 80%, and 6 target compounds (A-5, A-7 to A-10, B18) showed 100% insecticidal activity, which was comparable to the activity of the positive control fenoxycarb, and had the prospect of being used as an insecticide to control the Asian corn borer, an agricultural pest.

[0173] Example 58, Biological Activity of Compounds of Formula A and Formula B against Plutella xylostella

[0174] In this example, the representative compounds of the compounds of Formula A and Formula B (but not limited to these compounds) were used to test the insecticidal activity against Plutella xylostella. The leaf-dipping method proposed by the Insecticide Resistance Action Committee (IRAC) was used for biological activity evaluation. The specific steps were as follows: The target substance was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a stock solution of 200 mg / L, and the stock solution was continuously diluted with the buffer solution to different concentrations. The cabbage leaves were immersed in the solution with different insecticide concentrations for 3 seconds, and the control leaves were treated with 0.05% Triton X-100 and DMSO solution. After the leaves were dried at room temperature for 2 hours, they were placed in a petri dish (9 cm in diameter). Each concentration was repeated three times (fifteen second-instar larvae for each repetition). Finally, the petri dishes were placed in an incubator at 25 ± 2 °C, 70 ± 20% RH (relative humidity) and 14:10 h (light:dark photoperiod). The results were checked at 72 h, 96 h, 120 h, and 144 h respectively. If the insect body could not crawl normally when gently touched with a needle, it was considered dead. The formula for calculating the corrected mortality rate was as shown in (1).

[0175] Corrected mortality rate (%) = (T - C) × 100 / (100% - C) (1)

[0176] The corrected mortality rate was evaluated by formula (1), where T represented the mortality rate of the test compound group and C represented the mortality rate of the blank control group (T and C were expressed as percentages). The insecticidal activity data of some compounds of Formula A and Formula B against Plutella xylostella are shown in Table 4

[0177] Table 4, Insecticidal Activity of Representative Compounds of Formula A and Formula B against Plutella xylostella (200 mg / L)

[0178]

[0179]

[0180] As can be seen from Table 4, the partial compounds of Formula A and Formula B provided by the present invention have moderate to good insecticidal activities against the diamondback moth tested. At 144 h and a concentration of 200 mg / L, 10 compounds (A-2, A-3, A-5 to A-8, A-10, B6, B17, and B18) have insecticidal activities exceeding 80% against the diamondback moth, and 4 compounds (A-6, A-7, A-8, and A-10) have insecticidal activities exceeding 90%, which are superior to the activity of the positive control fenoxycarb, and have the prospect of being used as pesticides to control the diamondback moth, an agricultural pest.

[0181] Biological Activity of the Compounds Shown in Formula A and Formula B in Example 59 against Myzus persicae

[0182] In this example, the insecticidal activities of the representative compounds (but not limited to these compounds) shown in Formula A and Formula B were tested against Myzus persicae. The leaf-dipping method was used to determine the insecticidal activities against Myzus persicae. The target substances were dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a stock solution of 200 mg / L, and the stock solution was continuously diluted with the buffer solution to different concentrations. Cabbage leaves were immersed in the solution with different insecticide concentrations for 3 seconds, and the control leaves were treated with 0.05% Triton X-100 and DMSO solution. After the leaves were dried at room temperature for 2 hours, they were placed in a petri dish (diameter 3 cm), and 1.5% agar was added at the bottom for moisturizing. Each concentration was repeated three times (twenty Myzus persicae each time). Finally, the petri dishes were stored in an incubator at 25 ± 3°C, 70 ± 10% RH (relative humidity), and a 16:8 h (light:dark photoperiod). The results were checked after 48 h. If the insect body could not crawl normally when gently touched with a dissecting needle, it was considered dead. The formula for calculating the corrected mortality rate is as shown in Equation (1).

[0183] Corrected Mortality Rate (%) = (T - C) × 100 / (100% - C) (1)

[0184] The corrected mortality rate was evaluated by Equation (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). The insecticidal activity data of some compounds of Formula A and Formula B against Myzus persicae are shown in Table 5

[0185] Table 5. Insecticidal Activities of Representative Compounds of Formula A and Formula B against Myzus persicae (200 mg / L)

[0186]

[0187]

[0188] As can be seen from Table 5, the partial compounds of Formula A and Formula B provided by the present invention have moderate to good insecticidal activities against the tested Myzus persicae. At 48 h and a concentration of 200 mg / L, 10 compounds (B-2, B-7, B-8, B-10 - B-13, B-16, B-17, and B-20) have insecticidal activities exceeding 80% against Myzus persicae, and 8 compounds (B-2, B-7, B-10, B-11, B-13, B-16, B-17, and B-20) have insecticidal activities exceeding 90%, which are superior to the activity of the positive control pymetrozine. Therefore, they have the prospect of being used as pesticides to control the agricultural pest Myzus persicae.

[0189] Biological Activities of the Compounds Shown in Formula A and Formula B Against Acyrthosiphon pisum in Example 60

[0190] In this example, the insecticidal activities of the representative compounds (but not limited to these compounds) shown in Formula A and Formula B against Acyrthosiphon pisum were tested. The leaf-dipping method was also used for the activity determination against Acyrthosiphon pisum. The target substance was dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a stock solution of 200 mg / L. The stock solution was continuously diluted with the buffer solution to different concentrations. The broad bean leaves were immersed in the solutions with different insecticide concentrations for 3 seconds, and the control leaves were treated with 0.05% Triton X-100 and DMSO solution. After the leaves were dried at room temperature for 2 hours, they were placed in a culture dish (diameter 3 cm), and 1.5% agar was added to the bottom for moisture retention. Each concentration was repeated three times (20 Acyrthosiphon pisum each time). Finally, the culture dishes were placed in an incubator at 25 ± 3°C, 70 ± 10% RH (relative humidity), and a 16:8 h (light:dark photoperiod). After 48 h, the results were checked. If the insect body could not crawl normally when gently touched with a needle, it was considered dead. The calculation formula for the corrected mortality rate is as shown in (1).

