WATER-SOLUBLE ADJUVANT

Abstract

The present invention relates to a compound useful as a vaccine adjuvant for a cancer vaccine, a process for preparing the same, a pharmaceutical composition comprising the compound, and the use of the compound as a vaccine adjuvant for a cancer vaccine.

Description

WATER SOLUBLE ADJUVANT TECHNICAL FIELD The present invention relates to a compound useful as a vaccine adjuvant for vaccine (cancer vaccine or infection vaccine), a manufacturing process thereof, a pharmaceutical composition comprising the compound and the use of the compound as a vaccine adjuvant for the vaccine (cancer vaccine or infection vaccine). BACKGROUND OF THE INVENTION In general, cancer vaccine therapy activates a tumor-specific immune cell by using proteins or peptides obtained from tumor antigen to treat a cancer. Among therapies, a therapy in which tumor antigen peptide is used as an antigen is called cancer peptide vaccine therapy. In general, therapy with only tumor antigenic peptide produces low immunogenicity. Therefore, to induce cytotoxic T lymphocytes (CTL), which is important for antitumor immunity, a vaccine adjuvant is used together. For example, W / O emulsion can easily retain an antigenic peptide in its internal phase because it has an aqueous phase in the internal phase. Therefore, it has been reported that the use of W / O emulsion as a vaccine adjuvant shows effective CTL induction (Patent Literature 1). The W / O emulsion to be used as a vaccine adjuvant for the tumor antigenic peptide includes an emulsion composition for dilution (Patent Literature 1), as well as incomplete Freund's adjuvant (IFA) and Montanide™ (Non-patent Literature 1 and 2). Furthermore, Complete Freund's Adjuvant (CFA) is also known and is prepared by adding inactivated Mycobacterium Tuberculosis to the W / O emulsion. However, CFA has not been permitted for use in humans due to its toxicity (Non-Patent Literature 2). Conventionally, adjuvant compositions prepared by adding an inactivated bacterial body itself to an adjuvant such as CFA had been used to improve target activity, but recently vaccine adjuvants have been developed comprising a compound whose working mechanism is known. Among them, Toll-like receptor 7 (TLR7) has been reported to activate Thl cells to enhance cellular immunity that is necessary for antitumor activity (Non-patent Literature 3). Regarding TLR7, some small molecules are known to act as a ligand, and the imiquimod that has been on the market, as well as a compound that has a pyrimidine structure, have been reported to act as a ma / i / uazuuy agonist. TLR7 (Patent Literature 2). Some trials have been performed to improve a TLR7 agonist to find a new compound that has a suitable physical property as an adjuvant. For example, a TLR7 agonist having a conjugated phosphate group structure has been reported to bind to an insoluble metal particle such as alum adjuvant (Patent Literature 3, Non-Patent Literature 4 and 5). Previous technique Patent reference [Patent Literature 1] WO 2006 / 078059 [Patent Literature 2] WO2012 / 067081 [Patent Literature 3] WO2012 / 031140 Non-patent reference [Non-patent literature 1] J Immunother Cancer. 2016 Sep 20; 4:56 [Non-patent literature 2] Semin Immunol. 2010 Jun; 22(3): 155-61. [Non-patent literature 3] Vaccine. 2011 April 12; 29(17): 3341-55. [Non-patent literature 4] Sci Transí Med. 2014 Nov 19; 6(263): 263ral60 [Non-patent literature 5] 1 Med. Chem., 2016, 59 (12), pp 5868-5878 BRIEF DESCRIPTION OF THE INVENTION technical problem The purpose of the present invention may be to provide a conjugated TLR7 agonist to enhance adjuvant activity. Solution to the problem The present inventors have studied extensively to find a TLR7 agonist to enhance the adjuvant activity, and then have discovered that a TLR7 agonist to which water solubility is added by conjugating a TLR7 agonist having a pyrimidine structure with polyethylene glycol (PEG) has an excellent adjuvant activity. Based on the findings, the present invention has been achieved. According to the present invention, there is provided a pyrimidine derivative of the following formula (1) (hereinafter also referred to as the present compound). The present invention is as described below. ma / i / uazuuy (Point 1) A compound of formula (1): NH, ma / 1 / uazuuy or a pharmaceutically acceptable salt thereof, wherein X is hydrogen atom, sulfur atom, SO, SO2, or NR5, where R1 is Ci-e alkyl which may be substituted with 1-5 substituents independently selected from the group consisting of halogen, hydroxy, and Ci-e alkoxy, R2 and R3 are independently a hydrogen atom or C1-6 alkyl which may be substituted with 1-5 substituents independently selected from the group consisting of halogen, hydroxy, and C1-6 alkoxy, R4 is a hydrogen atom, halogen, hydroxy, C1-6 alkyl (which may be substituted with 1-3 same or different halogens), C1-6 alkoxy (which may be substituted with 1-3 same or different halogens) or cyano, L is a linker, and Y1 is -(CH2CH2O)m-R6, where R6 is hydrogen atom or C1-6 alkyl, and m is an integer from 3 - 100. (Point 2) The compound of item 1 or a pharmaceutically acceptable salt thereof, where X is methylene. (Point 3) The compound of item 1 or 2 or a pharmaceutically acceptable salt thereof, where R1 is C1-3 alkyl which may be substituted with 1-3 equal or different halogens. (Point 4) The compound of item 3 or a pharmaceutically acceptable salt thereof, where R1 is methyl. (Point 5) The compound of any of items 1 to 4 or a pharmaceutically acceptable salt thereof, where R4 is hydrogen atom, hydroxy, C1-3 alkyl, or C1-3 alkoxy. (Point 6) The compound of item 5 or a pharmaceutically acceptable salt thereof, where R4 is a hydrogen, hydroxy, or methoxy atom. (Point 7) The compound of any of items 1 to 6 or a pharmaceutically acceptable salt thereof, where R2 is Ci-e alkyl. (Point 8) The compound of any of items 1 to 7 or a pharmaceutically acceptable salt thereof, where R3 is a hydrogen atom, or C1-3 alkyl which may be substituted with 1-3 hydroxy. (Point 9) The compound of any of items 1 to 8 or a pharmaceutically acceptable salt thereof, wherein L is -O-, -NRY-, -C(O)-, -C(O)O-, -OC(O)-, -C(O)NRY-, -NRYC(O)-, -CH2NRY- , -CH2O-, OC(O)O-, -NR7C(O)O-, -OC(O)NRY-, -NR7C(O)NRY-, -OC(S)NRY-, or -NR7C(S) NRY-, where R7 is hydrogen atom or C1-6 alkyl, and RYes is hydrogen atom, C1-6 alkyl, or Y2, where Y2 is (CH2CH2O)n-R8 (where R8 is hydrogen atom or C1-6 alkyl , and n is an integer of 3 100). (Point 10) The compound of item 9 or a pharmaceutically acceptable salt thereof, where L is -C(O)NRY-, -CH2NRY-, -C(O)O-, or -CH2O-. μλ / 1 / uazuuy (Point 11) The compound of item 9 or a pharmaceutically acceptable salt thereof, where L is -C(O)NRY- or -CH2NRY-. (Point 12) The compound of item 9 or a pharmaceutically acceptable salt thereof, wherein L is -CH2NRy-, and RYes a hydrogen atom, Ci-6 alkyl, or Y2. (Point 13) The compound of item 9 or a pharmaceutically acceptable salt thereof, wherein L is -CH2NRy-, and RYes a hydrogen atom or Ci-6 alkyl. (Point 14) The compound of any of items 1 to 13 or a pharmaceutically acceptable salt thereof, wherein Y1es -(CH2CH2O)m-R6, R6 is a hydrogen atom or Ci-6 alkyl, and m is an integer from 3 - 40. (Point 15) The compound of item 14 or a pharmaceutically acceptable salt thereof, wherein Y1es -(CH2CH2O)m-R6, R6 is a hydrogen atom or Ci-6 alkyl, and m is an integer from 3 - 20. μλ / i / uazuuy (Point 16) The compound of item 1 or a pharmaceutically acceptable salt thereof, where the compound is a compound of formula (2): ΜΛ / I / UUZUUU or formula (3): where R2is Ci-6 alkyl, R3 is a hydrogen atom, or C1-3 alkyl which may be substituted with 1 - 3 hydroxy, R4 is a hydrogen, hydroxy, or methoxy atom, L is -CH2NRY-, -C(O)NRy-, -C(O)O-, or -CH2O-, RYes hydrogen atom, C1-6 alkyl, or Y2, Y1es -(CH2CH2O)m-R6, Y2es -(CH2CH2O)n-R8, R6 is hydrogen atom or C1-6 alkyl, R8 is a hydrogen atom or C1-6 alkyl, and m and n are independently an integer from 3 - 40. (Point 17) The compound of item 1 or a pharmaceutically acceptable salt thereof, where the compound is a compound of formula (2): NH2ma / t / zuz 1 / uazuuy or formula (3): where R2is Ci-6 alkyl, R3 is a hydrogen atom, or Ci 3 alkyl which may be substituted with 1 - 3 hydroxy, R4 is a hydrogen, hydroxy, or methoxy atom, L is -CH2NRY-, RYes hydrogen atom or C1-6 alkyl, Y1es -(CH2CH2O)m-R6, R6 is a hydrogen atom or C1-6 alkyl, and m is an integer from 3 - 20. (Point 18) The compound of item 1 or a pharmaceutically acceptable salt thereof, where the compound is a compound of formula (2): ma / 1 / uazuuy where R2is Ci-6 alkyl, R3 is hydrogen atom, or C1-3 alkyl which may be substituted with a hydroxy, R4 is hydrogen or methoxy atom, L is -CH2NRY-, RYes hydrogen atom or C1-6 alkyl, Y1es -(CH2CH2O)m-R6, R6 is a hydrogen atom or C1-6 alkyl, and m is an integer from 3 - 40. (Point 19) The compound of point 1 or a pharmaceutically acceptable salt thereof, which is selected from: l-(4-{[2-amino-4-methyl-6-(pentylamino)pyrimidin-5-yl]methyl}-3-methoxyphenyl)-2-methyl5,8,ll, 14-tetraoxa-2-azahexadecan-16-ol (example 1), l-{4-[(2-amino-4-{[(3S)-l-hydroxyhexan-3-yl]amino}- 6-met¡lp¡rimidin-5-yl)methyl]-3methoxyphen¡l}-2-methyl-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol (example 2), l-(3-{[2-am¡no-4-met¡l-6-(pent¡lam¡no)p¡r¡m¡d¡n-5-¡l]met¡l}-4- methoxyfen¡l)-2-met¡l5,8,ll,14-tetraoxa-2-azahexadecan-16-ol (example 3), l-(3-{[2-amino-4-met¡ l-6-(pent¡lam¡no)p¡r¡m¡d¡n-5-¡l]met¡l}-4-hydroxy¡phen¡l)-2-met¡l5,8, ll,14-tetraoxa-2-azahexadecan-16-ol (example 4), 4-[(2-amino-4-{[(2S)-l-hydroxy¡pentan-2-¡l]amino}- 6-met¡lp¡rmidín-5-yl)methyl]-N-(20hydroxy¡-3,6,9,12,15,18-hexaoxaicosan-l-yl)-3-methoxybenzamide ( example 5), 2,5,8,ll-tetraoxatridecan-13-l 4-[(2-amino-4-{[(2S)-l-hydroxylpentan-2-l]amino}-6 methylpyrimidin -5-l)methyl]-3-methoxybenzoate (example 6), 5-{[2-methoxy¡-4-(2,5,8,ll,14-pentaoxapentadecan-l-¡l)phen¡l]methyl}-6-methyl-N4pentylpyrmidine-2, 4-diamine (example 7), l-(4-{[2-amino-4-methyl-6-(pentylamino)pyrimidin-5-yl]methyl}-3-methoxyphenyl )-2-methyl5,8,ll,14,17,20,23,26,29-nonaoxa-2-azahentriacontan-31-ol (example 8), l-(4-{[2-amino -4-met¡l-6-(pent¡lam¡no)pyrám¡d¡n-5-¡l]met¡l}-3-methoxy¡phen¡l)-2-met¡l5,8 ,ll,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71-tricosaoxa-2azatriheptacontan-73-ol (example 9), l-(4-{[2-amino-4-methyl-6-(pentalamino)pyrimidin-5-yl]methyl}-3-methoxyphenyl)-2-methyl5,8,11 ,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80,83,86 ,89,92,95,98,10 l,104,107-pentatriacontaoxa-2-azanonahectan-109-ol (example 10), and 12-[(4-{[2-amino-4-methyl-6-(pentylamine)pyrimidin-5-l]methyl}-3-methoxyphenyl)methyl]3 ,6,9,15,18,21-hexaoxa-12-azatricosan-l,23-diol (example 11). (Point 20) The compound of point 1 or a pharmaceutically acceptable salt thereof, which is selected from: l-(4-{[2-amino-4-methyl-6-(pentylamino)pyrimidin-5-yl]methyl}-3-methoxyphenyl)-2-methyl5,8,ll, 14-tetraoxa-2-azahexadecan-16-ol (example 1), l-{4-[(2-amino-4-{[(3S)-l-hydroxy¡hexan-3-¡l]am¡ no}-6-methylpyrimídin-5-íl)methyl]-3methoxyphenyl}-2-methyl-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol (example 2), l-(3-{[2-am¡no-4-met¡l-6-(pent¡lam¡no)p¡r¡m¡d¡n-5-¡l]met¡l}-4- methoxyphenyl)-2-methyl5,8,ll,14-tetraoxa-2-azahexadecan-16-ol (example 3), and l-(3-{[2-amino-4-met ¡l-6-(pent¡lam¡no)pyrámid¡n-5-¡l]met¡l}-4-hydroxy¡phen¡l)-2-met¡l5,8,ll,14 -tetraoxa-2-azahexadecan-16-ol (example 4). (Point 21) A pharmaceutical composition comprising the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof. (Point 22) The pharmaceutical composition of item 21, which is an emulsion formulation, an oil-based suspension, a hydrogel formulation or a lipid formulation. ma / i / uazuuy (Point 23) The pharmaceutical composition of point 21, which is an emulsion formulation. (Point 24) The pharmaceutical composition of item 23, wherein the emulsion formulation is a water-in-oil emulsion. (Point 25) The pharmaceutical composition of item 24, wherein the emulsion formulation comprises (1) ethyl oleate, octyldodecyl myristate, sorbitan monooleate, glyceryl monooleate, polyoxyethylene 20 hydrogenated castor oil, glycerin and sodium dihydrogen phosphate, or ( 2) Montanide ISA 51VG. (Point 26) The pharmaceutical composition of item 21, which is a lipid formulation. (Point 27) The pharmaceutical composition of item 26, wherein the lipid formulation is a liposome formulation comprising phospholipids. (Point 28) The pharmaceutical composition of item 26 or 27, wherein the lipid formulation is a liposome formulation comprising sterols. (Point 29) The pharmaceutical composition of item 28, in which the ester is cholesterol (Item 30) The pharmaceutical composition of any of items 27 to 29, wherein the liposome formulation comprises at least one additive selected from the group consisting of inorganic acid, inorganic acid salt, organic acid, organic acid salt, sugars, buffering agent , antioxidant and polymers. (Point 31) μλ / i / uazuuy The pharmaceutical composition of any of items 21 to 30, which further comprises an antigen. (Point 32) The pharmaceutical composition of points 31, wherein the antigen is a pathogen-derived antigen or a tumor antigen. (Point 33) The pharmaceutical composition of item 31, wherein the antigen is a tumor antigen. (Point 34) The pharmaceutical composition of item 33, wherein the tumor antigen is a tumor antigen peptide. (Point 35) The pharmaceutical composition of item 34, wherein the tumor antigen peptide comprises at least one peptide or a pharmaceutically acceptable salt thereof that is selected from the group consisting of the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 1), ALLPAVPSL (SEQ ID NO: 8), SLGEQQYSV (SEQ ID NO: 9), RVPGVAPTL (SEQ ID NO: 10), VLDFAPPGA (SEQ ID NO: 4), CMTWNQMNL (SEQ ID NO: 11), CYTWNQMNL (SEQ ID NO: 2), TYAGCLSQIF (SEQ ID NO: 18), formula (4): CRMFPNAPYL Yo CYTWNQMNL where the bond between C-C is a disulfide bond, and formula (5): ma / iz / zuzi / uazuuy c CYTWNQMNL in which the bond between C-C is a disulfide bond; and at least one peptide or a pharmaceutically acceptable salt thereof which is selected from the group consisting of the following amino acid sequences: WAPVLDFAPPGASAYGSL (SEQ ID NO: 3), CWAPVLDFAPPGASAYGSL (SEQ ID NO: 12), WAPVLDFAPPGASAYGSLC (SEQ ID NO: 13), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 14), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 15), CNKRYFKLSHLQMHSRK (SEQ ID NO: 16), and KRYFKLSHLQMHSRKH (SEQ ID NO: 17). (Point 36) The pharmaceutical composition of item 34, wherein the tumor antigen peptide comprises at least one peptide or a pharmaceutically acceptable salt thereof that is selected from the group consisting of the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 1), ALLPAVPSL (SEQ ID NO: 8), SLGEQQYSV (SEQ ID NO: 9), RVPGVAPTL (SEQ ID NO: 10), VLDFAPPGA (SEQ ID NO: 4), CMTWNQMNL (SEQ ID NO: 11), CYTWNQMNL (SEQ ID NO: 2), and formula (4) : CRMFPNAPYL Yo CYTWNQMNL wherein the C-C bond is a disulfide bond, and at least one peptide or a pharmaceutically acceptable salt thereof that is selected from the group consisting of the following amino acid sequences: WAPVLDFAPPGASAYGSL (SEQ ID NO: 3), ma / i / uazuuy CWAPVLDFAPPGASAYGSL (SEQ ID NO: 12), WAPVLDFAPPGASAYGSLC (SEQ ID NO: 13), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 14), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 15), CNKRYFKLSHLQMHSRK (SEQ ID NO: 16), and KRYFKLSHLQMHSRKH (SEQ ID NOT: 17). (Point 37) The pharmaceutical composition of item 34, wherein the tumor antigen peptide is a combination of a peptide represented by the amino acid sequence of formula (4): CRMFPNAPYL I CYTWNQMNL where the bond between C-C is a disulfide bond, or a pharmaceutically acceptable salt thereof, and a peptide represented by the amino acid sequence of SEQ ID NO 3: WAPVLDFAPPGASAYGSL, or a pharmaceutically acceptable salt thereof. (Point 38) A vaccine adjuvant comprising the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof. (Point 39) The vaccine adjuvant from point 38, which is a vaccine adjuvant for the cancer vaccine. (Point 40) The compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof, which is used as a vaccine adjuvant. (Point 41) The compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof, which is used as a vaccine adjuvant for cancer vaccine. ma / / uazuuy (Point 42) A CTL inducer comprising the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof. (Point 43) An immunostimulant comprising the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof. (Point 44) A method of inducing CTL in mammals, comprising administering the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof to the mammal. (Point 45) A method of enhancing CTL induction in mammals, comprising administering the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof to the mammal. (Point 46) A method of enhancing the specific immune response in mammals to an antigen, comprising administering the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof to the mammal. (Point 47) Use of the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof in the preparation of a vaccine adjuvant. (Point 48) Use of the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof in the preparation of a vaccine adjuvant for cancer vaccine. (Point 49) A kit that includes a) the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising the compound of any of items 1 to 20 or a pharmaceutically acceptable salt thereof; and MA / I / UUZUUU b) an antigen or a pharmaceutical composition comprising an antigen. (Point 50) A kit that includes a) the compound of point 1 or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising the compound of point 1 or a pharmaceutically acceptable salt thereof; and b) a tumor antigen or a pharmaceutical composition comprising a tumor antigen. (Point 51) A kit that includes a) the compound of point 1 or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising the compound of point 1 or a pharmaceutically acceptable salt thereof; and b) a pathogen-derived antigen or a pharmaceutical composition comprising a pathogen-derived antigen. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows the results of test 3, that is, the compound of formula 4 and the peptide SEQ ID NO: 3 were mixed with Montanide ISA 51 VG to prepare a cocktail vaccine, the compound prepared in example 1 or the Reference Example 12 was added to the vaccine cocktail to prepare a vaccine, and the induction of CTL in vivo for SEQ ID NO: 2 by the prepared vaccine was tested in the IFNγ ELISPOT assay with an HLA-A transgenic mouse *24:02. The results are shown in figure 1. Figure 2 shows the results of test 5, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine comprising the compound of formula 4 and the peptide SEQ ID NO: 3 with Montanide ISA 51 VG , and the vaccine was administered to the mouse; Seven days before tumor transplantation of MCA-A24 / Kb-WT1 tumor cells into an HLA-A*24:02 transgenic mouse and seven days after transplantation, the vaccine was administered to the mouse; and TJ days after transplantation, tumor volume was measured. The results are shown in figure 2. Figure 3 shows the results of test 6, that is, a vaccine was prepared by adding the compound prepared in example 1 to a vaccine comprising the peptide of SEQ ID NO: 6 and Montanide ISA 51 VG; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 6 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The ma / i / uazuuy results are shown in Figure 3. Figure 4 shows the results of test 7, that is, a vaccine was prepared by adding the compound prepared in example 1 to a vaccine comprising the peptide of SEQ ID NO: 5 and Montanide ISA 51 VG; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 5 with an HLA-A'02:01 transgenic mouse using the IFNy ELISPOT assay. The results are shown in figure 4. Figure 5 shows the results of test 8, that is, a vaccine was prepared by adding the compound prepared in example 1 to a vaccine comprising the peptide of SEQ ID NO: 18 and Montanide ISA 51 VG; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 18 with an HLA-A*24:02 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 5. Figure 6 shows the results of test 9, that is, a vaccine was prepared by adding the compound prepared in example 8, 9 or 10 or the compound prepared in reference example 12 to a cocktail vaccine comprising the compound of formula 4 and the peptide SEQ ID NO: 3 with Montanide ISA 51 VG; and each vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNy ELISPOT assay. The results are shown in figure 6. Figure 7 shows the results of test 9, that is, a vaccine was prepared by adding the compound prepared in example 8, 9 or 10 or the compound prepared in reference example 12 to a cocktail vaccine comprising the compound of formula 4 and the peptide SEQ ID NO: 3 with Montanide ISA 51 VG; and each vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A'02:01 transgenic mouse using the IFNy ELISPOT assay. The results are shown in figure 7. Figure 8 shows the results of test 10, that is, a vaccine was prepared by adding the compound prepared in the example to a cocktail vaccine comprising the compound of formula 4 and the peptide SEQ ID NO: 3 with Montanide ISA 51 VG; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 8. Figure 9 shows the results of test 10, that is, a vaccine was prepared by adding the compound prepared in the example to a cocktail vaccine comprising the compound of formula 4 and the peptide SEQ ID NO: 3 with Montanide ISA 51 VG; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 9. Figure 10 shows the results of test 11, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (emulsified composition 1) ma / i / uazuuy comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 10. Figure 11 shows the results of test 11, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (emulsified composition 1) comprising the compound of formula 4 and the peptide SEQ ID NO: 3 ; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 11. Figure 12 shows the results of test 12, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (emulsified composition 2) comprising the compound of formula 4 and the peptide SEQ ID NO: 3 ; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 12. Figure 13 shows the results of test 12, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (emulsified composition 2) comprising the compound of formula 4 and the peptide SEQ ID NO: 3 ; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A'02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 13. Figure 14 shows the results of test 13, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (emulsified composition 3) comprising the compound of formula 4 and the peptide SEQ ID NO: 3 ; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 14. Figure 15 shows the results of test 14, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (oil suspension formulation) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 15. Figure 16 shows the results of test 14, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (oil suspension formulation) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 16. Figure 17 shows the results of test 15, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (hydrogel formulation) that ma / i / uazuuy comprises the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 17. Figure 18 shows the results of test 15, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (hydrogel formulation) comprising the compound of formula 4 and the peptide SEQ ID NO: 3 ; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 18. Figure 19 shows the results of test 16, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (liposome formulation 1) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 19. Figure 20 shows the results of test 17, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (liposome formulation 2) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A'02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 20. Figure 21 shows the results of test 17, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (liposome formulation 2) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 4 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 21. Figure 22 shows the results of test 18, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine (liposome formulation 3) comprising the compound of formula 4 and the peptide SEQ ID NO: 3; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLA-A*02:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 22. Figure 23 shows the results of test 19, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine comprising the peptide SEQ ID NO: 1 and the peptide SEQ ID NO: 17 with a composition preliminary emulsified; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 1 with an HLAA*02:01 / HLA-DRBl*01:01 transgenic mouse using the IFNy ELISPOT assay. The results are shown in figure 23. ma / i / uazuuy Figure 24 shows the results of test 19, that is, a vaccine was prepared by adding the compound prepared in example 1 to a cocktail vaccine comprising the peptide SEQ ID NO: 1 and the peptide SEQ ID NO: 17 with a composition preliminary emulsified; and the vaccine was tested on the induction of T helper cells in vivo for SEQ ID NO: 17 with an HLA-A*02:01 / HLA-DRBl*01:01 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 24. Figure 25 shows the results of test 20, that is, a vaccine was prepared by adding the compound prepared in example 1 to a vaccine comprising the compound of formula 5 and a preliminary emulsified composition; and the vaccine was tested for CTL induction in vivo for SEQ ID NO: 2 with an HLA-A*24:02 transgenic mouse using the IFNγ ELISPOT assay. The results are shown in figure 25. Figure 26 shows the results of tests 11-13, that is, a composition comprising the compound of formula 4 and the peptide SEQ ID NO: 3 was emulsified to prepare a cocktail vaccine; The compound prepared in Example 1 was added to the vaccine cocktail to prepare a vaccine; the vaccine was administered to the mouse; and the mouse's spleen was weighed. The results are shown in figure 26. Figure 27 shows the results of tests 14 and 15, that is, a composition comprising the compound of formula 4 and the peptide SEQ ID NO: 3 was suspended in oil base or formulated with hydrogel to prepare each cocktail vaccine ; The compound prepared in Example 1 was added to the vaccine cocktail to prepare each vaccine; the vaccine was administered to the mouse; and the mouse's spleen was weighed. The results are shown in figure 27. Figure 28 shows the results of tests 16-18, that is, a composition comprising the compound of formula 4 and the peptide SEQ ID NO: 3 was formulated in liposomes to prepare a cocktail vaccine; The compound prepared in Example 1 was added to the vaccine cocktail to prepare a vaccine; the vaccine was administered to the mouse; and the mouse's spleen was weighed. The results are shown in figure 28. DETAILED DESCRIPTION OF THE INVENTION Hereinafter, the terms used in this document are explained below. The number of substituents that are subsequently defined as optionally substituted or substituted should not be limited, if they may be substituted. Unless otherwise specified, the definition of each substituent group also extends over the case of partially including the substituent group or the case of the substituent group existing in another substituent group. ma / i / uazuuy The halogen used here includes, for example, fluorine, chlorine, bromine and iodine. Preferably it is fluorine or chlorine, more preferably fluorine. Ci-e alkyl means a straight or branched chain saturated hydrocarbon group having 1 to 6 carbon atoms. Ci-6 alkyl preferably includes CiY' alkyl, more preferably C1-3 alkyl. The term Ci-e alkyl includes, for example, methyl, ethyl, propyl, 1-methylethyl, butyl, 2-methylpropyl, 1-methylpropyl, 1,1-dimethylethyl, pentyl, 3-methylbutyl, 2-methylbutyl, 2, 2-dimethylpropyl, 1-ethylpropyl, 1,1-dimethylpropyl, hexyl, 4-methylpentyl, 3-methylpentyl, 2-methylpentyl, and 1-methylpentyl, and C1-4 alkyl includes examples of Ci-e alkyl always let the number of carbon atoms be 1-4. The term C1-3 alkyl includes examples of Ci-e alkyl as long as the number of carbon atoms is 1 - 3. Ci-e alkoxy means Ci-e alkyloxy, and the Ci-β alkyl moiety is as defined in said Ci-e alkyl. Ci-e alkoxy preferably includes Cu alkoxy, more preferably C1-3 alkoxy. The term Ci-e alkoxy includes, for example, methoxy, ethoxy, propoxy, 1-methylethoxy, butoxy, 2-methylpropoxy, 1-methyl I propoxy, 1,1-dimethylethoxy, pentyloxy, 3-methylbutoxy, 2-methylbutoxy, 2, 2-dimethylpropoxy, l-ethylpropoxy, 1,1-dimethylpropoxy, hexyloxy, 4-methylpentyloxy, 3methylpentyloxy, 2-methylpentyloxy, 1-methylpentyloxy, 3,3-dimethylbutoxy, 2,2-dimethylbutoxy, 1,1-dimethylbutoxy, and 1,2-dimethylbutoxy, and C1-4 alkoxy includes the examples of Ci-e alkoxy as long as the number of carbon atoms is 1-4. C1-3 alkoxy includes the examples of Ci e alkoxy as long as the number of carbon atoms is 1-3. Linker means a bivalent group having two binding sites in the functional group. The bivalent group includes, for example, C1-6 alkylene, C2-7 alkenylene, C27 alkynylene, C310 cycloalkylene, Ce 10 arylene, Cs 10 heteroarylene, ether, amine, carbonyl, ester, amido, carbonate, carbamate, thiocarbamate and thiourea. And, a bivalent group prepared by optionally combining these exemplified bivalent groups may be used herein. The linker preferably includes -O-, -NRY-, -C(O)-, -C(O)O-, -OC(O)-, -C(O)NRY-, -NRYC(O)- , CH2NRy-, -CH2O-, -OC(O)O-, -NR7C(O)O-, -OC(O)NRY-, -NR7C(O)NRY-, -OC(S)NRY-, and - NR7C(S)NRY-, where RY and R7 are as defined in point 9, and more preferably -C(O)NRY- and -CH2NRY-, and more preferably -CH2NRY-. As for the two binding sites in these exemplified linkers, the left binding site is attached to the benzene ring in the compound of formula (1), and the right binding site is attached to Y1 in the compound of formula (1). . Specifically, when the linker L is -CH2NRY-, the compound of formula (1) is represented as the following structure. μλ / 1 / uazuuy μλ / 1 / uazuuy Ci-5 alkylene means a straight or branched chain saturated hydrocarbon group having 1 to 6 carbon atoms. The term Ci-e alkylene includes, for example, methylene, ethylene, propylene, 1-methylethylene, butylene, 2-methylpropylene, 1-methylpropylene, 1,1-dimethylethylene, pentylene, 3-methylbutylene, 2-methylbutylene, 2,2- dimethylpropylene, 1-ethylpropylene, 1,1dimethylpropylene, hexylene, 4-methylpentylene, and 3-methylpentylene, and preferably methylene and ethylene. C2-7 alkenylene means a straight or branched chain unsaturated hydrocarbon group having 2 to 7 carbon atoms and 1 to 3 double bonds. C2-7 alkenylene includes, for example, vinylene, propenylene, methylpropenylene, butenylene, methylbutenylene, pentenylene, hexenylene and heptenylene, and preferably vinylene and propenylene. C2-7 alkynylene means a straight-chain or branched-chain unsaturated hydrocarbon group having 2 to 7 carbon atoms and a triple bond. C2-7 alkynylene includes, for example, ethynylene, propynylene, methylpropynylene, butynylene, methylbutynylene, pentynylene, hexynylene and heptynylene, and preferably ethynylene and propynylene. C3-10 cycloalkylene means cyclic alkylene having 3 to 10 carbon atoms, which may have a bridge structure. C3-10 cycloalkylene includes, for example, cyclopropylene, cyclobutylene, cyclopentylene, cyclohexylene, cycloheptylene, cyclooctylene and adamantylene, and preferably cyclopropylene and cyclobutylene. Ce-ium arylene means an aromatic hydrocarbon group having 6 to 10 carbon atoms. Ce-ium arylene includes, for example, phenylene, 1-naphthylene and 2-naphthylene, and preferably phenylene. C5-10 heteroarylene means 5- to 7-membered monocyclic aromatic heterocycle or 8- to 10-membered bicyclic aromatic heterocycle having 1 to 4 atoms independently selected from the group consisting of a nitrogen atom, an oxygen atom and a of sulfur C5-10 heteroarylene includes, for example, pyridylene, pyridazinilene, isothiazolylene, pyrrolylene, furylene, thienylene, thiazolylene, imidazolylene, pyrimidinylene, thiadiazolylene, pyrazolylene, oxazolylene, isooxazolylene, pyrazinylene, triazolylene, imidazolylene, triadilene, triazolylene, triazolylene, tetrazolylene , indolylene, indazolylene, quinolylene, isoquinolylene, benzofuranilene, benzothienylene, benzooxazolylene, benzothiazolylene, benzoisooxazolylene, benzoisothiazolylene, benzotriazolylene, benzoimidazolylene and 6,ll-dih¡drod¡benzo[b,e]thiepín¡lene. Preferably, it includes pyridylene, pyrimidinylene, quinolylene and isoquinolylene, and more preferably pyridylene, furylene and thienylene. In the present compound of formula (1), preferred The technique of the present invention is not limited to the scope of the compounds listed below. X preferably includes methylene, oxygen atom and NR5 where R5 is a hydrogen atom or Ci-6 alkyl, and more preferably methylene. Y1includes -(CH2CH2O)m-R6. Y2includes -(CH2CH2O)n-R8. R1 preferably includes Ci-e alkyl which may be substituted with the same or different 1-3 Ci-6 alkoxy. More preferably, it includes Ci-6 alkyl such as methyl, ethyl, propyl, 1-methylethyl, butyl, 2-methylpropyl, 1-methylpropyl and 1,1-dimethylethyl, and even more preferably methyl. R2 preferably includes (1) hydrogen atom, and (2) Ci-6 alkyl which may be substituted with 1-3 substituents independently selected from halogen and hydroxy. More preferably, it includes a hydrogen atom and Ci-6 alkyl, more preferably Ci-6 alkyl and even more preferably C3-4 alkyl. R3 preferably includes (1) hydrogen atom, and (2) Ci e alkyl which may be substituted with 1-3 substituents independently selected from halogen and hydroxy. R3 more preferably includes (1) hydrogen atom, and (2) C1-3 alkyl which may be substituted with 1-3 hydroxy. R3 more preferably includes (1) hydrogen atom, and (2) C1-3 alkyl which may be substituted with a hydroxy. R3 more preferably includes (1) hydrogen atom, and (2) Ci-2 alkyl which may be substituted with a hydroxy. R4 preferably includes (1) hydrogen atom, ΜΛ / I / UUZUUU (2) halogen, (3) hydroxy, (4) Ci-6 alkyl which may be substituted with 1 - 3 same or different halogens, (5) Ci-6 alkoxy which may be substituted with 1 - 3 equal or different halogens, and (6) cyano. R4 more preferably includes (1) hydrogen atom, (2) halogen, (3) hydroxy, (4) Ci-6 alkyl which may be substituted with 1 - 3 same or different halogens, and (5) Ci-6 alkoxy which can be substituted with 1 - 3 identical or different halogens. R4 even more preferably includes a hydrogen atom, hydroxy, Ci3 alkyl, and C1-3 alkoxy. R4 even more preferably includes a hydrogen, hydroxy, and methoxy atom, even more preferably hydroxy and methoxy, and more preferably a hydrogen and methoxy atom. R5 preferably includes a hydrogen atom and C1-3 alkyl. More preferably, it includes a hydrogen, methyl, ethyl, and propyl atom. R6 and R8 preferably independently include hydrogen atom, and C1-3 alkyl, more preferably independently a hydrogen atom, methyl, ethyl, and propyl, and more preferably a hydrogen and methyl atom. R7 preferably includes a hydrogen atom and C13 alkyl. More preferably, it includes a hydrogen, methyl, ethyl, and propyl atom. L preferably includes (i) -o-, (2) -NRY-, (3) -C(O)-, (4) -C(O)O-, (5) -OC(O)-, (6 ) -C(O)NRY-, (7) -NRYC(O)-, (8) -CH2NRy-, (9) -CH2O-, (10) -OC(O)O-, ma / t / zuz 1 / uazuuy (11) -NR7C(O)O-, (12) -OC(O)NRY-, (13) -NR7C(O)NRY-, (14) -OC(S)NRY-, and (15) -NR7C(5)NRY-, L more preferably includes (i) -o-, (2) -NRY-, (3) -C(O)-, (4) -C(O)O-, (5) -OC(O)-, ( 6) -C(O)NRY-, (7) -NRYC(O)-, (8) -CH2NRY-, and (9) -CHzO-. L even more preferably includes (1) -C(O)NRY-, (2) -CH2NRY-, (3) -C(O)O-, and (4) -CH2O-. L even more preferably includes (1) -C(O)NRY-, and (2) -CH2NRy-. L more preferably includes -CH2NRY-. The substitution positions of X, L, and R4 on the benzene ring may preferably be as follows (la) or (laa). m a / iz / zuzi / uazuuy RYpreferably includes a hydrogen atom, Ci-6 alkyl, and Y2, more preferably a hydrogen atom and Ci-6 alkyl, even more preferably a hydrogen atom, methyl, ethyl, and propyl. In another embodiment, RY preferably includes a hydrogen atom, Ci6 alkyl, and Y2, and more preferably a hydrogen atom, methyl, and Y2. m and n preferably independently include an integer of 3 - 40, more preferably an integer of 4 - 40, and more preferably an integer of 4 - 36. In another embodiment, m and n independently include an integer of 3 - 40, preferably an integer of 3 - 20, and more preferably an integer of 5 - 20. Preferred compounds of formula (1) include the following compounds or a pharmaceutically acceptable salt thereof. In a preferred embodiment, the present compound of formula (1) includes the following (A). (TO) A compound of formula (1) or a pharmaceutically acceptable salt thereof, wherein X is methylene, oxygen atom, sulfur atom, SO, SO2, or NR5, R1 is Ci-6 alkyl which may be substituted with 1 - 5 substituents independently selected from the group consisting of halogen, hydroxy, and Ci-6 alkoxy, R2 are R3 are independently (1) hydrogen atom, or (2) Ci e alkyl which may be substituted with 1 - 5 substituents independently selected from the group consisting of halogen, hydroxy, and Ci e alkoxy, R4 is (1) hydrogen atom, (2) halogen, (3) hydroxy, (4) Ci-6 alkyl which may be substituted with 1 - 3 same or different halogens, (5) Ci-6 alkoxy which may be substituted with 1 - 3 identical or different halogens, or (6) cyano, R5 is (1) hydrogen atom, or (2) Ci-6 alkyl, R6and R8are independently ma / i / uazuuy (1) hydrogen atom, or (2) Ci-6 alkyl, R7 is (1) hydrogen atom, or (2) Ci-6 alkyl, L is (i) -o-, (2) -NRY -, (3) -C(O)-, (4) -C(O)O-, (5) -OC(O)-, (6) -C(O)NRY-, (7) -NRYC( O)-, (8) -CH2NRy-, (9) -CHzO-, (10) -OC(O)O-, (11) -NR7C(O)O-, (12) -OC(O)NRY- , (13) -NR7C(O)NRY-, (14) -OC(S)NRY-, or (15) -NR7C(S)NRY-, RY is (1) hydrogen atom, (2) Ci alkyl -6, or (3) Y2, Y1 is -(CH2CH2O)m-R6, Y2 is -(CH2CH2O)n-R8, and m and n are independently an integer from 3 -100. In a preferred embodiment, the present compound of formula (1) includes the following (Β). (Β) A compound of formula (1) or a pharmaceutically acceptable salt thereof, wherein different, MA / I / υυζυυυ R2 is (1) hydrogen atom, or (2) Ci-6 alkyl, R3 is (1) hydrogen atom, or (2) Ci-e alkyl which may be substituted with 1 - 3 hydroxy, R4 is (1) hydrogen atom, (2) halogen, (3) hydroxy, (4) Ci-6 alkyl which may be substituted with 1 - 3 same or different halogens, (5) Ci-6 alkoxy which may be substituted with 1 - 3 identical or different halogens, R5 is (1) hydrogen atom, or (2) C1-3 alkyl, R6 and R8 are independently (1) hydrogen atom, or (2) C1-3 alkyl, L is (i) -o-, (2) -NRY-, (3) -C(O)-, (4) -C(O)O-, (5) -OC(O)-, (6) -C(O)NRY-, (7) -NRYC(O)-, (8) -CH2NRY-, or (9) -CH2O-, RYes (1) hydrogen atom, (2) C1-6 alkyl, or (3) Y2, Y1es -(CH2CH2O)m-R6, Y2es -(CH2CH2O)n-R8, and ma / 1 / uazuuy m and n are independently an integer from 3 - 40. In a preferred embodiment, the present compound of formula (1) includes the following (C). ÍQ m a / iz / ¿u¿i / uazuuy A compound of formula (1) or a pharmaceutically acceptable salt thereof, wherein R2 is Ci-6 alkyl, R3 is (1) hydrogen atom, or (2) C1-3 alkyl which may be substituted with a hydroxy, R4 is (1) hydrogen atom (2) hydroxy (3) alkyl C1-3, 0 (4) C1-3 alkoxy, R6 and R8 are independently a hydrogen atom, methyl, ethyl or propyl, L is (1) -C(O)NRY-, (2) -CH2NRY- , (3) -C(O)O-, 0 (4) -CH2O-, RY is a hydrogen atom, methyl, ethyl, propyl, 0 Y2, Y1 is -(CH2CH2O)m-R6, Y2 is -( CH2CH2O)n-R8, and m and n are independently an integer from 3 - 40. In a preferred embodiment, the present compound of formula (1) includes the following (D). (D) A compound of formula (2) or (3) or a pharmaceutically acceptable salt thereof, μλ / 1 / uazuuy where hydroxy, ÍE) R2is Ci-6 alkyl, R3 is a hydrogen atom, or C1-3 alkyl which may be substituted with 1 - 3 R4 is a hydrogen, hydroxy, or methoxy atom, L is -CH2NRy-, -C(O)NRy-, -C(O)O-, or -CH2O-, RYes an atom of hydrogen, methyl, ethyl, propyl, or Y2, Y1es -(CH2CH2O)m-R6, Y2es -(CH2CH2O)n-R8, R6 and R8 are independently a hydrogen, methyl, ethyl, or propyl atom, and m and n are independently an integer from 3 - 40. In another embodiment, the present compound of formula (1) includes the following (E). A compound of formula (2) or a pharmaceutically acceptable salt thereof, wherein R2 is C1-6 alkyl, R3 is a hydrogen atom, or C1-3 alkyl which may be substituted with a hydroxy, R4 is a hydrogen atom, or methoxy, L is -CH2NRY-, RYes an atom of hydrogen, methyl, ethyl, or propyl, Y1es -(CH2CH2O)m-R6, R6 is a hydrogen, methyl, ethyl, or propyl atom, and m is an integer from 4 - 36. The procedures for preparing the compound of the present invention are shown below. For example, the compound of formula (1) or a pharmaceutically acceptable salt thereof can be produced by the following procedures. μλ / 1 / uazuuy Procedure A-l In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (al-2) having a -CRA1RA2NRY- or -CRA1RA2O- linker can be prepared by the following procedure. a1-1 al-2 where R1, R2, R3, R4, R5, Here is a linker prepared in the present procedure. The present procedure is a substitution reaction to replace a leaving group, LGal, with a nucleophile, Nual-Y1. In the present procedure, the compound (al-2) can be obtained by reacting the compound (al-1) and Nu^-Y1 in the presence or absence of a suitable base in a suitable solvent. The leaving group includes, but should not be limited to, preferably fluorine, chlorine, bromine, iodine, methanesulfonyl, ethanesulfonyl and p-toluenesulfonyl, and more preferably chloro, bromo and methanesulfonyl. The nucleophile includes, but should not be limited to, preferably amino which may be substituted with RYdefined in point 9, alcohol and thiol, and more preferably amino which may be substituted with RYdefined in point 9, and alcohol. The base used here may be selected from the bases exemplified below, preferably including sodium hydride and potassium hydride. The solvent used here may be selected from the solvents exemplified below, which preferably includes DMF. The reaction time is generally from about 5 minutes to about 48 hours, and preferably from about 10 minutes to about 24 hours. The reaction temperature is generally from about -78°C to about 100°C, and preferably from about 0°C to about 100°C. ma / i / uazuuy Procedure A-2 In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (a2-2) having a linker of -O-, -NRY-, -C(O)O-, -CH2NRYo -CH2O- can be prepared by the following procedure. Substitution Reaction LGa2—γ1 where R1, R2, R3, R4, R5, The present procedure is a substitution reaction to replace a leaving group, LGa2, with a nucleophile, Nua2. In the present procedure, the compound (a2-2) can be obtained by reacting the compound (a2-l) and LGa2-Y1 in the presence or absence of a suitable base in a suitable solvent. LGa2, Nua2, and La2 are identical to the leaving group, nucleophile, and linker mentioned in procedure A-l, respectively. Each reaction condition of the present procedure complies with procedure A-l. The procedures for preparing the compound of the present invention are shown below. For example, the compound of formula (1) or a pharmaceutically acceptable salt thereof can be produced by the following procedures. Procedure B-l In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (bl-2) having a -CH2NRY- linker can be prepared by the following procedure. ma / i / uazuuy where R1, R2, R3, R4, R5, The present process is a reductive amination with an aldehyde and an amine. In the present procedure, the compound (bl-2) can be obtained by reacting the compound (bl-1) and RY-NH-Y1 in the presence of a suitable reducer in a suitable solvent. The reductant used herein includes, but is not limited to, preferably sodium borohydride, triacetoxyborohydride and picoline borane. The solvent used here may be selected from the solvents exemplified below, preferably including THF and chloroform. The reaction time is generally from about 5 minutes to about 48 hours, and preferably from about 10 minutes to about 24 hours. The reaction temperature is generally from about -78°C to about 100°C, and preferably from about 0°C to about 100°C. Procedure B-2 In compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (b2-2) having a -NRY- or -CH2NRY- linker can be prepared by the following procedure. ma / i / uazuuy where R1, R2, R3, R4, R5, The present process is a reductive amination with an aldehyde and an amine. In the present procedure, the compound (b2-2) can be obtained by reacting the compound (b2-l) and Y1-CHO in the presence of a suitable reductant in a suitable solvent. Each reaction condition of the present procedure complies with procedure B-l. The procedures for preparing the compound of the present invention are shown below. For example, the compound of formula (1) or a pharmaceutically acceptable salt thereof can be produced by the following procedure. Procedure C-l In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (cl-2) having a -O-, -NRY- or -NRYC(O)- linker can be prepared by the following procedure. where R1, R2, R3, R4, R5, The present procedure is a coupling reaction with a leaving group (LGC1) and a nucleophile (Nu^-Y1). In the present procedure, the compound (cl-2) can be obtained by reacting the compound (cl-1) and a nucleophile (Nu^-Y1) in the presence of a suitable catalyst in the presence or absence of a suitable base in a solvent appropriate. The catalyst used herein includes a transition metal such as palladium or a salt thereof, a complex containing it, and one supported by a carrier (for example, supported by a polymer). The leaving group includes, but should not be limited to, preferably boronic acid, boronate, halogen and trifluoromethanesulfonyl, and more preferably boronic acid, boronate, bromine atom, iodine atom and trifluoromethanesulfonate. The nucleophile includes, but should not be limited to, amine that may be substituted with RYdefined in item 9, alcohol, alkylmagnesium, alkylzinc and alkyllithium, and more preferably amine that may be substituted with Ci-6 alkyl and alcohol. The solvent used herein may be selected from the solvents exemplified below, which preferably includes a dioxane-water mixture. The reaction time is generally from about 5 minutes to about 48 hours, and preferably from about 10 minutes to about 24 hours. The reaction temperature is generally from about -78°C to about 100°C, and preferably from about 0°C to about 100°C. The procedures for preparing the compound of the present invention are shown below. For example, the compound of formula (1) or a pharmaceutically acceptable salt thereof can be produced by the following procedures. ma / i / uazuuy Procedure D-l In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (dl-2) having a -C(O)O- linker or -C(O)NRYlinker can be prepared by the following procedure. where R1, R2, R3, R4, R5, X, and Y1 are as defined in point 1, Nudles a nucleophile and Ldles a linker prepared in the present procedure. The present procedure is a condensation reaction with the compound (dl-1) having a carboxylic acid and Nudl-Y1. In the present procedure, the compound (dl-2) can be obtained by reacting the compound (dl-1) and a nucleophile (Nudl-Y1) in the presence of a suitable condensing agent in the presence or absence of a suitable base in a solvent. The nucleophile includes, but should not be limited to, preferably amine that may be substituted with RY defined in point 9, alcohol and thiol, and more preferably amine that may be substituted with a Ci-6 alkyl and alcohol. The condensing agent used here can be selected from conventionally used condensing agents, preferably including HBTU, HATU and l-ethyl-3-(3-dimethylaminopropyl) carbodiimide (including its hydrochloride). . The base used herein may be selected from the bases exemplified below, preferably including tercalkylamine, more preferably DIPEA and triethylamine. The solvent used here may be selected from the solvents exemplified below, preferably including DMF, dichloromethane, chloroform and THF. The reaction time is generally from about 5 minutes to about 48 hours, and preferably from about 10 minutes to about 24 hours. The reaction temperature is generally from about -78°C to about 100°C, and preferably from about 0°C to about 100°C. Procedure D-2 In the compounds according to formula (1) or a pharmaceutically acceptable salt thereof, the compound (d2-2) having a -OC(O)- or -NRYC(O-) linker can be prepared by the following procedure. μλ / i / uazuuy where R1, R2, R3, R4, R5, X, and Y1 are as defined in point 1, Nud2 is a nucleophile and Ld2 is a linker prepared in the present procedure. The present procedure is a condensation reaction with a compound having a carboxylic acid, Y^COOH and the compound (d2-l) having a nucleophile (Nud2). In the present procedure, the compound (d2-2) can be obtained by reacting the compound (d21) having a nucleophile and an electrophile (Y^COOH) in the presence of a suitable condensing agent in the presence or absence of a suitable base in a suitable solvent. Each reaction condition of the present procedure complies with procedure D-l. The starting materials (al-1, a2-l, bl-1, b2-l, cl-1, dl-1 and d2-l) used in processes A to D can be prepared, for example, according to with the processes described in document WO 2009 / 067081. For example, the present compounds according to formula (1) can be prepared by the following procedure. ma / i / uazuuy Procedure E-l e1-4 e1-5 where R1, R2, R3, R4, R5, L, and Y1 are as defined in point 1, LGe and LGe2 are leaving groups and Re is Ci-6 alkyl. The compound (el-1) which is the starting material of step e-1 can be derived as a commercial product or can be prepared according to procedures A to D with the corresponding starting compounds. Steps e-1 to e-4 are similar procedures described, for example, in WO 2009 / 067081. The base used in each step of the above procedures should be appropriately selected based on the reaction, starting compound, etc., which includes alkali bicarbonates such as sodium bicarbonate and potassium bicarbonate; alkali carbonate such as sodium carbonate and potassium carbonate; metal hydrides such as sodium hydride and potassium hydride; alkali metal hydroxides such as sodium hydroxide and potassium hydroxide; alkali metal alkoxides such as sodium methoxide and sodium t-butoxide; organic metal bases such as butyllithium and lithium diisopropylamide; and organic bases such as triethylamine, diisopropylethylamine, pyridine, 4-dimethylaminopyridine (DMAP) and l,8-diazabicyclo[5.4.0]undec-7-ene (DBU). The condensing agent may be that described in Jikken Kagaku Kouza (The Chemical Society of Japan ed., Maruzen) vol 22, which includes, for example, phosphates such as diethyl cyanophosphate and diphenylphosphorylazide; carbodiimides such as l-ethyl-3-(3-dimethylaminopropylj-carbodiimide hydrochloride (WSC'HCI) and dicyclohexylcarbodiimide (DCC); combinations of a disulfide such as 2,2'-dipyridyldisulfide and a phosphine such as triphenylphosphine; phosphorus halides such as N,N'-bis(2-oxo-3-oxazolidin¡l)phosphinic chloride (BOPCI); combinations of an azodicarboxylate diester such as diethyl azodicarboxylate and a phosphine such as triphenylphosphine; 2-halo-l-lower alkylpyridinium such as 2-chloro-l-methylpyridinium iodide; Ι,Γ-carbonyldiimidazole (CDI); diphenylphosphoryl azide (DPPA); diethylphosphoryl cyanide (DEPC); tetrafluoroborates such as 2-(tetrafluoroborate) lH-benzotriazol-l-yl)-l,l,3,3-tetramethyluronium (TBTU) and 2-chloro-l,3-dimethylamidezolidinium tetrafluoroborate (CIB); phosphates such as 2-(lH-benzotriazol-lyl)-l,l,3,3-tetramethyluronium hexafluorophosphate (HBTU), benzotráazol-l-ilox¡tris(dimethylamino)phosphonate or hexafluorophosphate (BOP), benzotriazol-l-yloxytris(pyrrolidinojphosphonium hexafluorophosphate (PYBOP) and 2-(7-aza-lH-benzotráazol-l-íl)-l,l,3,3-tetramethyl hexafluorophosphate luronío (HATU). The solvent used in each step of the above procedures should be appropriately selected based on the reaction, starting compound, etc., including, for example, alcoholic solvents such as methanol, ethanol and isopropanol; ketone solvents such as acetone and methyl ketone; halogenated hydrocarbon solvents such as methylene chloride and chloroform; ether solvents such as tetrahydrofuran (THF) and dioxane; aromatic hydrocarbon solvents such as toluene and benzene; aliphatic hydrocarbon solvents such as hexane and heptane; ester solvents such as ethyl acetate and propyl acetate; amide solvents such as Ν,Ν-dimethylformamide (DMF) and N-methyl-2-pyrrolidone; sulfoxide solvents such as dimethyl sulfoxide (DMSO); nitrile solvents such as acetonitrile; and water. The solvent used here may be one of these solvents or a mixture of two or more solvents selected from these solvents. And, if possible in the reaction, an organic base can be used as the solvent used here. The pharmaceutically acceptable salt includes an acid addition salt and a base addition salt. For example, the acid addition salt includes an inorganic acid salt such as hydrochloride, hydrobromide, sulfate, hydroiodide, nitrate and phosphate; and an organic acid salt such as citrate, oxalate, phthalate, fumarate, maleate, succinate, malate, acetate, formate, propionate, benzoate, trifluoroacetate, methanesulfonate, benzenesulfonate, para-toluenesulfonate and camphorsulfonate; and the base addition salt includes an inorganic base salt such as sodium salt, potassium salt, calcium salt, magnesium salt, barium salt and aluminum salt; and an organic base salt such as trimethylamine, triethylamine, pyridine, picoline, 2,6-lutidine, ethanolamine, diethanolamine, triethanolamine, tromethamine [tr¡s(hydroxy¡methyl)methylamine], tert-butylamine, cyclohexylamine , dicyclohexylamine, and N,Ndibenzylethylamine. Additionally, they include a basic or acidic amino acid salt such as arginine, lysine, ornithine, aspartate and glutamate. Suitable salts of starting compounds or desired compounds, and pharmaceutically acceptable salts are conventional non-toxic salts, which include an acid addition salt such as an organic acid salt (for example, acetate, trifluoroacetate, maleate, fumarate, citrate, tartrate, methanesulfonate, benzenesulfonate, formate, para-toluenesulfonate, etc.) and an inorganic acid salt (for example, hydrochloride, hydrobromide, hydroiodide, sulfate, nitrate, phosphate, etc.); a salt with an amino acid (for example, arginine, aspartate, glutamate, etc.); a metal salt such as an alkali metal salt (for example, sodium salt, potassium salt, etc.) and an alkaline earth metal salt (for example, calcium salt, magnesium salt, etc.); ammonium salt; and an organic base salt (for example, trimethylamine salt, triethylamine salt, pyridine salt, picoline salt, dicyclohexylamine salt, Ν,Ν'-dibenzylethylenediamine salt, etc.); and furthermore, what an experienced person selects appropriately. If it is desirable to fix the compound of the present invention as a salt, when the compound of the present invention is obtained as a salt, it can be purified without further reaction, and when obtained in free form, it can be dissolved or suspended in an organic solvent. appropriate and an acid or a base can be added to form a salt in a general manner. The compound of the present invention or a pharmaceutically acceptable salt thereof may sometimes exist in solvate form with water or various solvents. Said solvates also ma / t / zuz i / uazuuy are included in the present invention. The compound of formula (1) in which one or more Ή atoms are replaced by 2H(D) atoms is also within the scope of the present invention of formula (1). The present invention encompasses the compound of formula (1) or a pharmaceutically acceptable salt thereof. Furthermore, the present invention encompasses a hydrate thereof and a solvate thereof such as ethanolate thereof. Furthermore, the present invention encompasses all tautomers, stereoisomers and crystalline forms thereof. The present compound (1) also includes an optical isomer that is based on the chiral center, an atropisomer that is based on axiality caused by intramolecular rotational hindrance or planar chirality, other stereoisomers, tautomer and geometric isomer, all possible isomers of the which and a mixture thereof are included in the present invention. The mixture of optical isomers of the present compounds can be prepared in a conventional manner. Compounds having an asymmetric structure can be prepared, for example, by using a starting material that has an asymmetric center or by introducing an asymmetric structure anywhere in the process. For example, in the case of optical isomers, the optical isomers can be obtained using an optically active starting material or by resolving a mixture of optical isomers in an appropriate step. In case the compound of formula (1) or its intermediate has a basic functional group, the optical resolution thereof includes, for example, the diastereoisomeric method, where the compound is transformed into a salt thereof by reacting with a optically active acid (for example, a monocarboxylic acid such as mandelic acid, N-benzyloxyalanine and lactic acid; dicarboxylic acid such as tartaric acid, odiisopropylidene tartaric acid and malic acid; or a sulfonic acid such as camphorsulfonic acid and bromocamphorsulfonic acid), in an inert solvent (for example, alcohols such as methanol, ethanol and 2-propanol; an ether solvent such as diethyl ether; an ester solvent such as ethyl acetate; a hydrocarbon solvent such as toluene; an aprotic solvent such as acetonitrile; or a mixture of solvents thereof). In case the compound of formula (1) or its intermediate has an acidic functional group such as carboxyl group, the compound can also be resolved optically after forming its salt with an optically active amine (for example, an organic amine such as 1-phenylethylamine, quinine, quinidine, cinchonidine, cinchonine and strychnine). The present compounds of formula (1) and their intermediates can be isolated and purified in a manner known to a person of ordinary skill. It includes, for example, extraction, partitioning, reprecipitation, column chromatography (e.g., silica gel column chromatography, ion exchange column chromatography, and preparative liquid chromatography), and recrystallization. ma / i / uazuuy The recrystallization solvent used herein includes, for example, an alcohol solvent such as methanol, ethanol and 2-propanol; an ether solvent such as diethyl ether; an ester solvent such as ethyl acetate; an aromatic hydrocarbon solvent such as benzene and toluene; a ketone solvent such as acetone; a halogenated solvent such as dichloromethane and chloroform; a hydrocarbon solvent such as hexane; an aprotic solvent such as dimethylformamide and acetonitrile; water; and a mixed solvent thereof. As other purification methods, for example, the methods described in Jikken Kagaku Kouza (The Chemical Society of Japan ed., Maruzen) vol. 1 can be used. And, the structural determination of the present compounds can be easily carried out by a spectroscopic analytical method such as the nuclear magnetic resonance method, the infrared absorption technique and the analysis of circular dichroism spectra and mass spectrometry, considering the structure of each compound. of departure. Furthermore, each intermediate or final product in the above preparation procedures can also be transformed into another compound of the present invention by appropriately modifying its functional group, especially by extending various side chains of amino, hydroxy, carbonyl, halogen, etc.; and optionally do the aforementioned protection and unprotection if necessary. Modification of the functional group and extension of the side chain can be carried out by a conventional method (for example, see Comprehensive Organic Transformations, R. C. Larock, John Wiley & Sons Inc. (1999), etc.). The temperature for forming a salt is selected from the range of generally -50°C to the boiling point of a solvent used herein, preferably from 0°C to the boiling point and more preferably from room temperature to the boiling point. To improve optical purity, it is desirable to raise the temperature to approximately the boiling point of a solvent used here. When collecting a precipitated crystal on a filter, optional cooling can increase performance. The amount of an optically active acid or amine used herein is suitably about 0.5 - about 2.0 equivalents versus that of the substance compound, preferably about one equivalent. If appropriate, the crystal obtained can be recrystallized from an inert solvent (for example, alcohols such as methanol, ethanol and 2-propanol; an ether solvent such as diethyl ether; an ester solvent such as ethyl acetate; a hydrocarbon solvent such as toluene; an aprotic solvent such as acetonitrile; or a mixture thereof) to obtain its highly pure salt. And, if appropriate, the optically resolved salt can also be treated with an acid or a base to obtain its free form. Among the starting materials and intermediates in each preparation procedure mentioned above, compounds that are not described in each procedure are commercially available or can be prepared by a person having experience with a commercially available material in a known manner or in a similar way to the same. ma / i / uazuuy The present invention provides the compound of formula (1) defined above or a pharmaceutically acceptable salt thereof which is useful as a vaccine adjuvant, preferably vaccine adjuvant for cancer vaccine. Furthermore, the present invention provides a pharmaceutical composition comprising the compound of formula (1) defined above or a pharmaceutically acceptable salt thereof in combination with a pharmaceutically acceptable diluent or carrier (hereinafter referred to as the present pharmaceutical composition). The present compound or a pharmaceutically acceptable salt thereof can be used as an adjuvant to maintain or improve the immunostimulatory of an active ingredient having an immunostimulating activity. That is, the present compound or a pharmaceutically acceptable salt thereof has an activity to induce or potentiate an antigen-specific antibody, specifically antigen-specific IgG, and in more detail Thl-type antigen-specific IgG (e.g., IgG2c). And, the present compound or a pharmaceutically acceptable salt thereof has an activity to increase cytotoxic T lymphocytes (CTL). Or, the present compound or a pharmaceutically acceptable salt thereof has an activity to induce CTL in mammals or enhance the induction of CTL in mammals. And, the present compound or a pharmaceutically acceptable salt thereof has an activity to enhance CD4 positive (i.e., MHC class II restricted) and / or CD8 positive (i.e., MHC class I restricted) T cells. And, the present compound or a pharmaceutically acceptable salt thereof has an activity to increase antigen-specific T cells. And, the present compound or a pharmaceutically acceptable salt thereof has an activity to increase memory T cells, specifically, CD8 positive effector memory T cells. And, the present compound or a pharmaceutically acceptable salt thereof has the character to increase CTL more than the same moles of a compound that does not have a PEG structure when administered to a mammal. And the present compound or a pharmaceutically acceptable salt thereof has activity to activate immunocompetent cells. The present pharmaceutical composition may comprise a tumor antigen. As the tumor antigen, tumor antigen protein or tumor antigen peptide derived from tumor antigen protein can be used. The tumor antigen peptide used herein includes, preferably the antigen peptide mentioned below, more preferably tumor antigen peptide derived from NY-ESO-1, MAGE-3, WT1, OR7C1 and Her2 / neu, and even more preferably tumor antigen peptide tumor antigen derived from WT1. Furthermore, a peptide derived from a neoantigen resulting from a tumor genetic abnormality can also be used with the compound of the present invention or a pharmaceutically acceptable salt thereof. Furthermore, a pharmaceutical composition comprising the present compound or a pharmaceutically acceptable salt thereof and a tumor antigen has an action to inhibit the growth of the tumor expressing the antigen or the appearance of a tumor expressing the antigen. Therefore, the present compound or a pharmaceutically acceptable salt thereof is useful as a medicament for treating or preventing cancer by using it as a pharmaceutical composition in combination with the tumor antigen mentioned below. The tumor antigen peptide used here should not be limited to one in particular, but can be selected from the peptides and the like described in WO 2014 / 157692 or WO 2014 / 157704 Al. In one embodiment of the tumor antigen peptide, it includes, for example, peptides or pharmaceutically acceptable salts thereof of the following amino acid sequences: RMFPNAPYL (SEQ ID NO: 1), ALLPAVPSL (SEQ ID NO: 8), SLGEQQYSV (SEQ ID NO: 9), RVPGVAPTL (SEQ ID NO: 10), VLDFAPPGA (SEQ ID NO: 4), CMTWNQMNL (SEQ ID NO: 11), CYTWNQMNL (SEQ ID NO: 2), WAPVLDFAPPGASAYGSL (SEQ ID NO: 3) , CWAPVLDFAPPGASAYGSL (SEQ ID NO: 12), WAPVLDFAPPGASAYGSLC (SEQ ID NO: 13), CNKRYFKLSHLQMHSRKHTG (SEQ ID NO: 14), CNKRYFKLSHLQMHSRKH (SEQ ID NO: 15), CNKRYFKLSHLQMHSRK (SEQ ID NO: 16), KRYFKLSHLQMHSRKH (SE QID NO: 17) and TYAGCLSQIF (SEQ ID NO: 18). And peptides or pharmaceutically acceptable salts thereof of the following amino acid sequences of formula (4): CRMFPNAPYL I CYTWNQMNL where the bond between C-C is a disulfide bond, and formula (5): c CYTWNQMNL where the bond between C-C is a disulfide bond can be used as a tumor antigen peptide in the present invention. Tumor antigen peptides can be prepared in a general manner used in the peptide chemistry field. Synthetic methods include what is described in a reference (Peptide Synthesis, Interscience, New York, 1966; The Proteins, Vol. 2, Academic Press Inc., New York, 1976), etc. describe. In another embodiment, the pharmaceutical composition of the present invention may include an antigen. The antigen includes an antigen derived from pathogen, for example, a protein derived from virus or bacteria or partial protein thereof. And, a complex of the antigen and the carrier, etc., is included in the scope of the antigen in the present invention. The complex includes an antigen (including, but not limited to, protein and peptide) linked to a protein that is a carrier through a linker that is well known to a person of skill, and an antigen contained in a particle similar to virus (VLP). Therefore, the present compound or a pharmaceutically acceptable salt thereof is useful as a medicament for treating or preventing infection of viruses or bacteria by use in combination with the above-mentioned antigen. Examples of the route of administration of the pharmaceutical composition of the present invention include parenteral administration, specifically intravascular (e.g., intravenous), subcutaneous, intradermal, intramuscular, intratumoral, nodal, and transdermal administrations. In one embodiment, the pharmaceutical composition of the present invention may comprise a compound of formula (1) or a pharmaceutically acceptable salt thereof and a pharmaceutically acceptable diluent or carrier. The drug formulation of the present pharmaceutical composition includes a liquid formulation. The liquid formulation of the present invention includes an aqueous solution formulation / an aqueous suspension formulation, an oily solution formulation / an oily suspension formulation, a hydrogel formulation, a lipid formulation and an emulsion formulation. μλ / i / uazuuy The aqueous solution formulation or the aqueous suspension formulation includes, for example, a formulation prepared by dissolving or dispersing an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof in water. The oily solution formulation or the oily suspension formulation includes, for example, a formulation prepared by dissolving or dispersing an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof in an oily ingredient. The hydrogel formulation includes, for example, a formulation prepared by dissolving or dispersing an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof in water and adding viscosity to the formulation. The lipid formulation includes, for example, a liposome formulation comprising an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof. The emulsion formulation includes, for example, a formulation including an aqueous solution and an oily composition, comprising an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt of the same. In another embodiment of the present liquid formulation, the liquid formulation of the present invention includes, an aqueous solution formulation or an aqueous suspension formulation prepared by dissolving or dispersing a tumor antigen, and / or the compound of formula (1) or a salt pharmaceutically acceptable thereof in water; an oily solution formulation or an oily suspension formulation prepared by dissolving or dispersing a tumor antigen and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof in an oily ingredient; and an emulsion formulation comprising an aqueous solution and an oily composition. The additive used in the present aqueous solution formulation or aqueous suspension formulation includes, for example, purified water, water for injection, a pH regulating agent, a pH adjusting agent, a stabilizer, an isotonizing agent, a solubilizer and a solubilizing agent. The additive used in the present oil solution formulation or oil suspension formulation includes, for example, a pH regulating agent, a pH adjusting agent, a stabilizer, an isotonizing agent, animal or vegetable oil and fat, hydrocarbons, a fatty acid, fatty acid esters, a solubilizer and a solubilizing agent. The additive used in the present hydrogel formulation includes, for example, purified ma / i / uazuuy water, water for injection, a pH regulating agent, a pH adjustment agent, a stabilizer, an isotonizing agent, a solubilizer, a solubilizing agent and a thickener. The additive used in the present liposome formulation includes, for example, purified water, water for injection, a pH regulating agent, a pH adjusting agent, a stabilizer, an isotonizing agent, a solubilizer, a solubilizing agent and lipids. The present emulsion formulation used here includes oil-in-water emulsion (also called O / W emulsion), water-in-oil emulsion (also called W / O emulsion), water-in-oil-in-water emulsion (also known as W / O emulsion / W) and oil-in-water-in-oil emulsion (also known as O / W / O emulsion). The present emulsion formulation preferably includes a water-in-oil emulsion (W / O emulsion). The present emulsion formulation can be prepared by emulsifying an aqueous phase and an oil phase in a general manner. An antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof may be contained in an oil phase and / or an aqueous phase. The additive used in the present emulsion formulation includes, for example, water, a pH-regulating agent, a pH-adjusting agent, a stabilizer, an isotonizing agent, animal or vegetable oil and fat, hydrocarbons, a fatty acid, asters. of fatty acids, glycerol fatty acid esters, a hydrophilic surfactant and a lipophilic surfactant, wherein the water includes purified water and water for injection, the pH regulating agent includes phosphate and organic acid salt, the pH adjusting agent pH includes hydrochloric acid and sodium hydroxide, the stabilizer includes glycerin, propylene glycol and sulfite, the isotonizing agent includes sodium chloride, glucose, sucrose and mannitol, the animal or vegetable oil and fat includes olive oil, soybean oil and soybean oil. liver, hydrocarbon includes liquid paraffin, squalene and squalane, fatty acid includes oleic acid and myristic acid, fatty acid ester includes ethyl oleate, octyldodecyl myristate, cetyl 2-ethylhexanoate and isopropyl myristate, acid ester glycerin fatty acid includes medium chain triglycerides, medium chain diglycerides and medium chain monoglycerides, the hydrophilic surfactant includes polyoxyethylene castor oil, polyoxyethylene hydrogenated castor oil, polyoxyethylenesorbitan fatty acid ester and polysorbates, and the surfactant lipophilic includes glyceryl monooleate, glyceryl dioleate, sorbitan monooleate (Span™ 80), sorbitan sesquioleate, sorbitan dioleate, ma / i / uazuuy sorbitan trioleate (Span™ 85), PEG-30 dipolyhydroxy stearate and surfactant of plant origin (saponin, etc.). The specific composition of additives in the present emulsion formulation used herein includes, but is not limited to, an emulsified composition for dilution described in WO 2006 / 078059, Montanide ISA 51VG (Seppic), Montanide ISA 720 VG (Seppic) and Incomplete Adjuvant Freund's (IFA). The present W / O emulsion formulation includes a preparation comprising the compound of formula (1) or a pharmaceutically acceptable salt thereof, ethyl oleate, octyldodecyl myristate, sorbitan monooleate, glyceryl monooleate, polyoxyethylene hydrogenated castor oil 20, glycerin and sodium dihydrogen phosphate; and a preparation comprising the compound of formula (1) or a pharmaceutically acceptable salt thereof, and Montanide ISA 51 VG. In the liposome formulation of the present invention, liposome means a microvesicle composed of multiple lipid layers, such as a bilayer membrane of amphiphilic lipid molecule (lipid bilayer), having an internal phase. The preferred lipid multilayer is the lipid bilayer. The present liposome formulation includes an amphiphilic lipid molecule. The amphiphilic lipid molecule preferably includes one or more phospholipids. The phospholipid includes, for example, phosphatidylcholine, phosphatidylglycerol, phosphatidic acid, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol and sphingomyelin. The phospholipid preferably includes phosphatidylcholine, phosphatidylglycerol, phosphatidylethanolamine, sphingomyelin and phosphatidylserine. The phospholipid includes, more preferably phosphatidylcholine, sphingomyelin and phosphatidylserine. The fatty acid residue of the phospholipid includes, but is not limited to, saturated or unsaturated Cu-is fatty acid residue, for example, an acyl group derived from a fatty acid such as myristic acid, palmitic acid, stearic acid, oleic, and linoleic acid. And naturally occurring phospholipids, such as egg yolk lecithin and soy lecithin, and the phospholipid whose unsaturated fatty acid residue is hydrogenated, such as hydrogenated egg yolk lecithin and hydrogenated soy lecithin (also called hydrogenated soy phospholipid or hydrogenated soy phosphatidylcholine) can also be used here. The phospholipid content throughout the liposome membrane component (molar fraction) includes, but is not limited to, preferably 30-80%, and more preferably 40-70%. The liposome internally including the present compound may contain sterols. Sterols include cholesterol, β-sitosterol, stigmasterol, campesterol, brassicasterol, ergosterol and fucosterol, and preferably cholesterol. The sterol content throughout the liposome membrane component (molar fraction) includes, but is not limited to, preferably 0-60%, more preferably 10-50%, and even more preferably 30-50%. ma / i / uazuuy The liposome internally including the present compound may contain a polymer modified lipid. Polymer modified lipid means a polymer modified lipid. The polymer-modified lipid is denoted as lipid-polymer. The polymer portion in the polymer-modified lipid is preferably a hydrophilic polymer and more preferably a hydrophilic polymer in which the terminus of the polymer that is not linked to the lipid is alkoxylated. The polymer portion in the polymer-modified lipid is more preferably a hydrophilic polymer wherein the terminus of the polymer that is not attached to the lipid is methoxylated, ethoxylated or propoxylated. The polymer portion in the polymer-modified lipid is more preferably a hydrophilic polymer in which the terminus of the polymer that is not attached to the lipid is methoxylated. The polymeric moiety in the polymer-modified lipid includes, but is not limited to, for example, polyethylene glycol, polypropylene glycol, polyvinyl alcohol, polyvinylpyrrolidone, methoxypolyethylene glycol, methoxypolypropylene glycol, methoxypolyvinyl alcohol, methoxypolyvinylpyrrolidone, ethoxypolyethylene glycol, ethoxypolypropylene glycol, ethoxypolyvinyl alcohol, ethoxypolyvinylpyrrolidone, propoxypolyethylene. glycol, propoxypolypropylene glycol , propoxypolyvinyl alcohol and propoxypolyvinylpyrrolidone. The polymer part in the polymer modified lipid preferably includes polyethylene glycol, methoxypolyethylene glycol, methoxypolypropylene glycol, ethoxypolyethylene glycol, ethoxypolypropylene glycol, propoxypolyethylene glycol and propoxypolypropylene glycol. The polymer part in the polymer modified lipid includes, more preferably, polyethylene glycol, methoxypolyethylene glycol, ethoxypolyethylene glycol, ethoxypolypropylene glycol and propoxypolyethylene glycol. The polymer part in the polymer modified lipid includes, even more preferably, polyethylene glycol and methoxypolyethylene glycol. The polymer portion in the polymer modified lipid most preferably includes methoxypolyethylene glycol. The molecular weight of the polymeric part in polymer modified lipids includes, but is not limited to, for example, 100-10000 daltons, preferably 500-8000 daltons, more preferably 1000-7000 daltons, even more preferably 1500-5000 daltons, and most preferably 1500-3000 daltons. The lipid part of the polymer modified lipid includes, but is not limited to, for example, phosphatidylethanolamine and diacylglycerol. The lipid part of the polymer modified lipid includes, preferably phosphatidylethanolamine having a saturated or unsaturated fatty acid residue of Ci4-is and diacylglycerol having a saturated or unsaturated fatty acid residue of Ci4-is, more preferably phosphatidylethanolamine having a residue of Cw-ie saturated fatty acid and diacylglycerol having a C14-18 saturated fatty acid residue, and even more preferably phosphatidylethanolamine having a palmitoyl group or a stearoyl group and diacylglycerol having a palmitoyl group or a stearoyl group. The lipid portion of the polymer modified lipid most preferably includes distearoylphosphatidylethanolamine. The content of polymer modified lipid throughout the liposome membrane component (molar fraction) includes, but is not limited to, preferably 0-20%, more preferably 1-10% and even more preferably 2-6%. ma / i / uazuuy The liposome internally including the present compound may contain a pharmaceutically acceptable additive. The additive includes, for example, an inorganic acid, an inorganic acid salt, an organic acid, an organic acid salt, sugars, a pH regulating agent, an antioxidant and polymers. Inorganic acid includes, for example, phosphoric acid, hydrochloric acid and sulfuric acid. The inorganic acid salt includes, for example, disodium hydrogen phosphate, sodium chloride, ammonium sulfate and magnesium sulfate. The organic acid includes, for example, citric acid, acetic acid, succinic acid and tartaric acid. The organic acid salt includes, for example, sodium citrate, sodium acetate, disodium succinate and sodium tartrate. Sugar includes, for example, glucose, sucrose, mannitol, sorbitol and trehalose. The pH regulating agent includes, for example, L-arginine, L-histidine, trometamol (trishydroxymethylaminomethane, Tris) and a salt thereof. The antioxidant includes, for example, sodium sulfite, L-cysteine, sodium thioglycolate, sodium thiosulfate, ascorbic acid and tocopheroL. The polymers include, for example, polyvinyl alcohol, polyvinylpyrrolidone, carboxyvinyl polymer and sodium carboxymethyl cellulose. In the present oily suspension formulation, an antigen (tumor antigen or pathogen-derived antigen) and / or the compound of formula (1) or a pharmaceutically acceptable salt thereof may be contained in an oily ingredient, in a solution state or in dispersion state, or in both states. The additive used in the present oil suspension formulation includes, for example, a pH regulating agent, a pH adjusting agent, a stabilizer, an isotonizing agent, animal or vegetable oil and fat, hydrocarbons, a fatty acid, esters of fatty acids, a solubilizer and a solubilizing agent, wherein the pH regulating agent includes phosphate and organic acid salt, the pH adjusting agent includes hydrochloric acid and sodium hydroxide, the stabilizer includes glycerin, propylene glycol and sulfite, the agent isotonizing includes sodium chloride, glucose, sucrose and mannitol, animal or vegetable oil and fat includes olive oil, soybean oil and liver oil, hydrocarbon