[0191] Corrected Mortality Rate (%) = (T - C) × 100 / (100% - C) (1)

[0192] The corrected mortality rate was evaluated by 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). The insecticidal activity data of some compounds of Formula A and Formula B against Acyrthosiphon pisum are shown in Table 6

[0193] Table 6. Insecticidal Activities of Representative Compounds of Formula A and Formula B Against Acyrthosiphon pisum (200 mg / L)

[0194]

[0195]

[0196] As can be seen from Table 6, the partial compounds of Formula A and Formula B provided by the present invention have moderate to good insecticidal activities against the tested pea aphids. At 48 h and 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) have insecticidal activities exceeding 70% against pea aphids, and 3 compounds (A-6, B-10, and B-19) have insecticidal activities exceeding 80%, which are comparable to the activity of the positive control pymetrozine, and have the prospect of controlling the agricultural pest pea aphid as an insecticide.

[0197] Example 61. Biological Activities of the Compounds Shown in Formula A and Formula B against Aphis glycines

[0198] In this example, the representative compounds (but not limited to these compounds) shown in Formula A and Formula B were used to test the insecticidal activities against Aphis glycines. The leaf-dipping method was used for the activity determination against Aphis glycines. The target substances were dissolved in DMSO, and a certain amount of 0.05% (w / v) Triton X-100 buffer solution was added to prepare a stock solution of 200 mg / L, and the stock solution was continuously diluted with the buffer solution to different concentrations. Soybean leaves were immersed in the solutions with different insecticide concentrations for 3 seconds, and the control leaves were treated with 0.05% Triton X-100 and DMSO solutions. After the leaves were dried at room temperature for 2 hours, they were placed in a culture dish (diameter 3 cm), and 1.5% agar was added at the bottom for moisture retention. Each concentration was repeated three times (20 Aphis glycines each time). Finally, the culture dishes were kept in an incubator at 25 ± 3 °C, 70 ± 10% RH (relative humidity), and a 16:8 h (light:dark photoperiod). After 48 h, the results were checked, and if the insect body could not crawl normally when gently touched with a needle, it was regarded as dead. The calculation formula for the corrected mortality rate is as shown in Equation (1).

[0199] Corrected mortality rate (%) = (T - C) × 100 / (100% - C) (1)

[0200] The corrected mortality rate was evaluated by Equation (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). The insecticidal activity data of some compounds of Formula A and Formula B against Aphis glycines are shown in Table 7.

[0201] Table 7. Insecticidal Activities of Representative Compounds of Formula A and Formula B against Aphis glycines (200 mg / L)

[0202]

[0203] As can be seen from Table 7, the partial formula A and formula B compounds provided by the present invention have medium to good insecticidal activities against the tested Aphis glycines. At a concentration of 200 mg / L, 11 compounds (A-11 to A-14, A-16, A-21, A-24 to A-28) have an insecticidal activity of more than 70% against Aphis glycines, and 1 compound A-21 has an insecticidal activity of more than 90%, which is superior to the activity of the positive control pymetrozine, and has the prospect of being used as an insecticide to control the agricultural pest Aphis glycines.

[0204] The present invention has been described in detail above. For those skilled in the art, without departing from the gist and scope of the present invention and without unnecessary experiments, the present invention can be implemented within a relatively wide range under equivalent parameters, concentrations and conditions. Although specific embodiments of the present invention are given, it should be understood that the present invention can be further improved. In short, according to the principle of the present invention, this application intends to cover any modification, use or improvement of the present invention, including those that depart from the scope disclosed in this application and are made by conventional techniques known in the art.

Claims

1. An insect neuropeptide analogue, the structural formula of which is shown as Formula A and Formula B: In Formula A: wherein R1 is selected from any one of cinnamic acid and 4-nitrocinnamic acid or R1 does not exist; R2, R3, R4, and R5 are all amino acids; The amino group on the far right in Formula A is provided by the solid-phase resin used in solid-phase peptide synthesis; the carboxyl group of the amino acid shown by R5 forms -CONH2 with this 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, β-alanine or R6 does not exist; R7 and R8 are both amino acids; The amino group on the far right in Formula B is provided by the solid-phase resin used in solid-phase peptide synthesis, and the carboxyl group of the amino acid shown by R8 forms -CONH2 with this amino group.

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

3. The insect neuropeptide analogue according to claim 1, wherein In Formula B, R7 is selected from any one of glycine, L-tryptophan; R8 is selected from any one of L-leucine, L-histidine, glycine. Wherein, the carboxyl group contained in R6 forms an amide bond with the amino group of the amino acid shown by R7; The carboxyl group of the amino acid shown by R7 forms an amide bond with the amino group of the amino acid shown by R8.

4. 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 are Lepidoptera and Hemiptera pests.

6. The application according to claim 5, wherein The Lepidoptera pests are at least one of Asian corn borer and diamondback moth, and the Hemiptera pests are at least one of green peach aphid, pea aphid and soybean aphid.

7. A pest control agent, which contains the insect neuropeptide analogue according to any one of claims 1-3.

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

9. The pest control agent according to claim 8, wherein, The Lepidoptera pests are at least one of Asian corn borer and diamondback moth, and the Hemiptera pests are at least one of green peach aphid, pea aphid and 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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