includes liquid paraffin, squalene and squalane, fatty acid includes oleic acid and acid myristic, fatty acid esters include ethyl oleate, octyldodecyl myristate, cetyl 2-ethylhexanoate, isopropyl myristate, sucrose fatty acid ester, glycerin fatty acid ester, sorbitan fatty acid ester and acid ester propylene glycol fatty acid, the solubilizer or solubilizing agent includes glycerin, propylene glycol, macrogol and ethanol. The present hydrogel formulation includes, for example, a formulation prepared by dissolving or dispersing an antigen (tumor antigen or pathogen-derived antigen) and / or the ΜΛ / I / UUZUUU compound of formula (1) or a pharmaceutically acceptable salt thereof in water and adding viscosity to the formulation. The additive used in the present hydrogel formulation includes, for example, purified water, water for injection, a pH regulating agent, a pH adjusting agent, a stabilizer, an isotonizing agent, a solubilizer, a solubilizing agent and a thickener. , wherein the pH regulating agent includes phosphate and organic acid salt, the pH adjusting agent includes hydrochloric acid and sodium hydroxide, the stabilizer includes glycerin, propylene glycol and sulfite, the isotonizing agent includes sodium chloride, glucose, sucrose and mannitol, the solubilizer or solubilizing agent includes glycerin, propylene glycol, macrogol and ethanol, the thickener includes carmellose sodium, poloxamers and povidones. The compound of formula (1), or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition of the present invention can be used in combination with another additional drug (also called combination drug) in addition to the above tumor antigen. In one embodiment, the compound of formula (1), or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition of the present invention may be administered in combination with an immunomodulator, in addition to the aforementioned tumor antigen. As used herein, the term immunomodulator means any agent that controls the transmission of costimulatory signals generated during the activation of T cells by antigen-presenting cells by interacting with molecules that are involved in the transmission of the costimulatory signals and are present on the cells. antigen presenting and / or T cells, as well as any agent that directly or indirectly controls the function of molecules involved in the establishment of immune tolerance (immunosuppression) in the immune system. Since a tumor antigen peptide is effective in increasing tumor-reactive CTL in a tumor, it is potentially useful as an agent for coadministration with an immunomodulator, to decrease a necessary dose of an immunomodulator or reduce the adverse event caused by an immunomodulator. Therefore, the present disclosure provides, through the use of a WT1 antigen peptide in combination with an immunomodulator, patients with a therapy that has improved efficacy and safety. The immunomodulator may be an agent in the form of an antibody, a nucleic acid, protein, a peptide or small molecules, but is not limited to this. The immunomodulatory antibody includes an antibody fragment. Examples of the antibody fragment include light and heavy chain variable regions of an antibody (VH and VL), F(ab')2, Fab', Fab, ma / i / uazuuy Fv, Fd, sdFv and scFV. Protein as immunomodulator means any protein other than antibodies. Examples of the immunomodulator include, for example, immune checkpoint inhibitors, costimulatory molecule agonists, immune activating agents, and small molecule inhibitors. Immune checkpoint inhibitor inhibits the immunosuppressive effect induced by cancer cells or antigen-presenting cells. Examples of the immune checkpoint inhibitor include, but are not limited to, agents against a molecule selected from the group consisting of: (1) CTLA-4 (e.g., ipilimumab and tremelimumab); (2) PD-1 (e.g., nivolumab, pembrolizumab, AMP-224, AMP-514 (MEDI0680), and pidilizumab (CT011)); (3) LAG-3 (e.g., IMP-321 and BMS-986016); (4) BTLA; (5) KIR (e.g. IPH2101); (6) TIM-3 (e.g., LY3321367 and CA-327); (7) PD-L1 (e.g., durvalumab (MEDI4736), MPDL3280A, BMS-936559, avelumab (MSB0010718C), BMS-1001, BMS-1116, and CA-170,CA-327); (8) PD-L2; (9) B7-H3 (e.g., MGA-271); (10) B7-H4; (11) HVEM; (12) GAL9; (13) CD160; (14) VISTA (e.g., onvatilimab (JNJ-61610588), HMBD-002, and CA-170); (15) BTNL2; (16) TIGIT; (17) PVR; (18) BTN1A1; (19) BTN2A2; (20) BTN3A2 (Nat Rev Drug Discov. 2013; 12: 130-146; Nikkei Medical Cancer Review 2014; 9; Nat Revlmmunol. 2014; 14: 559-69); (21) CSF1-R; (22) VSIG-3; (23) CD112; (24) CD112R; and (25) CD96. The costimulatory molecule agonist enhances the activation of T cells by transmitting an auxiliary signal through a costimulatory molecule on T cells and / or antigen-presenting cells, and attenuates the immunosuppressive effect of cancer cells or antigen presenting cells. Examples of the costimulatory molecule agonist include, but are not limited to, agents against a molecule selected from the group consisting of: (1) 4-1BB; (2) 4-1BB-L; (3) OX40; (4) OX40-L; (5) GITR; (6) CD28; (7) CD40; (8) CD40-L; (9) ICOS; (10) ICOS-L; (11) LIGHT; (12) CD27; and (13) DNAM-1. The immune activating agent effectively stimulates killer T cells in lymph nodes by directly or indirectly activating immune cells such as T cells and dendritic cells. Examples of the immune activating agent include, but are not limited to, Toll-like receptor (TLR) agonists, stimulator of interferon gene (STING) agonists, cytokines, and anti-heat shock protein (HSP) agents. Examples of the Toll-like receptor (TLR) agonist include, but are not limited to, TLR1 / 2 agonists, TLR2 agonists, TLR3 agonists (e.g., Polyl:C), TLR4 agonists (e.g., lipopolysaccharide type S, paclitaxel, lipid A and monophosphoryl lipid A), TLR5 agonists (e.g. flagellin), TLR6 / 2 agonists (e.g. MALP-2), TLR7 agonist, TLR7 / 8 agonists (e.g. gardiquimod, imiquimod, loxoribin, and resiquimod (R848)), TLR7 / 9 agonists (e.g., hydroxychloroquine sulfate), TLR8 agonists (e.g., ma / i / uazuuy Motolimod (VTX-2337)), TLR9 agonists (e.g., CpG-ODN), and TLR11 agonists (e.g., profilin). Examples of the cytokine include, but are not limited to, IL-lo, IL-Ιβ, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL -9, IL-10, IL-11, IL-12, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, interferon (INF)-o, INF-β, INF-γ, SCF, GM-CSF, G-CSF, M-CSF, erythropoietin, macrophage inflammatory protein (MIP), and monocyte chemoattractant protein (MCP). Examples of heat shock protein (HSP) include, but are not limited to, HSP70, HSP90, HSP90o, Η5Ρ90β, HSP105, HSP72 and HSP40. Agents against a heat shock protein include HSP inhibitors. Examples of HSP90 inhibitors include, but are not limited to, tanespimycin (17-AAG), luminespib (AUY-922, NVP-AUY922), alvespimycin hydrochloride (17-DMAG), ganatespib (STA-9090), BIIB021, onalespib (AT13387), geldanamycin, NVP-BEP800, SNX-2112 (PF-04928473), PF-4929113 (SNX-5422), KW-2478, XL888, VER155008, VER-50589, CH5138303, VER-49009, NMS-E973 , PU-H71, HSP990 (NVP-HSP990) and KNK437. Examples of the small molecule inhibitor include, but are not limited to, histone deacetylase inhibitors, histone demethylase inhibitors, histone acetyltransferase inhibitors, histone methyltransferase inhibitors, DNA methyltransferase inhibitors, anthracycline antibiotics, platinum agents, MAPK, β-catenin inhibitors, STAT3 inhibitors, NF-kB inhibitors, JAK inhibitors, mTOR inhibitors, IDO inhibitors, COX-2 inhibitors, CXCR4 inhibitors, and arginase inhibitors. Examples of histone deacetylase inhibitor include, but are not limited to, vorinostat (SAHA, MK0683), entinostat (MS-275), panobinostat (LBH589), trichostatin A (TSA), mocetinostat (MGCD0103), BG45, BRD73954, belinostat (PXD101) (SB939), CUDC-101, M344, PCI34051, dacinostat (LAQ824), tubastatin A hydrochloride, abexinostat (PCI-24781), CLJDC-907, AR42, sodium phenylbutyrate, resminostat, tubacin, quisinostat dihydrochloride (JNJ-26481585) , MC1568, givinostat (ITF2357), droxinostat, chidamide (C S055, HBI-8000), CHR-2485, CHR-3996, DAC-060, FRM-0334 (EVP-0334), MGCD-290, CXD-101 (AZD -9468), CG200745, arginine butyrate, sulforaphane, SHP-141, CUDC-907, YM753 (OBP-801), sodium valproate, apicidin and CI994 (tacedinaline). Examples of the histone demethylase inhibitor include, but are not limited to, GSK J4 HCI, OG-L002, JIB-04, IOX1, SP2509, ORY-1001 (RG-6016), GSK Jl, ML324 and GSK-LSD1 2HCI. Examples of histone acetyltransferase inhibitor include, but are not limited to, C646, MG149, remodelin and anacardic acid. Examples of histone methyltransferase inhibitor include, but are not limited to, pinometostat (EPZ5676), EPZ005678, GSK343, BIX01294, tazemetostat (EPZ6438), 3μλ / i / uazuuy deazaneplanocin A (DZNeP) HCI, UNC1999, MM-102, SGC0946 , entacapone EPZ015666, UNC0379, Eli, MI-2 (menin-MLL inhibitor), MI-3 (menin-MLL inhibitor), PFI-2, GSK126, EPZ04777, BRD4770, GSK-2816126 and UNC0631. Examples of the DNA methyltransferase inhibitor include, but are not limited to, decitabine, azatidine, RG108, thioguanine, zebularine, SGI-110, CC-486, SGI-1027, lomeguatrib and procainamide hydrochloride. The anthracycline antibiotic intercalates between DNA strands to inhibit DNA relaxation. Examples of the antibiotic anthracycline include, but are not limited to, doxorubicin, liposomal doxorubicin, daunorubicin, pirarubicin, epirubicin, idarubicin, aclarubicin, amrubicin, aloin and mitoxantrone. Examples of platinum agents include, but are not limited to, cisplatin, carboplatin, miboplatin, nedaplatin, satraplatin (JM-126), oxaliplatin (ELOXATIN), triplatin tetranitrate and DDS formulations thereof. Examples of MAPK inhibitor include, but are not limited to, SB203580, doramapimod (BIRB796), SB202190 (FHPI), LY2228820, VX-702, SB239063, pexmetinib (ARRY-614), PH-797804, VX-745 and TAK -715. Examples of β-catenin inhibitor include but are not limited to XAV-939, ICG-001, IWR-l-endo, Wnt-C59 (C59), LGK-974, KY02111, IWP-2, IWP-L6 , WIKI4 and FH535. Examples of STAT3 inhibitor include, but are not limited to, S3I-201, static, niclosamide, nifuroxazide, napabucasin (BBI608), cryptotansinone, HO-3867, WHI-P154, FLLL32, STA21, WP1066 and SH-4-54 . Examples of the NF-kB inhibitor include, but are not limited to, QNZ (EVP4593), sodium 4-aminosalicylate, JSH-23, phenethyl caffeate, sodium salicylate, andrographolide and SC75741. Examples of JAK inhibitor include, but are not limited to, ruxolitinib (INCB018424), tofacitinib citrate (CP-690550), AZD1480, fedratinib (SAR302503, TG101348), AT9283, tyrphostin B42 (AG-490), momelotinib (CYT387 ), Tofacitinib (CP-690550, Tasocitinib), WP1066, TG101209, Gandinib 54, XL019, S -ruxolitinib (INCB018424), ZM39923 HCI, decernotinib (VX-509), cerdulatinib (PRT062070, PRT2070), filgotinib (GLPG0634), FLLL32, peficitinib (ASP015K, JNJ-547815632), GLPG0634 analog, Go6976, and Curcumol . Examples of mTOR inhibitor include, but are not limited to, sirolimus (rapamycin), deforolimus (AP23573, MK-8669), everolimus (RAD-001), temsirolimus (CCI-779, NSC683864), zotarolimus (ABT-578) , biolimus A9 (umirolimus), AZD8055, KU-0063794, voxtalisib (XL765, SAR245409), MHY1485, dactolisib (BEZ235, NVP-BEZ235), PI-103 and torkinib (PP242). Examples of IDO inhibitor include, but are not limited to, NLG919, analog INCB024360, indoximod (NLG-8189) and epacadostat (INCB024360). Examples of COX-2 inhibitor include, but are not limited to, valdecoxib, rofecoxib, carprofen, celecoxib, lumiracoxib, tolfenamic acid, nimesulide, niflumic acid, asaraldehyde, lornoxicam, meclofenamate sodium, amfenac sodium hydrate, diclofenac sodium, ketoprofen , ketorolac, naproxen sodium, indomethacin, ibuprofen, aspirin, mefenamic acid, bromfenac sodium, oxaprozin, zaltoprofen and nepafenac. Examples of CXCR4 inhibitor include, but are not limited to, WZ811, plerixafor (AMD3100) and plerixafor 8HCI (AMD3100 8HCI). The compound of formula (1), or a pharmaceutically acceptable salt thereof, or the composition as described herein may also be used in combination with one or more drugs selected from the group consisting of hormonal therapy agent, immunotherapeutic agent, biopharmaceutical, cell growth factor, cell growth factor inhibitor, cell growth factor receptor inhibitor, radiotherapeutic agent, auxiliary agent and chemotherapeutic agent. For example, one to five drugs, one to three drugs or a drug selected from the above group of drugs may be used in combination with the peptide or compound of formula (1), or a pharmaceutically acceptable salt thereof, or a combination thereof as described here. Examples of the hormone therapy agent include adrenal cortical hormone agents (e.g., spheroid anti-inflammatory agents, estrogen preparations, progesterone preparations and androgen preparations), anti-estrogen agents, estrogen control agents, hormone synthesis inhibitors. estrogens, anti-androgen agents, androgen control agents, androgen synthesis inhibitors, LH-RH agonist preparations, LH-RH antagonist preparations, aromatase inhibitors, steroid lactonase inhibitors, birth control pills, retinoids and agents that delay the metabolism of a retinoid. Examples of the hormone therapy agent include fosfestrol, diethylstilbestrol, fluoxymesterol, chlorotrianisene, methyl testosterone, medroxyprogesterone acetate, megestrol acetate, chlormadinone acetate, cyproterone acetate, danazol, allylestrenol, gestrinone, mepartricin, raloxifene, ormeloxifene, levormeloxifene, citrate tamoxifen, toremifene citrate, iodoxifene, pill formulations, mepitiostane, testololactone, aminoglutethimide, goserelin acetate, buserelin, leuprorelin, leuprolide, droloxifene, epithiostanol, ethinyl estradiol sulfonate, estramustine, fadrozole hydrochloride, anastrozole, terorazol, ketoconazole, letrozole l , exemestane, vorozole, formestane, exemestane, flutamide, bicalutamide, nilutamide, enzalutamide, mifepristone, finasteride, dexamethasone, prednisolone, betamethasone, triamcinolone, abiraterone, liarozole, bexarotene and DN101. μλ / i / uazuuy of insulin-like growth (IGF inhibitors), inhibitors of nerve growth factor (NGF inhibitors), inhibitors of brain-derived neurotrophic factor (BDNF inhibitors), inhibitors of endothelial cell growth factor vascular (VEGF inhibitors), colony-stimulating factor inhibitors (CSF inhibitors), platelet-derived growth factor inhibitors (PDGF inhibitors), erythropoietin inhibitors (EPO inhibitors), fibroblast growth factor inhibitors ( FGF inhibitors), hepatocyte growth factor inhibitors (HGF inhibitors), heregulin inhibitors and angiopoietin inhibitors. The term cell growth factor inhibitor is synonymous with the term growth factor inhibitor. Examples of cell growth factor receptor inhibitor include, but are not limited to, epidermal growth factor receptor inhibitors (EGFR inhibitors), insulin-like growth factor receptor inhibitors (IGFR inhibitors), nerve growth factor receptor inhibitors (NGFR inhibitors), brain-derived neurotrophic factor receptor inhibitors (BDNFR inhibitors), vascular endothelial cell growth factor receptor inhibitors (VEGFR inhibitors), stimulating factor inhibitors colony inhibitors (CSF inhibitors), platelet-derived growth factor receptor inhibitors (PDGFR inhibitors), erythropoietin receptor inhibitors (EPOR inhibitors), fibroblast growth factor receptor inhibitors (FGFR inhibitors) , hepatocyte growth factor receptor inhibitors (HGFR inhibitors), heregulin receptor inhibitors, and angiopoietin receptor inhibitors. The term cell growth factor receptor inhibitor is synonymous with the term growth factor receptor inhibitor. Examples of the radiotherapeutic agent include, but are not limited to, radioactive materials and radiosensitizers. Auxiliary agent is an agent used together with an anticancer agent to suppress a side effect or vomiting caused by the anticancer agent. Examples of the auxiliary agent include, but are not limited to, aprepitant, ondansetron, lorazepam, dexamethasone, diphenhydramine, ranitidine, cimetidine, ranitidine, famotidine, cimetidine, Procrit, epoetin alfa, filgrastim, oprelvekin, leucovorin and granulocyte colony-stimulating factor -macrophages (GMCSF). Examples of the chemotherapeutic agent include, but are not limited to, alkylating agents, platinum agents, antimetabolites, topoisomerase inhibitors, DNA intercalators, antimitotic agents, antitumor antibiotics, anticancer agents of plant origin, epigenetic drugs, immunomodulators, molecular targeted drugs , angiogenesis inhibitors and other chemotherapeutic agents. Some typical examples of m a / i / uazuuy chemotherapeutic agents are listed below. Examples of the alkylating agent include, but are not limited to, nitrogen mustard, nitrogen mustard N-oxide hydrochloride, chlorambucil, cyclophosphamide, ifosfamide, thiotepa, carboquone, improsulfan tosylate, busulfan, nimustine hydrochloride, mitobronitol, melphalan, dacarbazine , procarbazine, ranimustine, estramustine sodium phosphate, triethylenemelamine, carmustine, lomustine, streptozocin, pipobroman, etoglucid, altretamine, ambamustine, dibrospidio hydrochloride, fotemustine, prednimustine, bendamustine, uramustine, semustine, pumitepa, ribomustine, temozolomide, treosulfan, trofosfamide, zinostatin estimalamer, adozelesin, cystemustine, bizelesin, mechlorethamine, uracil mustard, streptozocin, trabectedin, becaterin, chlormethine, mannosulfan, triaziquone, procarbazine, kamfosfamide, nitrosoureas and DDS formulations thereof. Examples of platinum agents include, but are not limited to, cisplatin, carboplatin, miboplatin, nedaplatin, satraplatin, oxaliplatin, triplatin tetranitrate and DDS formulations thereof. Examples of the antimetabolite include, but are not limited to, antifolates, pyrimidine metabolism inhibitors, purine metabolism inhibitors, ribonucleotide reductase inhibitors and nucleotide analogs. Examples of the antimetabolite include, but are not limited to, mercaptopurine, 6-mercaptopurine riboside, thioinosine, methotrexate, pemetrexed, eoshitabine, enocitabine, cytarabine, cytarabine ocphosphate, ancitabine hydrochloride, 5-FU agents (e.g., fluorouracil, carzonal, bennan, lunachol, lunapon, tegafur, tegafur-uracil, tegafur-gimeracil-oteracil potassium (TS1), UFT, doxyfluridine, carmofur, gallocitabine, emitfur and capecitabine), aminopterin, nelarabine, leucovorin calcium, tabloid, butocin, folinate calcium, calcium folinate, calcium levofolinate, cladribine, emitfur, fludarabine, gemcitabine, hydroxycarbamide, pentostatin, piritrexim, idoxuridine, mitoguazone, thiazofurin, ambamustine, bendamustine, floxuridine, nelarabine, leucovorin, hydroxyurea, thioguanine, asparaginase, bortezomib, raltitrexed, clofarabine, enocitabine, sapacitabine, azacitidine, sulfadiazine, sulfamethoxazole, trimethoprim, liproxstatin-1, D4476, xanthohumol, epacadostat (INCB024360), vidofludimus, P7C3, GMX1778 (CHS828), NCT-501, SW033291, Ro618048 and DDS formulations thereof . Examples of the topoisomerase inhibitor include, but are not limited to, doxorubicin, daunorubicin, epirubicin, idarubicin, anthracenedione, mitoxantrone, mitomycin C, bleomycin, dactinomycin, plicatomycin, irinotecan, camptothecin, rubitecan, belotecan, etoposide, teniposide, topotecan, amsacrine and DDS formulations thereof. Examples of the DNA intercalator include, but are not limited to, proflavin, doxorubicin (adriamycin), daunorubicin, dactinomycin, thalidomide, and DDS formulations of the same. Examples of the antimitotic agent include, but are not limited to, paclitaxel, paclitaxel derivatives (e.g., DHA paclitaxel, paclitaxel polyglutamate, nab-paclitaxel, micellar paclitaxel, 7a-glucosyloxyacetylpaclitaxel and BMS-275183), docetaxel, vinorelbine vincristine, vinblastine, vindesine, vinzolidine, etoposide, teniposide, ixabepilone, larotaxel, ortataxel, tesetaxel, ispinesib, colchicine, vinflunine and DDS formulations thereof. Examples of the antitumor antibiotic include, but are not limited to, actinomycin D, actinomycin C, mitomycin C, chromomycin A3, mithramycin A, bleomycin hydrochloride, bleomycin sulfate, peplomycin sulfate, daunorubicin hydrochloride, doxorubicin hydrochloride, aclarubicin, piclorubicin hydrochloride, epirubicin hydrochloride, amrubicin hydrochloride, neocarzinostatin, zinostatin estimalamer, mithramycin, sarcomycin, carzinophilin, mitotane, zorubicin hydrochloride, mitoxantrone hydrochloride, darrubicin hydrochloride, liposomal doxorubicin and DDS formulations thereof . Examples of the plant-derived anticancer agent include, but are not limited to, irinotecan, nogitecan, etoposide, etoposide phosphate, eribulin, sobuzoxane, vinblastine sulfate, vincristine sulfate, vindesine sulfate, teniposide, paclitaxel, paclitaxel injection, docetaxel, DJ-927, vinorelbine, topotecan and DDS formulations thereof. Examples of the epigenetic drug include, but are not limited to, DNA methylation inhibitors, histone deacetylase (HDAC) inhibitors, DNA methyl transferase (DNMT) inhibitors, histone deacetylase activators, histone demethylase inhibitors, and methylated nucleotides. Specific examples of the epigenetic drug include, but are not limited to, vorinostat, belinostat, mocetinostat (MGCD0103), entinostat (SNDX-275), romidepsin, azacitidine, decitabine, GSK2879552 2HI, SGC707, ORY-1001 (RG-6016), PFI-4, SirReal2, GSK2801, CPI-360, GSK503, AMI-1, CPI-169 and DDS formulations thereof. Examples of the immunomodulator include, but are not limited to, thalidomide, lenalidomide, pomalidomide and DDS formulations thereof. The molecular targeted drug may be a small molecule or an antibody. Examples of the molecular targeted drug include, but are not limited to, kinase inhibitors, proteasome inhibitors, monoclonal antibodies, mTOR inhibitors, TNF inhibitors, and T cell inhibitors. Examples of the kinase inhibitor include, but are not limited to, tyrosine kinase inhibitors, serine / threonine kinase inhibitors, Raf kinase inhibitors, cyclin-dependent kinase (CDK) inhibitors, and mitogen-activated protein kinase (MEK) inhibitors. ). Specific examples of the kinase inhibitor include, but are not limited to, ma / i / uazuuy imatinib, gefitinib, erlotinib, afatinib, dasatinib, bosutinib, vandetanib, sunitinib, axitinib, pazopanib, lenvatinib, lapatinib, nintedanib, nilotinib, crizotinib, ceritinib, alectinib, ruxolitinib, tofacitinib, ibrutinib, sorafenib, vemurafenib, dabrafenib, palbociclib, trametinib, regorafenib, cedivanib, lestaurtinib, bandetinib, vatalanib, seliciclib, tivantinib, canertinib, pelitinib, tesevatinib, cediranib, motesanib, midostaurin, foretinib, cabozantinib, selumetinib, neratinib, volasertib, saracatinib, enzastaurin, tandutinib, semaxanib, alvocidib, ICR-62, AEE788, PD0325901, PD153035, TK787, amcasertib (BBI503), E6201, E7050 and DDS formulations thereof. Examples of the proteasome inhibitor include, but are not limited to, bortezomib, carfilzomib and DDS formulations thereof. Examples of the monoclonal antibody include, but are not limited to, anti-CD22 antibodies, anti-CD20 antibodies, anti-CD25 antibodies, anti-CD30 antibodies, antiCD33 antibodies, anti-CD5 antibodies, anti-CD52 antibodies, receptor antibodies. anti-epidermal growth factor (EGFR antibodies), anti-vascular endothelial cell growth factor antibodies (VEGF antibodies), anti-TNF-α antibodies, anti-IL-1 receptor antibodies, anti-IL-2 receptor antibodies, anti-IL-5 receptor antibodies, anti-IL-6 receptor antibodies, anti-HER2 antibodies, anti-IgE antibodies, anti-IgG antibodies, anti-RS virus antibodies, anti-CCR4 antibodies, associated antigen 4 antibodies to anti-cytotoxic T lymphocytes (CTLA-4, CD152), anti-PD-1 antibodies, anti-receptor activator of nuclear factor kB ligand (RANKL) antibodies, anti-c-Met antibodies and anti-CXCR4 antibodies. Specific examples of the monoclonal antibody include, but are not limited to, ibritumomab tiuxetan, rituximab, cetuximab, infliximab, basiliximab, brentuximab vedotin, tocilizumab, trastuzumab, bevacizumab, omalizumab, mepolizumab, gemtuzumab, ozogamicin, palivizumab, ranibizumab, certolizumab, ocrelizumab, mogamulizumab, eculizumab, pertuzumab, alemtuzumab, inotuzumab, panitumumab, ofatumumab, golimumab, adalimumab, ramucirumab, nivolumab, anakinra, denosumab, ipilimumab, pembrolizumab, matuzumab, farletuzumab, MORAb-004, MORAb009, and DDS formulations thereof. Examples of mTOR inhibitor include, but are not limited to, everolimus (RAD001), rapamycin (sirolimus), AZD8055, temsirolimus (CCI-779, NSC683864), KU-0063794, voxtalisib (XL-765, SAR245409), MHY1485, dactolisib (BEZ235), PI-103, torkinib (PP242), ridaforolimus (deforolimus, MK-8669), INK-128 (MLN0128), Torinl, omipalisib (GSK2126458, GSK458), OSI-027, PF-04691502, apitolisib (GDC -0980, RG7422), GSK1059615, gedatolisib (PF-05212384, PKI587), WYE-132, PP121, WYE-354, AZD2014, Torin2, WYE-687, CH5132799, WAY-600, ETP-46464, GDC-0349, XL 388 , zotarolimus (ABT-578), tacrolimus (FK506), BGT226 (NVP-BGT226), Palomid 529 (P529), chrysophanic acid and DDS formulations thereof. Examples of the TNF inhibitor include, but are not limited to, etanercept, ma / i / uazuuy lenalidomide (CC-5013), pomalidomide, thalidomide, necrostatin-1 and QNZ (EVP4593). Examples of the T cell inhibitor include, but are not limited to, abatacept. Examples of the angiogenesis inhibitor include, but are not limited to, CM101, IFN-o, IL-12, platelet factor 4, suramin, semaxanib, thrombospondin, VEGFR antagonists, combinations of an angiostatic steroid and heparin, derived angiogenesis inhibitors of cartilage, matrix metalloproteinase inhibitors, batimastat, marimastat, angiostatin, endostatin, 2-methoxyestradiol, tecogalan, thrombospondin, ανβ3 inhibitors, linomide, ADH-1, E7820 and DDS formulations thereof. Examples of the other chemotherapeutic agent include, but are not limited to, finasteride, sobuzoxane, obatoclax, efaproxiral, tipifarnib and lonafarnib. The pharmaceutical composition of the present invention may further contain other additives, and examples of such additives include surfactants, antioxidants, preservatives and soothing agents. The compound of formula (1) or a pharmaceutically acceptable salt thereof can be administered simultaneously with or at any interval before or after the antigenic substance (immunogen) in a unit dose generally ranging from 5 to 5000 mg / m2 of the surface area. body, that is, from approximately 0.1 ng / kg to 100 mg / kg, which provides an effective dose for the vaccine adjuvant. The unit dosage form for injections generally contains, for example, 1 ng to 250 mg of the active ingredient and is preferably used in a dose ranging from 1 ng to 50 mg / kg of the active ingredient per day. However, the daily dose may vary depending on the host to be treated, the route of administration and the severity of the disease to be treated. Thus, the optimal dosage can be determined by a physician treating an individual patient or warm-blooded animal. The term treatment, as used herein, means to relieve some or all of the symptoms of the disease, in whole or in part, or to prevent or delay the progression of the disease. The term prevention, as used here, means primary prevention of the disease (prevention of the onset of the disease) or secondary prevention of the disease (prevention of relapse in a patient whose symptoms have been relieved or the disease has been cured after the onset of the disease, prevention of recurrence). Since the compound of the present invention or a pharmaceutically acceptable salt thereof has immune adjuvant activity in vitro or in vivo, it is useful as a vaccine adjuvant to maintain or improve the immunogenicity of the antigen (tumor antigen or pathogen-derived antigen). The compound of the present invention or a pharmaceutically acceptable salt of ma / i / uazuuy itself has adjuvant activity for cellular immunity in vitro or in vivo and, therefore, is useful as a vaccine adjuvant to maintain or enhance the immunogenicity of the tumor antigen . The compound of the present invention or a pharmaceutically acceptable salt thereof can be used to maintain or enhance the effect of an immunostimulant to treat or prevent a disease, that is, a substance that induces an antigen-specific immune reaction (tumor antigen or antigen derived from pathogen). The pharmaceutical composition comprising the compound of the present invention or a pharmaceutically acceptable salt thereof, and a substance that enhances the immune response specific to the tumor antigen or pathogen (also called tumor antigen or pathogen-derived antigen) is also included in a embodiment of the present invention. The tumor antigen includes, but is not limited to, an antigen protein or an antigen peptide (partial peptide) derived from said antigen protein, a tumor antigen protein or a tumor antigen peptide (partial peptide) derived from said protein of tumor antigen, or a complex thereof with a carrier. In a specific embodiment of the present invention, the present compound or a pharmaceutically acceptable salt thereof can treat or prevent cancer by administration with a tumor antigen protein or a tumor antigen peptide for cancer immunotherapy. Cancer includes, for example, leukemia, myelodysplastic syndrome, multiple myeloma, malignant lymphoma, stomach cancer, colon cancer, lung cancer, breast cancer, germ cell cancer, liver cancer, skin cancer, bladder cancer , prostate cancer, uterine cancer, cervical cancer, ovarian cancer, brain tumor, bone cancer, pancreatic cancer, head and neck cancer, malignant skin or intraorbital melanoma, rectal cancer, anal cancer, testicular cancer, fallopian tube carcinoma, endometrial carcinoma, uterine-cervical carcinoma, vaginal carcinoma, vulvar carcinoma, Hodgkin's disease, non-Hodgkin's lymphoma, esophageal cancer, small intestine cancer, cancer of the endocrine system, thyroid cancer , parathyroid cancer, adrenal cancer, soft tissue sarcoma, urethral cancer, penile cancer, acute myeloid leukemia, chronic myeloid leukemia, acute lymphoblastic leukemia, chronic or acute leukemia including chronic lymphocytic leukemia, childhood solid cancer, lymphocytic lymphoma, kidney / ureter cancer, renal pelvic carcinoma, central nervous system (CNS) tumor, primary CNS lymphoma, tumor angiogenesis, spinal tumor, pontine glioma, pituitary adenoma, Kaposi sarcoma, squamous cell carcinoma, planocellular carcinoma, lymphoma T cells, polytypic glioblastoma, malignant melanoma, non-small cell lung cancer, renal cell cancer and asbestos-induced cancer. Treatment or prevention of cancer includes preventing metastatic disease and tumor recurrence, and preventing and treating paraneoplastic syndrome. In a specific embodiment, the compound of the present invention or a pharmaceutically acceptable μλ / i / uazuuy salt thereof, when administered in combination with an active ingredient of a vaccine for preventing infectious diseases, can prevent various infectious diseases such as genital warts, common warts, plantar warts, hepatitis B, hepatitis C, herpes simplex virus, molluscum contagiosum, smallpox, human immunodeficiency virus (HIV), human papillomavirus (HPV), RS virus, norovirus, cytomegalovirus (CMV), viruses varicella zoster (VZV), rhinovirus, adenovirus, coronavirus, influenza and parainfluenza; bacterial diseases such as tuberculosis, mycobacterium avium and Hansen's disease; infections such as mycosis, chlamydia, Candida, Aspergillus, cryptococcal meningitis, Pneumocystis carini, cryptosporidiosis, histoplasmosis, toxoplasmosis, malaria, trypanosome infection and leishmaniasis. Examples of the active ingredient of the vaccine to prevent infection include, but are not limited to, substances derived from microorganisms / pathogens including bacteria, fungi, protozoa and viruses that cause infectious diseases, such as antigenic protein, antigenic peptide (partial peptide). of said antigenic protein, polysaccharide, lipid and a combination thereof or a combination of the substance derived from said microorganisms / pathogens and a carrier. Examples of the viral antigenic peptide derived from the viral antigen include, but are not limited to, peptide 58-66 of the influenza matrix protein (Jager E et al., Int. J. Cancer 67: 54 (1996) ), HPV16 E7 peptide 86-93 (van Driel WJ et al., Eur. 1 Cancer 35:946 (1999)), HPV E7 peptide 12-20 (Scheibenbogen C et al., J. Immunother 23: 275 (2000) ), HPV16 E7 peptide 11-20 (Smith JWI et al., J. Clin. Oncol. 21: 1562 (2003)), HSV2 gD (Berman PW et al., Science 227: 1490 (1985)), CMV gB ( Frey SE et al., Infect Dis. 180: 1700 (1999), Gonczol E. et al., Exp. Opin. Biol. Ther. 1: 401 (2001)), and CMV pp65 (Rosa CL et al., Blood 100: 3681 (2002), Gonczol E. et al., Exp. Opin. Biol. Ther. 1: 401 (2001)). The carrier, as used herein, is a substance, such as a protein and a lipid, to which an antigenic protein or an antigenic peptide is chemically and / or physically attached, and examples include, but are not limited to , CRM 197 (Vaccine. 2013 Oct 1; 31(42):482733), KLH (Cancer Immunol Immunother. 2003 Oct; 52(10):608-16), virus-like particles (PLoS ONE 5(3): e9809) and liposomes (J Liposome Res. 2004; 14(3-4):175-89). The antigenic protein can be prepared by cloning cDNA, which encodes the antigenic protein, and expressing it in a host cell, according to a textbook such as Molecular Cloning 2aed., Coid Spring Harbor Laboratory Press (1989). The synthesis of the antigenic peptide can be carried out according to a method generally used in peptide chemistry, for example, as described in the literature (Peptide Synthesis, Interscience, New York, 1966; The Proteins, Vol. 2, Academic Press Inc., New York, 1976). ma / t / zuz i / uazuuy In one embodiment, the present invention further provides a kit comprising: a) a compound of formula (1) or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising a compound of formula (1) or a pharmaceutically acceptable salt thereof; and b) an antigen (tumor antigen or pathogen-derived antigen) or a pharmaceutical composition comprising an antigen (tumor antigen or pathogen-derived antigen). The antigen is not limited as long as it is an antigen that can be used as an active ingredient of vaccines, which includes antigenic proteins as mentioned above, antigenic peptides (partial peptides) derived from said antigenic proteins and a complex thereof with a carrier. In one embodiment, the present invention provides a kit comprising: a) a compound of formula (1) or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising a compound of formula (1) or a pharmaceutically acceptable salt thereof; and b) a tumor antigen or a pharmaceutical composition comprising a tumor antigen. The tumor antigen herein should not be limited as long as the tumor antigen can be used as an active ingredient for a cancer vaccine, including the aforementioned tumor antigenic protein or a tumor antigenic peptide (partial peptide) derived from said antigenic protein, and also a complex of the same with a carrier. In one embodiment, the present invention provides a kit comprising: a) a compound of formula (1) or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising a compound of formula (1) or a pharmaceutically acceptable salt thereof; and b) a pathogen-derived antigen or a pharmaceutical composition comprising a pathogen-derived antigen. The pathogen-derived antigen herein should not be limited as long as the pathogen-derived antigen can be used as an active ingredient for an infectious vaccine, including the above-mentioned pathogen-derived antigenic protein or a pathogen-derived antigenic peptide (partial peptide) derived of said antigenic protein derived from a pathogen, and also a complex thereof with a carrier. In one embodiment of the present invention, the present invention provides the use of a compound of formula (1) or a pharmaceutically acceptable salt thereof in the preparation of a vaccine adjuvant. Furthermore, in one embodiment of the present invention, the present invention ma / i / uazuuy provides the use of a compound of formula (1) or a pharmaceutically acceptable salt thereof as a vaccine adjuvant in the preparation of a vaccine for treating cancer or infection. In one embodiment of the present invention, the present invention provides the use of a compound of formula (1) or a pharmaceutically acceptable salt thereof in the preparation of a vaccine adjuvant for a cancer vaccine. Furthermore, in one embodiment of the present invention, the present invention provides the use of a compound of formula (1) or a pharmaceutically acceptable salt thereof as a vaccine adjuvant in the preparation of a cancer vaccine for treating cancer. In one embodiment of the present invention, there is provided the use of a compound of formula (1), or a pharmaceutically acceptable salt thereof, for the manufacture of a vaccine adjuvant for an infection vaccine. In one embodiment of the present invention, there is provided the use of a compound of formula (I) as defined above, or a pharmaceutically acceptable salt thereof, as a vaccine adjuvant in the manufacture of an infection vaccine for the treatment of a infection. Furthermore, one embodiment of the present invention provides a method for treating or preventing cancer or infection, or preventing the progression thereof, comprising a step of administering a compound of formula (I) as defined above, or a pharmaceutically acceptable salt, together with an antigen (tumor antigen or pathogen-derived antigen), to a patient. One embodiment of the present invention provides a method for the treatment or prevention of cancer, or the prevention of the progression thereof, comprising a step of administering a compound of formula (I) as defined above, or a pharmaceutically acceptable salt of the itself, along with a tumor antigen, to a patient. One embodiment of the present invention provides a method for treating or preventing infection, or preventing the progression thereof, comprising a step of administering a compound of formula (I) as defined above, or a pharmaceutical salt acceptable thereof, together with a pathogen-derived antigen, to a patient. EXAMPLES The present invention will be further described with reference to the following examples which should not be considered limiting in any respect. Fmoc: 9-fluorenylmethyloxycarbonyl Boc: tert-butoxycarbonyl ma / i / uazuuy Alko: p-alkoxybenzyl PEG: polyethylene glycol tBu: tere-butyl HBTU: O-(benzotrazol-l-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate DIPEA: Ν,Ν-diisopropylethylamine DMF: N,N-dimethylformamide TFA: trifluoroacetic acid TIS: triisopropylsilane THF: tetrahydrofuran TBS: tert-butyldimethylsilyl group TBDPS: tert-butyldiphenylsilyl group High-performance liquid chromatography mass spectrometer (LCEM) analysis conditions are shown below. Condition A LCEM EM Detector: LCMS-IT-TOF HPLC: Shimadzu Nexera X2 LC 30AD Column: Kinetex 1.7 μ C18 100A New column 50 x 2.1 mm Flow rate: 1.2ml / min Wavelength: 254 / 220nm Mobile phase: A: 0.1% formic acid / water B: acetonitrile Time schedule: Step Time (min) ma / i / uazuuy 1 0.01-1.40 A:B = 90:10 - 5:95 2 1.40-1.60 A:B = 5:95 3 1.61-2.00 A:B = 99:1 Condition B LCEM EM Detector: ACQUITY™ SQ Detector (Waters) HPLC: ACQUITY™ System Column: Waters ACQUITY™ UPLC BEH C18 (1.7 pm, 2.1 mm x 30 mm) Flow rate: 0.8ml / min Wavelength: 254 / 220nm Mobile phase: A: 0.06% formic acid / acetonitrile B: 0.06% formic acid / water Time program: 0.0-1.30 A:B - 2:98 - 96:4 Column temperature: 25°C REFERENCE EXAMPLE 1 Synthesis of a peptide consisting of an amino acid sequence: RMFPNAPYL fArqMet-Phe-Pro-Asn-Ala-Pro-Tvr-Leu') (SEO ID NO: 11 Starting from 1.00 g of (Fmoc-Lys(Boc)-Alko-PEG Resin) (WATANABE CHEMICAL INDUSTRIES, LTD.; 0.23 mmol / g, 0.23 mmol) as a starting material, the peptide chain was elongated by phase synthesis solid of the Fmoc / tBu method. Solid-phase synthesis was performed with the CS336X peptide synthesizer (CSBio), and the Fmoc group was deprotected by treatment with 20% piperidine in DMF for 5 minutes or 20 minutes. Coupling of the protected amino acid to the resin composite was performed by reacting the resin composite with a solution of 1.05 mmol of the protected amino acid, 1 mmol of HBTU, and 2 mmol of DIPEA in DMF for one hour. The obtained resin was washed with DMF and ether and dried under vacuum to give a peptide resin. 10 ml of a TFA / water / TIS mixture (volume ratio: 94 / 2.5 / 2.5) was added to the peptide resin and the mixture was stirred at room temperature for 2 hours. The resin was removed by filtration and the reaction solution was concentrated under reduced pressure. The reaction solution was cooled to ice temperature and diethyl ether (50 ml) was added. The resulting precipitate was collected on a filter, washed with ether and dried in vacuo to give a crude peptide. The crude peptide obtained was dissolved in a mixture of 20% acetic acid / water and acetonitrile (volume ratio: 1 / 1) and purified according to the condition shown below to give RMFPNAPYL trifluoroacetate (Arg-Met -Phe-Pro-Asn-Ala-Pro-Tyr-Leu) (SEQ ID NO: 1)(0.16 g). The trifluoroacetate obtained was converted into its acetate in a common way, which was evaluated. Mass spectrometry: m / z = 554.73 [M+2H]+2, retention time: 0.82 min (LCEM A condition) Purification condition HPLC System: High Performance HPLC Preparative System (Gilson) Column: YMC ODS-A 3 cmφ x 25 cm, 10 pm Eluate 1: 0.1% TFA / water Eluate 2: 0.035% TFA / acetonitrile Flow rate: 20ml / min MA / i / uazuuu Gradient method: Time (min) Concentration of eluate 2 (%) 0 10 25 50 ma / i / uazuuy According to the method described in Reference Example 1, the peptides shown in Table 1 were prepared as their trifluoroacetate from each corresponding starting material. These compounds were treated as reference examples since they are not found within the present compounds. Reference Example 3 was converted into its acetate in a common manner, which was evaluated as follows. TABLE 1 Reference Example No. SEQ ID NO: Amino acid sequence and structure Condition A LCEM (m / z, retention time (min)) 2 2 CYTWNQMNL 586.7 [M+2H]+2, 0.87 3 3 WAPVLDFAPPGASAYGSL 910.3 [M+ 2H]+2, 0.95 4 4 VLDFAPPGA 884.4 [M-Η]-, 0.75 5 5 VLQELNVTV 507.8 [M+2H]+2, 1.14 6 6 GLYDGMEHL 517.7 [M+2H]+2, 1.12 7 7 KIFGSLAFL 498.2 [M +2H]+2, 1.34 According to the method described in WO 2014 / 157692, the compound shown in Table 2 (in which the C-C bond is a disulfide bond) was prepared as its trifluoroacetate. The compound was treated as a reference example since it is not within the present compounds. TABLE 2 Reference Example No. Formula No. Structure Condition A LCEM (m / z, retention time (min)) 8 4 CRMFPNAPYL 1 CYTWNQMNL 794.60 [M+3H]+3, 0.88 REFERENCE EXAMPLE 9 Preparation of N-2,2,3,3-Dentamethyl-4,7,10,13,16-Dentaoxa-3-silaoctadecane-18-amine OTBS Step 1 EITHER To a solution of 14-amino-3,6,9,12-tetraoxatetradecan-l-ol (1.60 g) which is a known compound in THF (25 ml), triethylamine (4.7 ml) and ethyl trifluoroacetate (2.4 ml) were added. ), and the solution was stirred at room temperature for 2 hours. The reaction solution was concentrated under reduced pressure, and the crude product obtained was purified by silica gel chromatography (mobile phase: chloroform / methanol) to give 2,2,2-trifluoro-N-(14-hydroxy¡-3 ,6,9,12tetraoxatetradecan-l-yl)acetamide (1.00 g). m / z = 334 [M+H]+, Rt = 0.507 (LCEM condition B) Step 2 To a solution of the compound (3.91 g) prepared in Reference Example 10 (step 1) in DMF (20 ml) were added triethylamine (4.90 ml) and tert-butyldimethylchlorosilane (3.54 g), and the solution was stirred at room temperature. for 2 hours. The reaction solution was diluted with ethyl acetate, washed with water and brine, dried over sodium sulfate, filtered, and concentrated under reduced pressure. The crude product obtained was purified by silica gel chromatography (mobile phase: hexane / ethyl acetate) to give 2,2,2-trifluoro-N-(2,2,3,3-tetramethyl-4,7 ,10,13,16-pentaoxa-3silaoctadecan-18-yl)acetamide (3.70 g). m / z = 448 [M+H]+, Rt = 1.153 (LCEM condition B) Step 3 ma / i / uazuuy To a solution of the compound (4.44 g) prepared in Reference Example 10 (step 2) in DMF (20 ml) were added cesium carbonate (6.46 g) and methyl iodide (1.6 g), and the solution was stirred at room temperature for 2 hours. The reaction solution was diluted with ethyl acetate, washed with water and brine, dried over sodium sulfate, filtered, and concentrated under reduced pressure. The crude product obtained was purified by silica gel chromatography (mobile phase: hexane / ethyl acetate) to give 2,2,2-trifluoro-N-methyl-N-(2,2,3,3-tetramet l-4,7,10,13,16-pentaoxa3-silaoctadecan-18-yl)acetamide (3.31 g). m / z = 463 [M+H]+, Rt = 1.210 (LCEM B condition) To a solution of the compound (117 mg) prepared in Reference Example 10 (step 3) in methanol (5 ml) was added potassium carbonate (70 mg), and the solution was stirred at room temperature for 5 hours. The reaction solution was concentrated, and the crude product obtained was purified by silica gel chromatography (mobile phase: chloroform / methanol) to give N2,2,3,3-pentamethyl-4,7,10,13,16- pentaoxa-3-silaoctadecane-18-amine (67 mg). m / z = 366 [M+H+], Rt = 0.718 (LCEM condition B) REFERENCE EXAMPLE 10 Preparation of N,2,2-trimethyl-3,3-diphenyl-4,7,10,13,16-Dentaoxa-3-silaoctadecane-18 amine HN. .EITHER. .EITHER. Or OTBDPS The title compound was prepared according to the procedure of Reference Example 9. m / z = 490 [M+H]+, Rt = 0.953 (LCEM condition B). REFERENCE EXAMPLE 11 Preparation of f3S)-3-fΓ2-amino-5-ff2-methoxy-4-Γfmethylamino')methyl1phenyl·methiΠ-6- The title compound was prepared according to the procedure described in WO 2012 / 066336. m / z = 194 [M+2H]+2, Rt = 0.552 (LCEM condition B) REFERENCE EXAMPLE 12 Preparation of 5-(-Γ2-πΐ6ίοχϊ-4Τ(ηΐ6ίϊΐ3Γηίηο)πιβίϊΙ1ΐ6ηϊΙ>ηΐ6ίίΠ-6-πιβίϊΙ-Ν4pentylpyrimidine-2,4-diamine The title compound was prepared from 5-{[4-(chloromethyl)-2-methoxyphenyl]methyl}6-methyl-N4-pentylpyramidine-2,4-diam which is a known compound according to a reaction and treatment similar to the procedure of example 1. m / z = 179 [M+2H]+2, Rt = 0.475 (LCEM condition B) REFERENCE EXAMPLE 13 Preparation of 3-CΓ2-amino-4-methyl-6-fDentilamino)pyrimidin-5-yl1methyll·-4methoxybenzaldehyde ma / i / uazuuy The title compound was prepared from methyl 3-{[2-amino-4-methyl-6(pentylamino)pyrimidin-5-íl]methyl}-4-methoxybenzoate which is a known compound of according to a reaction and treatment similar to the procedure described in WO 2017 / 061532. m / z = 179 [M+2H]+2, Rt = 0.475 (LCEM condition B) REFERENCE EXAMPLE 14 Preparation of 3-fΓ2-amino-4-methyl-6-fpentylamino)pyrimidin-5-yl1methyll·-4hydroxybenzaldehyde To a solution of Reference Example 13 (104 mg) in dichloromethane (5 ml) was added a solution of boron tribromide in dichloromethane (1.0 M, 0.8 ml) under ice cooling and the solution was stirred at room temperature for 6 hours. . Saturated aqueous sodium bicarbonate was added to the reaction solution. The mixture was extracted with chloroform and the organic layer was dried over sodium sulfate, filtered and concentrated. The crude product obtained was purified by silica gel chromatography (mobile phase: chloroform / methanol) to give the title compound (54 mg). m / z = 329 [M+H]+, Rt = 0.748 (condition B LCEM) ma / i / uazuuy REFERENCE EXAMPLE 15 Preparation of 5-f<2-methoxy-5-Γfmethylamino)methyl1phenyl·meth¡Π-6-methyl-N4pentylpyrimidine-2,4-diamine The title compound was prepared from Reference Example 13 according to a reaction and treatment similar to the procedure of Example 3. m / z = 179 [M+2H]+2, Rt = 0.599 (LCEM condition B) REFERENCE EXAMPLE 16 Preparation of 2-fr2-amino-4-methyl-6-fpentylamino')pyrimidin-5-yl1methyl'>-4rfmethylaminolmethyllphenol The title compound was prepared from Reference Example 14 according to a reaction and treatment similar to the procedure of Example 3. m / z = 173 [M+2H]+2, Rt = 0.562 (LCEM condition B) REFERENCE EXAMPLE 17 N,2,2,3,3-Pentamethyl-4,7,10,13,16,19,22,25,28,31-decaoxa-3-silatritriacontane-33amine ma / i / uazuuy The title compound was prepared according to the procedure of Reference Example). m / z = 587 [M+H]+, Rt = 0.865 (condition B LCEM) REFERENCE EXAMPLE 18 N,2,2,3,3-Pentamethyl4,7.10,13,16.19,22.25,28,31,34.37,40.43.46.49,52.55,58.61.64.67,70,73-tetracosaoxa3-silaDentaheDtacontane-75-amine The title compound was prepared according to the procedure of Reference Example 9. m / z = 402 [M+3H]+3, Rt = 0.946 (LCEM condition B) REFERENCE EXAMPLE 19 N,2,2,3,3-Pentamethyl4,7,10,13,16,19,22,25,28,31,34,37,40,43,46,49,52,55,58,61, 64,67,70,73,76,79,82,85,88, 91,94,97,100,103,106,109-hexatriacontaoxa-3-silahendecahectane-lll-amine HN / ^VTBS \ / 36 The title compound was prepared according to the procedure of Reference Example 9. m / z = 866 [M+2H]+2, Rt = 0.948 (condition B LCEM) ma / 1 / uazuuy EXAMPLE 1 Preparation of l-(4-<Γ2-am¡no-4-methyl-6-ÍDentalam¡no)D¡r¡m¡d¡n-5-¡l1methyl¡ll·-3methoxypheni0-2- methyl-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol' trifluoroacetate To a solution of 5-{[4-(chloromethyl)-2-methoxyphenyl]methyl}-6-methyl-N4-pentylpyrimide2,4-diamine (75 mg) which is a compound Known in acetonitrile (3 ml), Reference Example 9 (76 mg), potassium carbonate (65 mg), and potassium iodide (67 mg) were added, and the solution was stirred at 60°C for 8 hours. The reaction solution was concentrated and purified by reverse phase HPLC as in the case of reference example 1 to give the title compound (96 mg). m / z = 290 [M+2H]+2, Rt = 0.623 (condition B LCEM)XH-NMR (CDCI3): δ 7.34 (s, 1H), 6.92 (d, J = 8.0 Hz, 1H), 6.96 ( d, J = 8.0 Hz, 1H), 6.08 (t, J = 5.6 Hz, 1H), 3.96 (s, 3H), 3.88 (m, 2H), 3.70 (m, 2H), 3.64-3.55 (m, 18H ), 3.47 (s, 1H), 3.34 (dd, J = 6.8, 12 Hz, 2H), 2.81 (s, 3H), 2.47 (s, 3H), 1.49-1.42 (m, 2H), 1.30-1.23 ( m, 2H), 1.211.13 (m, 2H), 0.85 (t, J = 7.2 Hz, 3H) EXAMPLE 2 Prepare 2-ηΐ6ίϊΙ-5,8,11,14-ί6ίΓ3θΧ3-2-3Ζ3ή6Χ3άβ€3η-16ol-trifluoroacetate ma / i / uazuuy The title compound was prepared from (3S)-3-[(2-amino-5-{[4-(chloromethyl)-2methoxyphenyl]methyl}-6-methylpyrimidin-4-yl)amino] hexan-l-ol which is a known compound according to a reaction and treatment similar to the procedure of example 1. m / z = 305 [M+2H]+2, Rt = 0.527 (LCEM condition B) EXAMPLE 3 Preparation of l-f3-tT2-3mino-4-methyl-6-fpentyl3mino)pyrimidín-5-yl1methyl'}-4methoxyphenin-2-methyl-5.8,11.14-tetraoxa-2-azahexadecan- 16-oltrifluoroacetate N.H. To a solution of Reference Example 13 (64.3 mg) in THF (5 ml) were added Reference Example 9 (101 mg), acetic acid (5.4 μΙ), and triacetoxyborohydride (199 mg), and the solution was stirred at temperature environment for 24 hours. Water was added to the reaction solution and saturated aqueous sodium bicarbonate was added to neutralize the solution. The mixture was extracted with ethyl acetate. The organic layer was washed with brine, dried over sodium sulfate, filtered, and concentrated. The crude product obtained was purified by HPLC to give the desired compound protected with TBDPS. The obtained protected compound was dissolved in methanol and the solution was stirred at room temperature for 12 hours. The reaction solution was concentrated and purified by reverse phase HPLC to give the title compound (26 mg). m / z = 290 [M+2H]+2, Rt = 0.661 (condition B LCEM)TH-NMR (CDCh): δ 7.32 (dd, J = 1.6, 8.4 Hz, 1H), 7.13 (d, J = 1.6 Hz, 1H), 6.87 (d, J = 8.4 Hz, 1H), 6.24 (t, J = 4.8 Hz, 1H), 4.26 (m, 2H), 3.86 (s, 3H), 3.81 (m, 2H), 3.64-3.49 (m, 18H), 3.29 (dd, J = 6.8, 12.8 Hz, 2H), 2.70 (s, 3H), 2.43 (s, 3H), 1.44-1.36 (m, 2H), 1.24-1.17 ( m, 2H), 1.13-1.07 (m, 2H), 0.80 (t, J = 7.2 Hz, 3H) μλ / i / uazuuy EXAMPLE 4 Preparation of l-O-TrZ-amino^-methyl-e-fDentilaminolDirimidin-S-illmethyll·^hydroxypheniΠ-2-methyl-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol^trifluoroacetate To a solution of Reference Example 14 (30 mg) in THF (5 ml) were added Reference Example 9 (49 mg), acetic acid (2.6 μΙ), and triacetoxyborohydride (97 mg), and the solution was stirred at room temperature. environment for 24 hours. Water was added to the reaction solution and saturated aqueous sodium bicarbonate was added to neutralize the solution. The mixture was extracted with ethyl acetate. The organic layer was washed with brine, dried over sodium sulfate, filtered, and concentrated. The crude product obtained was purified by HPLC to give the desired compound protected with TBDPS. The obtained protected compound was dissolved in methanol and the solution was stirred at room temperature for 12 hours. The reaction solution was concentrated and purified by reverse phase HPLC to give the title compound (13 mg). m / z = 290 [M+2H]+2, Rt = 0.661 (LCEM B condition) ^-NMR (CDCh): δ 7.30 (t, J = 5.2 Hz, 1H), 7.07 (d, J = 2.0 Hz, 1H), 6.97 (dd, J = 1.6, 8.0 Hz, 1H), 6.89 (d, J = 8.4 Hz, 1H), 4.10 (m, 2H), 3.70 (t, J = 5.6 Hz, 2H), 3.63 ( d, J = 5.6 Hz, 2H), 3.55-3.49 (m, 18H), 3.26 (dd, J = 7.2, 13.2 Hz, 2H), 2.68 (s, 3H), 2.43 (s, 3H), 1.47-1.40 (m, 2Η), 1.24-1.15 (m, 2H), 1.13-1.05 (m, 2H), 0.76 (t, J = 6.8 Hz, 3H) μλ / 1 / uazuuy EXAMPLE 5 Preparation of 4-Γf2-amino-4-<Γf2S)-l-hydroxypentan-2-yl1aminol·-6-methylpyrimidin-5¡HmethylTN-f 20-hydroxy¡-3,6,9.12,15.18-hexaoxaicosan -l-yl)-3-methoxybenzamide either To a solution of 4-[(2-amino-4-{[(2S)-hydroxypentan-2-¡l]amino}-6methyl¡lpirimidín-5-¡l)methyl] acid -3-methoxybenzoic (30 mg) which is a known compound in DMF (1 mL) diisopropylethylamine (25.9 mg), 20-amino-3,6,9,12,15,18-hexaoxaicosan-l were added -ol (31.3 mg), and HATU (33.5 mg), and the solution was stirred at room temperature for 24 hours. Saturated aqueous sodium bicarbonate was added to the reaction solution and the mixture was extracted with a chloroform / methanol mixture (10:1), dried over magnesium sulfate, filtered and concentrated. The crude product obtained was purified by aminosilica gel column chromatography (mobile phase: chloroform / methanol) to give the title compound (28.1 mg). m / z = 683 [M+H]+, Rt = 0.558 (LCEM B condition)1H-NMR (CDCh): δ 7.49 (1H, s), 7.21 (1H, d, J = 7.9 Hz), 7.05 (1H , s),6.95 (1H, d, J = 7.9 Hz), 4.77 (1H, d, J = 6.7 Hz), 4.68 (2H, s), 4.01-3.92 (1H, m), 3.94 (3H, s) , 3.75-3.68 (4H, m), 3.67-3.51 (26H, m), 3.42-3.35 (1H, m), 2.28 (3H, s), 1.45-1.36 (1H, m), 1.29-1.20 (1H, m), 1.16-1.06 (2H, m), 0.80 (3H, t, J = 7.3 Hz). EXAMPLE 6 Preparation of 2,5,8,ll-tetraoxatridecan-13-yl 4-Γf2-amino-4-fΓf2S')-l-hydroxypentan-2-yl1aminol·-6-methylDirimidin-5¡Dmethyl1-3-methoxy¡benzoate To a solution of 4-[(2-amino-4-{[(2S)-hydroxy¡pentan-2-¡l]amino}-6methyl¡lp¡rmád¡n-5-yl acid )methyl]-3-methoxy¡benzoic acid (30 mg) which is a known compound in THF (1.5 mL) 2,5,8, ll-tetraoxatñdecan-13-ol (501 mg), diisopropylethylamine (36.2 mg) were added ), and l-ethH-STS-dimethylaminopropyljcarbodiimide hydrochloride (46.1 mg), and the solution was stirred at 60°C for 10 hours. The reaction solution was purified by silica gel column chromatography (mobile phase: chloroform / methanol) to give the title compound (16.2 mg). m / z = 565 [M+H]+, Rt = 0.665 (LCEM B condition) ^-NMR (CDCh): δ 7.56 (1H, d, J = 7.9 Hz), 7.51 (1H, s), 6.99 (1H , d, J = 7.9 Hz), 6.12 (1H, d, J = 7.9 Hz), 4.41 (2H, t, J = 4.6 Hz), 4.20-4.10 (1H, m), 3.93 (3H, s), 3.86 -3.41 (18H, m), 3.29 (3H, s), 3.02 (1H, q, J = 7.5 Hz), 2.44 (3H, s), 1.50-1.22 (2H, m), 1.12-0.91 (2H, m ), 0.74 (3H, t, J = 7.0 Hz). EXAMPLE 7 Prepared ,4-diam¡na nh2 ma / 1 / uazuuy EITHER. To 2,5,8,ll-tetraoxatridecan-13-ol was added sodium hydride (7.2 mg, content >55%), and the mixture was stirred at room temperature for one hour. 5-{[4-(Chloromethyl)-2methoxyphenyl]methyl}-6-methyl-N4-pentylpyrimidine-2,4-dyamine (20 mg) which is a compound known, was added and the mixture was stirred at 60°C for 3 hours. Water was added to the reaction solution and the mixture was extracted with chloroform, dried over magnesium sulfate, filtered and concentrated. The crude product obtained was purified by silica gel column chromatography (eluent: chloroform / methanol) to give the title compound (6.7 mg). m / z = 536 [M+H]+, Rt = 0.850 (LCEM B condition) ^-NMR (CDCI3): δ 6.88 (1H, s), 6.84 (1H, d, J = 7.3 Hz), 6.78 (1H , d, J = 7.3 Hz), 5.80-5.40 (2H, br), 4.46 (2H, s), 3.86 (3H, s), 3.67-3.46 (19H, m), 3.30 (3H, s), 3.24 ( 2H, td, J = 7.0, 5.5 Hz), 2.35 (3H, s), 1.36 (2H, m), 1.23-1.05 (4H, m), 0.78 (3H, t, J = 7.0 Hz). EXAMPLE 8 Preparation of l-(4-4Γ2-amino-4-methyl-6-(Dentilamino)pyrimidin-5-yl1methyll·-3methoxyphenín-2-methyl-5,8,11,14 ,17,20,23,26,29-nonaoxa-2-azahentriacontan-31-ol ma / 1 / uazuuy nh2 To a mixture of 5-{[4-(chloromet¡I)-2-methoxy¡phen¡l]met¡l}-6-met¡l-N4-pent¡lp¡r¡m¡d¡n2,4 -diamine (40 mg) which is a known compound, reference example 17 (64.6 mg), potassium iodide (36.6 mg) and potassium carbonate (30.5 mg), acetonitrile (1 ml) was added and the mixture was stirred at 80°C for 2 hours. The reaction solution was diluted with chloroform, filtered to remove insoluble matter, and concentrated. Chloroform (1 ml) and TFA (0.1 ml) were added to the residue and the mixture was stirred at room temperature for one hour. The reaction solution was neutralized with aqueous sodium carbonate, extracted with chloroform, dried over magnesium sulfate, filtered and concentrated. The crude product obtained was purified by aminosilica gel column chromatography (mobile phase: chloroform / methanol) to give the title compound (28.4 mg). m / z = 400 [M+2H]+2, Rt = 0.583 (condition B LCEM)1H-NMR (CDCI3): δ 6.86 (1H, s), 6.81 (1H, d, J = 7.9 Hz), 6.73 ( 1H, d, J = 7.9 Hz), 6.00-5.00 (2H, br), 3.85 (3H, s), 3.68 (2H, t, J = 4.6 Hz), 3.63-3.50 (40H, m), 3.44 (2H , s), 3.24 (2H, q, J = 6.5 Hz), 2.54 (2H, t, J = 6.1 Hz), 2.32 (3H, s), 2.19 (3H, s), 1.41-1.34 (2H, m) , 1.23-1.16 (2H, m), 1.13-1.05 (2H, m), 0.78 (3H, t, J = 7.3 Hz). EXAMPLE 9 Preparation of l-f4-fΓ2-amino-4-methyl-6-fpentylamino'>pyrimidin-5-yl1methyll·-3methoxyphenin-2-methyl5.8.11.14.17.20.23.26.29.32.35.38.41.44,47,50, 53.56,59.62.65,68,71-tricosaoxa-2azatriheptacontan-73-ol M A / t / ZUZ I / U9ZUU9 nh2 The title compound (31.6 mg) was prepared from Reference Example 18 (83 mg) according to a reaction similar to the procedure of Example 8. m / z = 708 [M+2H]+2, Rt = 0.672 (LCEM B condition) ^-NMR (CDCb): δ 6.83 (1H, s), 6.79 (1H, d, J = 7.9 Hz), 6.69 ( 1H, d, J = 7.3 Hz), 4.79 (1H, s), 4.56 (2H, s), 3.83 (3H, s), 3.76-3.40 (99H, m), 3.21 (2H, dd, J = 12.5, 7.0 Hz), 2.53 (2H, t, J = 6.1 Hz), 2.24 (3H, s), 2.18 (3H, s), 1.39-1.32 (2H, m), 1.22-1.14 (2H, m), 1.12- 1.04 (2H, m), 0.77 (3H, t, J = 7.0 Hz). EXAMPLE 10 Preparation of l-f4-fΓ2-amino-4-methyl-6-fpentylamino')pyrimidin-5-yl1methyll·-3methoxyphenin-2-methyl5,8,11,14,17,20,23,26,29,32, 35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80,83,86,89, 92,95,98,101,104,107-pentatriacontaoxa-2-azanonahectan-109-ol The title compound (26.3 mg) was prepared from Reference Example 19 (95 mg) according to a reaction similar to the procedure of Example 8. m / z = 487 [M+4H]+4, Rt = 0.693 (condition B LCEM)1H-NMR (CDCh): δ 6.83 (1H, s), 6.79 (1H, d, J = 7.9 Hz), 6.69 ( 1H, d, J = 9.2 Hz), M A / 1 / uazuuu 4.81 (1H, s), 4.60 (2H, s), 3.83 (3H, s), 3.76-3.38 (147H, m), 3.21 (2H, dd, J = 12.5, 7.0 Hz), 2.53 (2H, t, J = 5.8 Hz), 2.24 (3H, s), 2.18 (3H, s), 1.39-1.32 (2H, m), 1.21-1.14 (2H, m), 1.12-1.06 (2H, m), 0.77 (3H , t, J = 7.3 Hz). EXAMPLE 11 Preparation of l2-Γf4- <γ2-amino-4-metil-6-fdentilamino)dirim¡d¡n-5-il1metill·-3metoxifen¡nmetil1-3,6,9,l5,l8,2l-hexaoxa-l2-azatr¡cosan-l,23-diolN The title compound (13.1 mg) was prepared from 3,6,9,15,18,21-hexaoxa-12azatricosan-l,23-diol (40.7 mg) according to a reaction similar to the procedure of example 1. m / z = 349 [M+2H]+2, Rt = 0.554 (LCEM B condition) iH-NMR (CDCh): δ 6.85 (1H, s), 6.79 (1H, d, J = 7.9 Hz), 6.73 ( 1H, d, J = 7.9 Hz), 4.85 (1H, t, J = 5.5 Hz), 4.57 (2H, s), 3.83 (3H, s), 3.68-3.42 (34H, m), 3.21 (2H, td, J = 7.2, 5.3 Hz), 2.67 (4H, t, J = 6.1 Hz), 2.24 (3H, s), 1.41-1.33 (2H, m), 1.23-1.09 (4H, m), 0.78 (3H, t, J = 7.0 Hz). Test 1 Human TLR7 reporter gene assay The HEK293 / SEAPorter™ cell line (Imgenex Corporation) is a stably cotransfected cell line that expresses full-length human TLR7 and the secretory alkaline phosphatase (SEAP) reporter gene under the transcriptional regulation of an NF-κΒ response element. TLR7 expression of the cell line has already been tested by flow cytometry. Transfectants with stable expression were selected using the antibiotic blasticidin and Geneticin. TLR signaling leads to NF-κΒ translocation and promoter activation results in SEAP gene expression. Specific activation of TLR7 was assessed by determining the level of SEAP produced after 24-hour incubation of cells at 37°C with each compound prepared in the examples and reference examples in the presence of 0.1% (v / v) dimethyl sulfoxide (DMSO). v). The human TLR7 activity for the present compound was evaluated by the human TLR7 reporter gene assay, and the results are shown in Tables 3 and 4 as the concentration of compound that produced half the maximum level of SEAP induction (ECso). . ma / i / uazuuy Test 2 Mouse TLR7 reporter gene assay The HEK-Blue™ mTLR7 cell line (Invivogen) is a stably cotransfected cell line that expresses full-length mouse TLR7 and the secretory SEAP reporter gene under the transcriptional regulation of an NF-κΒ response element. The TLR7 expression of the cell line has already been tested by RT-PCR. Transfectants with stable expression were selected using the antibiotic blasticidin and zeocin. TLR signaling leads to NF-κΒ translocation and promoter activation results in SEAP gene expression. The specific activation of TLR7 was evaluated by determining the level of SEAP produced after incubation for 2024 hours of the cells at 37 ° C with each compound prepared in the examples and reference examples in the presence of 0.1% (v / v) DMSO. The mouse TLR7 activity for the present compound was evaluated by the mouse TLR7 reporter gene assay, and the results are shown in Tables 5 and 6 as the compound concentration that produced half-maximal level of SEAP induction. (ECso). TABLE 5 Example No. EC50 (nM) 101.32(1) 28 2 21 TABLE 6 ECso Reference Example No. (nM) 11 2 12 15 μλ / i / uazuuy The results of tests 1 and 2 suggest that the example compounds and the reference example compounds of the present invention can act as agonists of mouse and human TLR7. Test 3 Evaluation of CTL induction in vivo in HLA-A*24:02 transgenic mouse The in vivo adjuvant activity of the compound of example 1 and the compound of reference example 12 was evaluated in the following procedure. To a cocktail vaccine comprising the compound of formula 4 prepared in Reference Example 8 and the peptide of SEQ ID NO: 3 prepared in Reference Example 3 with Montanide ISA 51 V (hereinafter referred to as cocktail vaccine b) was added the compound prepared in example 1 or the compound prepared in reference example 12 respectively to prepare each vaccine. The vaccine was administered to an HLA-A*24:02 transgenic mouse and the adjuvant activity of each vaccine was evaluated by the antigen-specific cytotoxic T lymphocyte (CTL) induction assay method. The CYTWNQMNL (SEQ ID NO: 2) in the compound of formula 4 corresponds to an antigen peptide derived from a WT1 protein restricted by HLA-A'24:02. The HLA-A*24:02 transgenic mouse (C57BL / 6CrHLA-A2402 / Kb) expresses a chimeric HLA of a human MHC (HLA-A*24:02) and a mouse MHC (H-2Kb). The mouse can induce CTL with a peptide that can induce CTL in HLA-A'24:02 positive humans (Int J Cancer. 2002; 100: 565-70). The ability to induce CTL specific for the peptide (SEQ ID NO: 2) was evaluated by the cocktail b vaccine by measuring whether IFNy can be produced after stimulation of mouse splenocytes with the peptide (SEQ ID NO: 2). Furthermore, the character of exerting adjuvant activity in vivo by the compound of example 1 or the compound of reference example 12 was evaluated by comparing the number of CTL induced by the vaccine cocktail b and the number of CTL induced by the vaccine prepared by adding the compound prepared in example 1 or the compound in reference example 12 for vaccine cocktail b, and check the presence or absence of the increase in number. Specifically, the compound of formula 4 and the peptide of SEQ ID NO: 3 were dissolved in DMSO, and then diluted with water for injection to concentrations of compound of formula 4 of 6 mg / ml and peptide of SEQ ID NO: 3 of 4.5 mg / ml. The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG to prepare the vaccine cocktail. b. Mice were injected with cocktail b vaccine intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide of SEQ ID NO: 3 per body. Or, in the step of preparing vaccine cocktail b, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body, and 100 ng of compound prepared in example 1 per body. Or, in the step of preparing vaccine cocktail b, the compound prepared in Reference Example 12 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into the mice intradermally in the area of the tail base in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body, and 69 ng of the compound prepared in reference example 12 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. To detect IFNy-producing splenocytes, an IFNy ELISPOT assay kit was used. In particular, an ELISPOT plate was treated with an anti-mouse IFNy antibody the day before the preparation of splenocyte samples. The next day, the plate was blocked by treatment with RPMI 1640 medium with 10% fetal bovine serum (FBS). To the blocked ELISPOT plate, splenocyte samples from HLA-A*24:02 transgenic mice were added at 2.5 x 105 cells / well. Peptide (SEQ ID NO: 2) in the presence of 0.1% (v / v) DMSO was added to the wells containing splenocytes at a final concentration of 10 pg / ml. The splenocyte added with peptide was incubated overnight at 37°C under a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted on the ImmunoSpot analyzer (C.T.L.). Figure 1 shows the results of the IFNy ELISPOT assay using the HLA-A*24:02 transgenic mouse. The scale on the vertical axis of the graph in Figure 1 indicates the number of cells that produced IFNy in response to stimulation with the added cells. The vaccine administered to the mice is indicated on the horizontal axis. The black bars and white bars in Figure 1 show the results that the splenocyte of the HLA-A'24:02 transgenic mouse was incubated in the presence or absence of the peptide of SEQ ID NO: 2, respectively. Therefore, the difference in cell count between the black bar and the white bar shows the count of IFNy-producing cells specific for the peptide of SEQ ID NO: 2 that was induced in the mouse body by the administration of the vaccine, i.e. CTL count. The white bar counts in Figure 1 were almost imperceptible. It suggests that the mouse splenocyte reacted very little in the absence of the desired peptide. The results of the present test showed that the cocktail b vaccine induced CTL that responded to the peptide of SEQ ID NO: 2 in the HLA-A*24:02 transgenic mouse. And, the CTL counts responding to the peptide of SEQ ID NO: 2 increased when adding the compound prepared in example 1 or the compound prepared in reference example 12 to vaccine cocktail b. Furthermore, the increase in CTL counts was greater in the case of adding the compound prepared in example 1 to the vaccine cocktail b, compared to the case of the compound prepared in reference example 12. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Furthermore, the results also show that the effect of increasing CTL with the compound prepared in example 1 is greater, compared to the case of the compound prepared in reference example 12 which has no PEG structure. Test 4 Evaluation of adjuvant activity in vivo in HLA A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of example 1 and the compound of reference example 12 was evaluated in the following procedure. A cocktail vaccine comprising the compound of formula 4 prepared in Reference Example 8 and the peptide of SEQ ID NO: 3 prepared in Reference Example 3 with a preliminarily emulsified composition (hereinafter referred to as cocktail vaccine a) is added the compound prepared in example 1 or the compound prepared in reference example 12 respectively to prepare each vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of each vaccine was evaluated by the antigen-specific CTL induction test method. Formula 4 compound: CRMFPNAPYL I CYTWNQMNL where the bond between C-C is a disulfide bond. The RMFPNAPYL (SEQ ID NO: 1) in the Compound of formula 4 and VLDFAPPGA (SEQ ID NO: 5) in the peptide of SEQ ID NO: 3 correspond to antigen peptides derived from an HLA-A*02 restricted WT1 protein :01. The HLA-A*02:01 transgenic mouse (C57BL / 6CrHLA-A2.1DRl) lacks mouse MHC and instead expresses a chimeric HLA of a human MHC (HLA-A*02:01) and a human MHC. mouse (H2Db), and HLA-DRBl*01:01. The mouse can evaluate the pharmacological activity of immunotherapeutic agents that include a CTL-inducing peptide in HLA-A'02:01-positive humans (Eur J Immunol. 2, 004; 34: 3, 060-9). The ability to induce CTL specific for the antigenic peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was evaluated by the vaccine by measuring whether IFNy can be produced after stimulation of mouse splenocytes with the corresponding peptide. Furthermore, the nature of exerting adjuvant activity in vivo by the compound of Example 1 or the compound of Reference Example 12 was evaluated by comparing the number of CTL induced by the cocktail vaccine and the number of CTL induced by the vaccine prepared by adding the compound prepared in example 1 or the compound of reference example 12 for vaccine cocktail a, and verifying the presence or absence of the increase in number. Specifically, in vivo adjuvant activity was evaluated as follows. 0.312 g of sodium dihydrogen phosphate dihydrate was dissolved in 80 g of water for injection. 14.0 g of ethyl oleate, 14.0 g of octyldodecyl myristate, 2.0 g of sorbitan monooleate, 2.8 g of glyceryl monooleate, 0.4 g of castor oil hydrogenated with polyoxyethylene 20 and 0.4 g of glycerin were mixed. 2.354 ml of the mixture (corresponding to 2.077 g) was placed in a test tube and 0.396 ml of aqueous sodium dihydrogen phosphate (corresponding to 0.396 g) was gradually added to the test tube that was being shaken with a mixer (ULTRATURRAX TIO , IKA or Touch Mixer MT-51, Yamato Scientific) to emulsify the mixture in the test tube. The emulsion obtained was called preliminary emulsified composition. The preparation amount was adjusted as appropriate. The compound of formula 4 and the peptide of SEQ ID NO: 3 were dissolved in DMSO and then diluted with water for injection to concentrations of compound of formula 4 of 3 mg / ml and peptide of SEQ ID NO: 3 of 2.25 mg / ml. ml. The diluted peptide solution was mixed and emulsified with an equal volume of the above preliminary emulsified composition to prepare vaccine cocktail a. The cocktail vaccine was injected into mice intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide of SEQ ID NO: 3 per body. Or, in the cocktail vaccine preparation step a, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 32.5 ng of compound prepared in example 3 per body. Or, in the cocktail vaccine preparation step a, the compound prepared in Reference Example 12 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the area of the tail base in an amount to administer 300 pg of μλ / i / uazuuy compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 22.5 ng of compound prepared in reference example 12 per body. One week later, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. To detect IFNy-producing splenocytes, an IFNy ELISPOT assay kit was used. In particular, an ELISPOT plate was treated with an anti-mouse IFNy antibody the day before the preparation of splenocyte samples. The next day, the plate was blocked by treatment with RPMI 1640 medium with 10% FBS. To the blocked ELISPOT plate, the prepared splenocyte samples were added at 1.25 x 105 cells / well. Peptide (SEQ ID NO: 1 or SEQ ID NO: 4) in the presence of 0.1% (v / v) DMSO was added to the wells containing splenocytes at a final concentration of 10 pg / ml. The splenocyte added with peptide was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the ELISPOT plate was subjected to treatment for cell staining according to the manufacturer's protocol. Stained spots were counted on the ImmunoSpot analyzer. The results show that the cocktail vaccine comprising the compound of formula 4 and the peptide of SEQ ID NO: 3 induced CTL that responded to the peptide of SEQ ID NO: 1 or SEQ ID NO: 4 in the HLA-A* transgenic mouse 02:01. And, like the result of test 3, the CTL counts responding to the peptide of SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the compound prepared in example 1 to the cocktail vaccine a, compared to the case of the compound prepared in reference example 12. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Furthermore, the results also show that the effect of increasing CTL with the compound prepared in example 1 is greater, compared to the case of the compound prepared in reference example 12 which has no PEG structure. Test 5 Effect to improve the in vivo suppressor effect of the vaccine for the growth of tumor vaccine A suspension of 3-methylcholanthrene in corn oil was administered to an HLA-A*24:02 transgenic mouse intradermally in the ventral region. From the tumor generated at the administration site, tumor cells expressing HLA-A*2402 / Kb were obtained. Established cell lines stably expressing the WT1 antigen peptide (SEQ ID NO: 2) in cells (here, also referred to as MCA-A24 / Kb-WT1 tumor cells) were suspended in Hanks' balanced salt solution and transplanted intradermally to the region. ventral of HLA-A*24:02 transgenic mouse (5 x 105 cells per mouse). Mice prepared to receive a vehicle (group a), a vaccine (group b) or a vaccine containing the compound prepared in example 1 (group c). Six mice per group were used. Seven days before tumor transplantation and seven days after tumor transplantation, for mice in group a, a composition comprising water for injection was emulsified with an equal volume of Montanide ISA 51 VG and the emulsion was administered intradermally to the area from the base of the tail (0.1 ml per administration per mouse). For group b mice, a composition comprising the compound of formula 4 and the peptide of SEQ ID NO: 3 was emulsified with an equal volume of Montanide ISA 51 VG and the emulsion was administered intradermally to the base area. tail (per administration, 300 pg of compound of formula 4 per body and 225 pg of peptide of SEQ ID NO: 3 per body). For mice in group c, a composition comprising the compound of formula 4, peptide of SEQ ID NO: 3, and the compound prepared in Example 2 was emulsified with an equal volume of Montanide ISA 51 VG and the emulsion was administered by intradermally in the tail base area (per administration, 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 100 ng of compound prepared in example 2 per body) . Tumor size was measured 27 days after tumor transplantation and tumor volume was calculated. Figure 2 shows the average tumor volumes of six mice in each group on day T7 after tumor transplantation. The vaccine (group b) significantly suppressed the growth of tumor cells, compared to the vehicle case (group a) (non-parametric Dunnett's multiple test, *: p < 0.05). Furthermore, the vaccine to which the compound prepared in Example 2 was added more potently suppressed the growth of tumor cells (group c, **: p < 0.01). The results show that the preventive effect to suppress tumor growth with a vaccine can be enhanced by adding the present compound to the vaccine. According to the method described in Reference Example 1, the peptide shown in Table 7 was prepared as its trifluoroacetate from the corresponding starting material. These compounds were treated as reference examples since they are not found within the present compounds. ma / i / uazuuy TABLE 7 Reference Example No. SEQ ID NO: Amino acid sequence and structure Condition A LCEM (m / z, retention time (min)) 20 17 KRYFKLSHLQMHSRKH 420.2[M+5H]+5, 0.64 21 18 TYAGCLSQIF 1102.5[M+ H]+, 1,142 min According to the method described in WO 2007 / 063903, the compound shown in Table 8 (where the C-C bond is a disulfide bond) was prepared as its trifluoroacetate. The compound was treated as a reference example since it is not among the present compounds. ma / i / uazuuy TABLE 8 Reference Example No. Formula No. Structure Condition A LCEM (m / z, retention time (min)) 22 5 c CYTWNQMNL 1291.4 [M+H]+, 1.051 min Test 6 Evaluation of adjuvant activity in viw in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine prepared by mixing the peptide SEQ ID NO: 6 prepared in Reference Example 6 with Montanide ISA 51 VG (hereinafter referred to as vaccine c) the compound prepared in Example 1 was added to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. The GLYDGMEHL in the peptide of SEQ ID NO: 6 corresponds to an antigen peptide derived from a MAGE-A10 protein restricted by HLAA'02:01. The ability to induce CTL specific for the antigen peptide (SEQ ID NO: 6) was evaluated by vaccine c by measuring whether IFNγ can be produced upon stimulation of mouse splenocytes with the peptide. Furthermore, the ability to exert adjuvant activity in vivo by the compound of Example 1 was evaluated by comparing the number of CTL induced by vaccine c and the number of CTL induced by the vaccine prepared by adding the compound prepared in Example 1 to the vaccine. c, and check the presence or absence of the increase in number. Specifically, the peptide of SEQ ID NO: 6 was dissolved in DMSO and then diluted with water for injection to concentrations of 0.1 mg / ml. The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG to prepare vaccine c. Vaccine c was injected to mice intradermally in the tail base area in an amount to administer 10 pg of peptide of SEQ ID NO: 6 per body. Or, in vaccine preparation step c, the compound prepared in example 1 was added to the diluted peptide solution to prepare number of CTL induced by the vaccine prepared by adding the compound prepared in example 1 to the vaccine d , and check the presence or absence of the increase in number. Specifically, the peptide of SEQ ID NO: 5 was dissolved in DMSO and then diluted with water for injection to concentrations of 2 mg / ml. The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG for vaccine d. Vaccine d was injected into mice intradermally in the tail base area in an amount to administer 100 pg of peptide of SEQ ID NO: 5 per body. Or, in vaccine preparation step d, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 100 pg of peptide of SEQ ID NO: 5 per body and 330 ng of the compound prepared in example 1 per body. One week later, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 5) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in an atmosphere of 5% CO2 to restimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 4. In Figure 4, the vertical axis indicates the average number of cells that produced IFNy in response to stimulation with the added cells, out of three mice per group. The vaccine administered to the mice is indicated on the horizontal axis. The black bars and white bars in Figure 4 show the results that the splenocyte of the HLA-A*02:01 transgenic mouse was incubated in the presence or absence of the peptide SEQ ID NO: 5, respectively. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 5 were more in the case of adding the compound prepared in example 1 to the vaccine d, compared to the case of not adding compound . The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 8 Evaluation of adjuvant activity in viw in HU\-A*24: 02 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine prepared by mixing the peptide SEQ ID NO: 18 prepared in Reference Example 20 with Montanide ISA 51 VG (hereinafter referred to as vaccine e) the compound prepared in Example 1 was added to prepare a vaccine. The vaccine was administered to an HLA-A'24:02 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the ma / 1 / uazuu method and antigen-specific CTL induction test. The TYAGCLSQIF in the peptide of SEQ ID NO: 18 corresponds to an antigen peptide derived from an Or7cl protein restricted by HLA-A*24:02. The ability to induce CTL specific for the antigen peptide (SEQ ID NO: 18) was evaluated by the vaccine by measuring whether IFNγ can be produced upon stimulation of mouse splenocytes with the peptide. Furthermore, the ability to exert adjuvant activity in vivo by the compound of Example 1 was evaluated by comparing the number of CTL induced by vaccine e and the number of CTL induced by the vaccine prepared by adding the compound prepared in Example 1 to the vaccine. e, and check the presence or absence of the increase in number. Specifically, the peptide of SEQ ID NO: 18 was dissolved in DMSO and then diluted with water for injection to concentrations of 3 mg / ml. The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG to prepare vaccine e. Vaccine e was injected into mice intradermally in the tail base area in an amount to administer 300 pg of peptide of SEQ ID NO: 18 per body. Or, in vaccine preparation step e, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of peptide of SEQ ID NO: 18 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 3, the peptide (SEQ ID NO: 18) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in an atmosphere of 5% CO2 to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 5. In Figure 5, the vertical axis indicates the average number of cells that produced IFNy in response to stimulation with the added cells, out of three mice per group. The vaccine administered to the mice is indicated on the horizontal axis. The black bars and white bars in Figure 5 show the results that the splenocyte of the HLA-A'24:02 transgenic mouse was incubated in the presence or absence of the peptide SEQ ID NO: 18, respectively. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 18 were more in the case of adding the compound prepared in Example 1 to the vaccine e, compared to the case of not adding compound . The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. ma / 1 / uazuuy Test 9 Evaluation of in vivz adjuvant activity in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compounds prepared in examples 8, 9 and 10 and the compound prepared in reference example 12 was evaluated in the following procedure. To the vaccine cocktail b comprising the compound of formula 4 prepared in reference example 8 and the peptide of SEQ ID NO: 3 prepared in reference example 3 with Montanide ISA51 VG was added the compound prepared in example 8, 9 or 10, or the compound prepared in reference example 12 to prepare each vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of each vaccine was evaluated by the antigen-specific CTL induction test method. Specifically, the compound of formula 4 and the peptide of SEQ ID NO: 3 were dissolved in DMSO, and then diluted with water for injection to concentrations of compound of formula 4 of 3 mg / ml and peptide of SEQ ID NO: 3 of 2.25 mg / ml. The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG to prepare cocktail vaccine b. Cocktail b vaccine was injected into mice intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide of SEQ ID NO: 3 per body. Or, in the step of preparing cocktail vaccine b, the compound prepared in example 8, 9 or 10, or the compound prepared in reference example 12 was added to the diluted peptide solution to prepare a vaccine, and the Prepared vaccine was injected to mice intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body, and 0.4 nmol of compound prepared in example 8, 9 or 10, or the compound prepared in reference example 12 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to restimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 6 and Figure 7. The results of the present test showed that the CTL counts responding to the peptide were more in the case of adding the compound prepared in Example 8, 9 10 or the compound prepared in reference example 12 to vaccine cocktail b, compared to the case of not adding compound. Furthermore, the results showed that the CTL counts responding to the peptide in the case of adding the compound prepared in example 8, 9 or 10 is more, compared to the case of the compound prepared in ma / i / uazuu and the example of reference 12. The above results show that the induced CTL count increases by adding the compound prepared in example 8, 9 or 10 to the vaccine, and strongly suggest that the compound prepared in example 8, 9 or 10 has adjuvant activity in vivo. Furthermore, the results also show that the effect of increasing CTL with the compound prepared in example 8, 9 or 10 is greater, compared to the case of the compound prepared in reference example 12 that does not have a PEG structure. Test 10 Evaluation of adjuvant activity in vivo in HU\-A'02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 11 was evaluated in the following procedure. To a vaccine cocktail b such as test 9, the compound prepared in example 11 was added to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. Specifically, the compound of formula 4 and the peptide of SEQ ID NO: 3 were dissolved in DMSO, and then diluted with water for injection to concentrations of compound of formula 4 of 3 mg / ml and peptide of SEQ ID NO: 3 of 2.25 mg / mL The diluted peptide solution was mixed and emulsified with an equal volume of Montanide ISA 51 VG to prepare vaccine cocktail b. Vaccine cocktail b was injected to mice intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide of SEQ ID NO: 3 per body. Or, in the step of preparing vaccine cocktail b, the compound prepared in Example 11 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of the compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 0.4 nmol of the compound prepared in example 11 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 8 and Figure 9. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 ma / 1 / uazuuy were more in the case of adding the compound prepared in example 11 to vaccine cocktail b, compared to the case of adding no compound. The above results show that the induced CTL count increases upon adding the compound prepared in Example 11 to the vaccine, and strongly suggest that the compound prepared in Example 11 has adjuvant activity in vivo. Test 11 Evaluation of adjuvant activity in viw in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a cocktail vaccine (emulsified composition 1) comprising the compound of formula 4 prepared in reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as cocktail vaccine f) was added compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the above emulsified composition 1 was prepared as follows. 95.8% (w / w) soybean oil, 3% (w / w) PEG-30 dipolyhydroxy stearate, and 1.2% (w / w) polysorbate 80 were mixed to prepare an oil phase mixture. The preparation amount was adjusted as appropriate. The compound of formula 4 and the peptide SEQ ID NO: 3 were mixed with pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) to adjust each concentration to 3 mg / ml and 2.25 mg / ml, respectively. The prepared peptide dilution was mixed with an equal volume of the oil phase mixture to give an emulsified product, vaccine cocktail f. Mice were injected with vaccine cocktail f intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide SEQ ID NO: 3 per body. Or, in the cocktail vaccine preparation step f, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 0.04 nmol or 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ma / 1 / uazuuy plate were counted. ELISPOT. The results are shown in Figure 10 and Figure 11. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the compound prepared in Example 1 to vaccine cocktail f, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 12 Evaluation of adjuvant activity in viw in transgenic mouse HL A-A*02:01 The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a cocktail vaccine (emulsified composition 2) comprising the compound of formula 4 prepared in reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as cocktail vaccine g) was added compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the above emulsified composition 2 was prepared as follows. 95.8% (w / w) medium chain triglyceride (MYGLYOL 812), 3% (w / w) PEG-30 dipolyhydroxy stearate and 1.2% (w / w) polysorbate 80 were mixed to prepare a phase mixture. oily The preparation amount was adjusted as appropriate. The compound of formula 4 and the peptide SEQ ID NO: 3 were mixed with pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) to adjust each concentration to 3 mg / ml and 2.25 mg / ml, respectively. The prepared peptide dilution was mixed with an equal volume of the oil phase mixture to give an emulsified product, vaccine cocktail g. Mice were injected with cocktail g vaccine intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body and 225 pg of peptide SEQ ID NO: 3 per body. Or, in the step of preparing the vaccine cocktail g, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of the compound of formula 4 per body, 225 pg of peptide of SEQ ID NO: 3 per body and 0.04 nmol or 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. . Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 12 and Figure 13. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the prepared compound in example 1 to the cocktail g vaccine, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 13 Evaluation of adjuvant activity in viw in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a cocktail vaccine (emulsified composition 3) comprising the compound of formula 4 prepared in reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as cocktail vaccine h) was added compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the above emulsified composition 3 was prepared as follows. 95.8% (w / w) isopropyl myristate, 3% (w / w) PEG-30 dipolyhydroxy stearate, and 1.2% (w / w) polysorbate 80 were mixed to prepare an oil phase mixture. The preparation amount was adjusted as appropriate. The compound of formula 4 and the peptide SEQ ID NO: 3 were mixed with pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) to adjust each concentration to 3 mg / ml and 2.25 mg / ml, respectively. The prepared peptide dilution was mixed with an equal volume of the oil phase mixture to give an emulsified product, vaccine cocktail h. Mice were injected with cocktail h vaccine intradermally in the tail base area in an amount to administer 300 pg of the compound of formula 4 per body and 225 pg of the peptide SEQ ID NO: 3. Or, in the step of To prepare the vaccine cocktail h, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the tail base area in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide SEQ ID NO: 3, and 0.04 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in an atmosphere of 5% CO2 to restimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 14. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 1 were more in the case of adding the compound prepared in Example 1 to the vaccine cocktail h , compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Figure 26 shows the results for each spleen weight in the mice tested in tests 11-13. The present results show that the administration of example 1 does not induce a pronounced increase in spleen weight and suggest that the compound prepared in example 1 has adjuvant activity in vivo without causing splenomegaly. Test 14 Evaluation of adjuvant activity in viw in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a cocktail vaccine (oil suspension formulation) comprising the compound of formula 4 prepared in reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as cocktail vaccine i) was added the compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the above oil suspension formulation was prepared as follows. Sucrose fatty acid ester (RYOTO SUGAR ESTER L-195) was dissolved in cyclohexane to adjust the concentration to 125 mg / ml, and then the compound of formula 4 and the peptide SEQ ID NO: 3 were added to the solution to adjust each concentration at 0.75. mg / ml and 0.5625 mg / ml to give an oil phase mixture. pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) was added to the oil phase mixture at 1 ml to 2 ml of the oil phase mixture and the mixture was dispersed with a homogenizer and lyophilized. To the lyophilized product, 1 ml of isopropyl myristate was added to give an oily suspension formulation, vaccine cocktail i. The preparation amount was adjusted μλ / 1 / uazuuy as appropriate. Mice were injected with vaccine cocktail I intradermally in the tail base area in an amount to administer 300 pg of Compound of formula 4 per body and 225 pg of peptide SEQ ID NO: 3 per body. Or, in the cocktail vaccine preparation step i, the compound prepared in Example 1 was added to the pH 2.5 buffer to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide SEQ ID NO: 3 per body, and 0.04 nmol or 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 15 and Figure 16. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the compound prepared in example 1 to vaccine cocktail i, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 15 Evaluation of adjuvant activity in viw in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine (hydrogel formulation) comprising the compound of formula 4 prepared in Reference Example 8 and the peptide SEQ ID NO: 3 prepared in Reference Example 3 (hereinafter referred to as vaccine cocktail j) the compound was added. prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A'02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the above hydrogel formulation was prepared as follows. The compound of formula 4, peptide SEQ ID NO: 3 and polyoxyethylene (196) polyoxypropylene (67) glycol were mixed with pH 2.5 buffer (10 mM tartaric acid) to adjust each concentration to 1.5 mg / ml, 1.125 ma / 1 / uazuuy mg / ml and 200 mg / ml, respectively. The mixture was cooled to ice temperature to give a hydrogel formulation, vaccine cocktail j. The preparation amount was adjusted as appropriate. Vaccine cocktail j was injected to mice intradermally in the tail base area in an amount to administer 300 pg of Compound of formula 4 per body and 225 pg of peptide SEQ ID NO: 3 per body. Or, in the step of preparing vaccine cocktail j, the compound prepared in Example 1 was added to the pH 2.5 buffer to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of ​​the cola in an amount to administer 300 pg of compound of formula 4 per body, 225 pg of peptide SEQ ID NO: 3 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 17 and Figure 18. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the prepared compound in example 1 to vaccine cocktail j, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Figure 27 shows the results for each spleen weight in the mice tested in tests 14 and 15. The present results show that the administration of example 1 does not induce a pronounced increase in spleen weight and suggest that the compound prepared in example 1 has adjuvant activity in vivo causing splenomegaly. Test 16 Evaluation of adjuvant activity in vivo in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine (liposome formulation 1) comprising the compound of formula 4 prepared in reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as vaccine cocktail k) was added compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the CTL induction test method. 100 antigen specific. For example, the liposome formulation 1 above was prepared as follows. 47.1 mg of hydrogenated soy phosphatidylcholine and 15.47 mg of cholesterol were dissolved in t-butyl alcohol and the mixture was lyophilized. To the lyophilized product, 2 ml of pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) containing 2.5 mg / ml of the compound of formula 4 and 1,875 mg / ml of peptide SEQ ID NO: 3 were added, and the solution was filtered through a 0.1 pm polycarbonate membrane filter with an extruder (Mini-Extruder, Avanti Polar Lipids) that was heated to approximately 65°C to give liposome formulation 1, vaccine cocktail k. The preparation amount was adjusted as appropriate. Mice were injected with cocktail k vaccine intradermally in the tail base area in an amount to administer 500 pg of compound of formula 4 per body and 375 pg of peptide SEQ ID NO: 3 per body. Or, in the step of preparing the vaccine cocktail k, the compound prepared in Example 1 was added to the pH 2.5 buffer to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of ​​the cola in an amount to administer 500 pg of compound of formula 4 per body, 375 pg of peptide SEQ ID NO: 3 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in an atmosphere of 5% CO2 to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 19. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 1 were more in the case of adding the compound prepared in example 1 to the vaccine cocktail k , compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 17 Evaluation of in vivo adjuvant activity in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine (liposome formulation 2) comprising the compound of formula 4 prepared in μλ / 1 / uazuuy 101 reference example 8 and the peptide SEQ ID NO: 3 prepared in reference example 3 (hereinafter referred to as vaccine cocktail I) the compound prepared in example 1 was added to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the liposome formulation 2 above was prepared as follows. 42.66 mg of sphingomyelin and 15.47 mg of cholesterol were dissolved in t-butyl alcohol and the mixture was lyophilized. To the lyophilized product, 2 ml of pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) containing 2.5 mg / ml of compound of formula 4 and 1,875 mg / ml of peptide SEQ ID NO: 3 were added, and the solution was filtered through a 0.1 pm polycarbonate membrane filter with an extruder (Mini-Extruder, Avanti Polar Lipids) which was heated to approximately 65°C to give liposome formulation 2, vaccine cocktail I. The preparation amount was adjusted as appropriate. The cocktail vaccine was injected into mice intradermally in the tail base area in an amount to administer 500 pg of compound of formula 4 per body and 375 pg of peptide SEQ ID NO: 3 per body. Or, in the step of preparing vaccine cocktail I, the compound prepared in Example 1 was added to the pH 2.5 buffer to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of ​​the cola in an amount to administer 500 pg of compound of formula 4 per body, 375 pg of peptide SEQ ID NO: 3 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 4) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 20 and Figure 21. The results of the present test showed that the counts of CTL responding to the peptide SEQ ID NO: 1 or SEQ ID NO: 4 were more in the case of adding the prepared compound in example 1 to the vaccine cocktail I, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. ma / i / uazuuy 102 Test 18 Evaluation of adjuvant activity in v / ko in HLA-A*02:01 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine (liposome formulation 3) comprising the compound of formula 4 prepared in Reference Example 8 and the peptide SEQ ID NO: 3 prepared in Reference Example 3 (hereinafter referred to as cocktail m vaccine) was added compound prepared in example 1 to prepare a vaccine. The vaccine was administered to an HLA-A*02:01 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. For example, the liposome formulation 3 above was prepared as follows. 36.7 mg of l,2-dipalmitoyl-sn-glycero-3-phosphocholine, 7.58 mg of 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine sodium salt and 15.47 mg of cholesterol in t-butyl alcohol / water mixture and the mixture was lyophilized. To the lyophilized product, 2 ml of pH 2.5 buffer (10 mM tartaric acid, 10% trehalose) containing 2.5 mg / ml of compound of formula 4 and 1,875 mg / ml of peptide SEQ ID NO: 3 were added, and the solution was filtered through a 0.1 pm polycarbonate membrane filter with an extruder (Mini-Extruder, Avanti Polar Lipids) that was heated to approximately 65°C to give liposome formulation 3, vaccine cocktail m. The preparation amount was adjusted as appropriate. Mice were injected with cocktail m vaccine intradermally in the tail base area in an amount to administer 500 pg of compound of formula 4 per body and 375 pg of peptide SEQ ID NO: 3 per body. Or, in the step of preparing the vaccine cocktail m, the compound prepared in Example 1 was added to the pH 2.5 buffer to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of ​​the cola in an amount to administer 500 pg of compound of formula 4 per body, 375 pg of peptide SEQ ID NO: 3 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1) was added to the ELISPOT plate containing splenocytes at a final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in an atmosphere of 5% CO2 to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 22. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 1 were more in the case of adding the compound prepared in Example 1 to the vaccine cocktail m , compared to the case of not adding compound. ma / 1 / uazuuy 103 The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Figure 28 shows the results for each spleen weight in the mice tested in tests 16-18. The present results show that the administration of example 1 does not induce a pronounced increase in spleen weight and suggest that the compound prepared in example 1 has adjuvant activity in vivo without causing splenomegaly. Test 19 Evaluation of in vivo adjuvant activity in HLAA*02:01 / HLA-DRBrOl:01 transgenic mice The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. A cocktail vaccine comprising the peptide SEQ ID NO: 1 prepared in Reference Example 1 and the peptide SEQ ID NO: 17 prepared in Reference Example 20 with a preliminarily emulsified composition (hereinafter referred to as cocktail vaccine n) is added the compound prepared in Example 1 to prepare each vaccine. The vaccine was administered to an HLA-A*02:01 / HLA-DRBl'01:01 (C57BL / 6CrHLA-A2.1DRl) transgenic mouse, and the adjuvant activity of each vaccine was evaluated by the specific CTL assay method. of antigen and induction of antigen-specific helper T cells. The peptide SEQ ID NO: 17 is an auxiliary peptide derived from the WT1 protein. Specifically, peptide SEQ ID NO: 1 and peptide SEQ ID NO: 17 were dissolved in DMSO, and then diluted with water for injection to concentrations of peptide SEQ ID NO: 1 of 2 mg / ml and peptide SEQ ID NO: 17 of 4. mg / mL The prepared peptide dilution was mixed with an equal volume of the preliminary emulsified composition prepared as test 4 to give an emulsified product, vaccine cocktail no. Mice were injected with vaccine cocktail n intradermally in the tail base area in an amount to deliver 200 pg of peptide SEQ ID NO: 1 per body and 400 pg of peptide SEQ ID NO: 17 per body. Or, in the step of preparing the vaccine cocktail n, the compound prepared in Example 1 was added to the diluted peptide solution to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the tail in an amount to administer 200 pg of peptide SEQ ID NO: 1 per body, 400 pg of peptide SEQ ID NO: 17 per body and 0.04 nmol or 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 4, the peptide (SEQ ID NO: 1 or SEQ ID NO: 17) was added to the ELISPOT plate containing splenocytes at a final concentration M A / i / uazuuu 104 of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to restimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The results are shown in Figure 23 and Figure 24. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 1 were more in the case of adding the compound prepared in Example 1 to the vaccine cocktail n, compared to the case of not adding compound. Furthermore, the results showed that the counts of helper T cells responding to the peptide SEQ ID NO: 17 were more in the case of adding the compound prepared in example 1 to the vaccine cocktail n, compared to the case of not adding any compound. The above results show that the induced CTL count and the T helper cell count increase by adding the compound prepared in Example 1 to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 20 Evaluation of adjuvant activity in viw in HU\-A*24:02 transgenic mouse The in vivo adjuvant activity of the compound of Example 1 was evaluated in the following procedure. To a vaccine prepared by mixing the compound of formula 5 prepared in Reference Example 22 with a preliminarily emulsified composition (hereinafter referred to as vaccine or) the compound prepared in Example 1 was added to prepare a vaccine. The vaccine was administered to an HLA-A*24:02 transgenic mouse and the adjuvant activity of the vaccine was evaluated by the antigen-specific CTL induction test method. Specifically, the compound of formula 5 was dissolved in DMSO and then diluted with water for injection to compound concentrations of formula 5 of 3 mg / ml. The dilution of the prepared compound was mixed with an equal volume of the preliminary emulsified composition prepared as test 4 to give an emulsified product, vaccine or. Vaccine O was injected into mice intradermally in the tail base area in an amount to administer 300 pg of Compound of formula 5 per body. Or, in the vaccine preparation step o, the compound prepared in Example 1 was added to the solution of the diluted compound to prepare a vaccine, and the prepared vaccine was injected into mice intradermally in the base area of the glue in an amount to administer 300 pg of compound of formula 5 per body and 0.4 nmol of the compound prepared in example 1 per body. The administrations were carried out twice, which had an interval of one week. One week after the final administration, the mice were sacrificed with CO2 gas. Splenocytes were collected from the spleens removed from the mice. Like test 3, the peptide (SEQ ID NO: 2) was added to the ELISPOT plate containing splenocytes at a μλ / 1 / uazuuy 105 final concentration of 10 pg / ml, and the plate was incubated overnight at 37°C in a 5% CO2 atmosphere to re-stimulate the peptide in vitro. Then, after removing the supernatant from the wells, the stained spots on the ELISPOT plate were counted. The result is shown in Figure 25. The results of the present test showed that the CTL counts responding to the peptide of SEQ ID NO: 2 were more in the case of adding the compound prepared in Example 1 to the vaccine or, compared to the case of not adding compound. The above results show that the induced CTL count increases when the compound prepared in Example 1 is added to the vaccine, and strongly suggest that the compound prepared in Example 1 has adjuvant activity in vivo. Test 21 According to the method of test 1, the human TLR7 reporter gene assay was performed with the following samples, and the result was shown in the following table. M A / t / zuz 1 / υυζυυυ TABLE 9 Example No. Human EC50 (nM) 3 637 11 774 8 388 9 3987 10 3807 The result of test 21 suggests that the example compounds of the present invention can act as agonists of human TLR7. Test 22 According to the method of test 1, the human TLR7 reporter gene assay was performed with the following samples, and the result was shown in the following table. The cell used in this paper was the HEK-Blue™ hTLR7 cell line (Invivogen). The HEK-Blue™ hTLR7 cell line is a stably cotransfected cell line that expresses full-length human TLR7 and the secretory reporter gene SEAP under the transcriptional regulation of an NF-κΒ response element. The TLR7 expression of the cell line has already been tested by RTPCR. Transfectants with stable expression were selected using the antibiotic blasticidin and zeocin. 106 TABLE 10 Example No. ECso (nM) 5 7270 6 119 7 71 ma / i / uazuuy

Claims

1. A compound of formula (1): or a pharmaceutically acceptable salt thereof, wherein X is methylene, oxygen atom, sulfur atom, SO, SO2, or NR5, wherein R5 is a hydrogen atom or alkyl of Ci-6, R1 is an alkyl of Ci-6 that may be substituted with 1-5 substituents independently selected from the group consisting of halogen, hydroxy, and alkoxy of Ci-6, R2 and R3 are independently a hydrogen atom or alkyl of Ci-6 that may be substituted with 1-5 substituents independently selected from the group consisting of halogen, hydroxy, and alkoxy of Ci-6, R4 is a hydrogen atom, halogen, hydroxy, alkyl of Ci-6 (which may be substituted with 1-3 identical or different halogens), alkoxy of Ci-6 (which may be substituted with 1-3 identical or different halogens), or cyano, L is a linker, and Y1 is -(CH2CH2O)m-R6, where R6 is a hydrogen or alkyl atom of Ci e, and m is an integer from 3 - 100.

2. The compound according to claim 1 or a pharmaceutically acceptable salt thereof, further characterized in that X is methylene.

3. The compound according to claim 1 or 2 or a pharmaceutically acceptable salt thereof, further characterized in that R1 is a C1-3 alkyl that may be substituted with 1-3 identical or different halogens.

4. The compound according to claim 3, or a pharmaceutically acceptable salt thereof, further characterized in that R1 is methyl.

5. The compound according to any of claims 1 to 4 or a pharmaceutically acceptable salt thereof, further characterized in that R4 is a hydrogen atom, hydroxy, C1-3 alkyl, or C1-3 alkoxy.

6. The compound according to claim 5 or a pharmaceutically acceptable salt thereof, further characterized in that R4 is a hydrogen atom, 108 hydroxy, or methoxy.

7. The compound according to any of claims 1 to 6 or a pharmaceutically acceptable salt thereof, further characterized in that R2 is an alkyl of Ci-e.

8. The compound according to any of claims 1 to 7 or a pharmaceutically acceptable salt thereof, further characterized in that R3 is a hydrogen atom, or a C1-3 alkyl that may be substituted with 1-3 hydroxyl. ma / 1 / uazuuy The compound according to any one of claims 1 to 8 or a pharmaceutically acceptable salt thereof, further characterized in that L is -O-, -NRY-, -C(O)-, -C(O)O-, -OC(O)-, -C(O)NRY-, -NRYC(O)-, -CH2NRY-, -CH2O-, -OC(O)O-, -NR7C(O)O-, -OC(O)NRY-, NR7C(O)NRY-, -OC(S)NRY-, or -NR7C(S)NRY-, wherein R7 is a hydrogen atom or C1-6 alkyl, and RY is a hydrogen atom, C1-6 alkyl, or Y2, wherein Y2 is -(CH2CH2O)n-R8 (where R8 is a hydrogen atom or C1-6 alkyl, and n is an integer from 3 - 100).

10. The compound according to claim 9 or a pharmaceutically acceptable salt thereof, further characterized in that L is -C(O)NRY-, -CH2NRY-, C(O)O-, or -CH2O-.

11. The compound according to claim 9 or a pharmaceutically acceptable salt thereof, further characterized in that L is -CH2NRY-, and RY is a hydrogen atom, C1-6 alkyl, or Y2.

12. The compound according to any one of claims 1 to 11 or a pharmaceutically acceptable salt thereof, further characterized in that Y1 is -(CH2CH2O)m-R6, R6 is a hydrogen or C1-6 alkyl atom, and ym is an integer from 3 to 40.

13. The compound according to claim 1 or a pharmaceutically acceptable salt thereof, further characterized in that the compound is a compound of formula (2): 109 or formula (3): ma / 1 / uazuuy where R2 is a C1-6 alkyl, R3 is a hydrogen atom, or a C1-3 alkyl that may be substituted with 1-3 hydroxy, R4 is a hydrogen atom, hydroxy, or methoxy, L is -CH2NRY-, RY is a hydrogen atom or a C1-5 alkyl, Y1 is -(CH2CH2O)m-R6, R6 is a hydrogen atom or a C1-6 alkyl, and ym is an integer from 3 to 20.

14. The compound according to claim 1 or a pharmaceutically acceptable salt thereof, further characterized in that the compound is a compound of formula (2): wherein R2 is a C1-6 alkyl, R3 is a hydrogen atom, or a C1-3 alkyl which may be substituted with a hydroxy, R4 is a hydrogen atom or methoxy, L is -CH2NRY-, RY is a hydrogen atom or a C1-6 alkyl, Y1 is -(CH2CH2O)m-R6, R6 is a hydrogen atom or a C1-6 alkyl, and ym is an integer from 3 to 40.

15. The compound of claim 1 or a pharmaceutically acceptable salt thereof, further characterized because it is selected from: l-(4-{[2am¡no-4-met¡l-6-(pent¡lam¡no)p¡r¡m¡d¡n-5-¡l]met¡l}-3-methoxyphen¡l)-2-met¡l-5,8,ll,14-tetraoxa-2azahexade-ol,16-ol l-{4-[(2-am¡no-4-{[(3S)-lh¡drox¡hexane-3-¡l]am¡no}-6-met¡lp¡rim¡d¡n-5-yl)meth¡l]- 110 3-methoxyphen¡l}-2-meth¡l-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol, l-(3-{[2-amino-4-met¡l-6(pent¡lam¡no)pyrimidine-5-¡l]meth¡l}-4-methoxyphen¡l)-2-met¡l-5,8,ll,14-tetraoxa-2-azahexadecan-16-ol, 1(3-{[2-arnino-4-rnet¡l-6-(pent¡lamino)pyrimidine-5-yl]methyl}-4-hydroxyphen¡l)-2-met¡l-5,8,ll,14-tetraoxa-2azahexadecan-16-ol, 4-[(2-amino-4-{[(2S)-l-hydroxypentane-2-yl]am¡no}-6-methylpyr¡m¡d¡n-5-yl)methyl]-N(20-hydroxy-3,6,9,12,15,18-hexaoxaicosan-l-yl)-3m 4-[(2-amino-4-{[(2S)-lh¡droxypentane-2-¡l]am¡no}-6-meth¡lp¡rm¡n-5-¡l)met¡l]-3-methox¡benzoate of 2,5,8,11-tetraoxatridecane-13-lo 5-{[2-methox¡-4-(2,5,8,ll,14-pentaoxapentadecane-l-¡l)phen¡l]meth¡l}-6-methyl-N4-pent¡lp¡r¡md¡na2,4-diamine, l-(4-{[2-am¡no-4-met¡l-6-(pentylam¡no)p¡r¡m¡n-5-yl]meth}-3-methox¡phenyl)-2-meth¡l5,8,ll,14,17,20,23,26,29-noxazole-2-azone,31-azone l-(4-{[2-amino-4-methyl-6(pent¡lam¡no)p¡r¡m¡d¡n-5-l]meth¡l}-3-methoxyphen¡l)-2-meth¡l5.8,ll,14.1 7,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71-tricosaoxa-2azatriheptacontan-73-ol, l-(4-{[2-amino-4-meth¡l-6-(pentylamino)pyrimid¡n-5-yl]meth¡l}-3-methox¡phen¡l)-2methyl5,8,11, 14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80,83,86,89,92,95,98,10 l,104,107-pentatriacontaoxa-2-azanonehectan-109-ol, y 12-[(4-{[2-am¡no-4-methyl-6(pent¡lam¡no)p¡nmid¡n-5-¡l]met¡l}-3-methox¡phen¡l)meth¡l]-3,6,9,15,18,21-hexaoxa-12-azone-codisanol,¡3.

16. The requirement for compliance with recommendation 1 or a pharmaceutically acceptable solution for the same product, also characterized by selecting: l-(4-{[2am¡no-4-met¡l-6-(pent¡lam¡no)p¡rim¡din-5-¡l]met¡l}-3-metox¡phen¡l)-2-met¡l-5,8,ll,14-tetraoxa-2azahexadecan-16-ol, l-(4-{[2-amino-4-methyl-6-(pentylamino)pyrimid¡n-5-yl]methyl}-3-methox¡phenyl)-2methyl-5,8,11,14,17,20,23,26,29-nonaoxa-2-azahentr¡acontan-31-ol, l-(4-{[2-amino-4-methyl-6(pent¡lam¡no)p¡rimidin-5-¡l]met¡l}-3-methoxifen¡l)-2-met¡l5,8,11,14,1 7,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71-tricosaoxa-2azatriheptacontan-73-ol, l-(4-{[2-amino-4-met¡l-6-(pentylamino)pyrimid¡n-5-yl]met¡l}-3-methox¡phen¡l)-2methyl5,8,11, 14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80,83,86,89,92,95,98,10 l,104,107-pentatriacontaoxa-2-azanonahectan-109-ol, y 12-[(4-{[2-amino-4-methyl-6(pent¡lam¡no)p¡nmid¡n-5-¡l]met¡l}-3-methox¡phenyl)met¡l]-3,6,9,15,18,21-hexaoxa-12-azatr¡cosan-l,23diol.

17. A pharmaceutical composition, comprising the compound of any of claims 1 to 16 or a pharmaceutically acceptable salt thereof.

18. The pharmaceutical composition according to claim 17, further characterized in that it is an emulsion formulation, an oil-based suspension, a hydrogel formulation, or a lipid formulation. ma / i / uazuuy 111 19. The pharmaceutical composition according to claim 18, further characterized in that it is an emulsion formulation.

20. The pharmaceutical composition according to claim 19, further characterized in that the emulsion formulation is a water-in-oil emulsion.

21. The pharmaceutical composition according to claim 20, further characterized in that the emulsion formulation comprises (1) ethyl oleate, octyldodecyl myristate, sorbitan monooleate, glyceryl monooleate, polyoxyethylene hydrogenated castor oil 20, glycerin, and sodium dihydrogen phosphate, or (2) Montanide ISA 51VG.

22. The pharmaceutical composition according to claim 18, further characterized in that it is a lipid formulation.

23. The pharmaceutical composition according to claim 22, further characterized in that the lipid formulation is a liposome formulation comprising phospholipids.

24. The pharmaceutical composition according to claim 22 or 23, further characterized in that the lipid formulation is a liposome formulation comprising sterols.

25. The pharmaceutical composition according to claim 24, further characterized in that the steral is cholesterol.

26. The pharmaceutical composition according to any of claims 23 to 25, further characterized in that the liposome formulation comprises at least one additive selected from the group consisting of inorganic acid, inorganic acid salt, organic acid, organic acid salt, sugars, buffering agent, antioxidant, and polymers.

27. The pharmaceutical composition according to any of claims 17 to 26, further characterized in that it further comprises an antigen.

28. The pharmaceutical composition according to claim 27, further characterized in that the tumor antigen is a tumor antigen peptide.

29. The pharmaceutical composition according to claim 28, further characterized in that the tumor antigen peptide is a combination of a peptide represented by the amino acid sequence of formula (4): CRMFPNAPYL I CYTWNQMNL where the linkage between CC is a disulfide bond, or a pharmaceutically acceptable salt thereof, and a peptide represented by the amino acid sequence of SEQ ID NO 3: WAPVLDFAPPGASAYGSL, ma / i / uazuuy 112 or a pharmaceutically acceptable salt thereof.

30. A vaccine adjuvant for a cancer vaccine comprising the compound of any one of claims 1 to 16 or a pharmaceutically acceptable salt thereof.

31. A kit comprising (a) the compound of claim 1 or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition comprising the compound of claim 1 or a pharmaceutically acceptable salt thereof; and (b) a tumor antigen or a pharmaceutical composition comprising a tumor antigen.