Peptide and conjugate containing said peptide

Abstract

The present invention relates to: a peptide; a conjugate containing the peptide; compositions respectively containing the peptide and the conjugate; and others. This peptide comprises the following amino acid sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-S-3Py6NH2-HseMe-dk-Y, or an amino acid sequence having a structure such that substitution, addition, deletion or insertion occurs in 1-10 amino acid residues selected from the group consisting of amino acid residues located at position-1, position-2, position-3, position-4, position-5, position-7, position-8, position-9, position-10 and position-11 in the above-mentioned amino acid sequence. This conjugate contains the peptide.

Description

Peptides and conjugates containing the peptides

[0001] The present invention relates to a peptide, a conjugate comprising the peptide and a payload (sometimes referred to as a "peptide conjugate," a "peptide complex," or simply a "conjugate"), and uses of the peptide or conjugate.

[0002] CA9 (Carbonic anhydrase IX, carbonic anhydrase-9) is one of 15 carbonic anhydrases and is a homodimeric transmembrane protein localized on the cell membrane (Non-Patent Document 1). CA9 has three domains: a catalytic domain, a proteoglycan-like domain, a membrane-spanning domain, and a cytoplasmic tail. One of its functions is to convert water molecules and carbon dioxide into hydrogen ions and bicarbonate ions in the catalytic domain, which requires zinc, and regulates the intracellular and extracellular pH to a state suitable for cell proliferation (Non-Patent Document 2). In fact, in vitro and tumor-bearing mouse studies have confirmed that tumor cells in which CA9 was knocked out exhibit slower tumor cell proliferation than wild-type cells, demonstrating experimental evidence that CA9 is involved in tumor cell proliferation (Non-Patent Document 3). Furthermore, in patients with various tumors, CA9 expression levels have been significantly associated with overall survival, disease-free survival, local control, disease-specific survival, metastasis-free survival, and progression-free survival, suggesting that patients with tumors with high CA9 expression are at higher risk of local recurrence, disease progression, and metastasis, regardless of tumor type or location (Non-Patent Document 4). Based on these reports, CA9 is expected to be a promising target for detecting tumors with poor prognosis. The mechanism by which CA9 expression is induced has been reported to be activation of the hypoxia-inducible factor (HIF) 1α pathway (Non-Patent Document 5), and it has been reported that many patients, particularly clear cell renal cell carcinoma and colorectal cancer, have high CA9 expression levels (Non-Patent Document 6) (Non-Patent Document 7). In colorectal cancer, activation of the HIF 1α pathway associated with hypoxia results in high CA9 expression in tumor tissues of approximately 70% of patients (Non-Patent Document 7). On the other hand, it has been reported that in more than half of patients with clear cell renal cell carcinoma, the HIF1α pathway is chronically activated even under normoxic conditions (Non-Patent Document 5), due to somatic mutations or hypermethylation of the promoter region of the VHL (Von Hippel-Lindau) gene, a tumor suppressor gene (Non-Patent Document 8), and CA9 is highly expressed in tumor tissues of approximately 90% of patients (Non-Patent Document 6).Metastatic colorectal cancer and metastatic renal cell carcinoma are diseases with extremely poor prognoses, with a 5-year survival rate of 20% or less, and therefore the establishment of diagnostic and therapeutic methods for these diseases is urgently needed.To date, cancer therapeutics targeting CA9 have been developed using antibodies such as girentuximab, but have failed to demonstrate efficacy (Non-Patent Document 9). Therefore, antibody-RI conjugates have been developed by conjugating girentuximab with a chelating agent and attaching PET and therapeutic nuclides. PET imaging using antibody-RI conjugates enables highly sensitive tumor detection, but the long blood half-life of the antibody necessitates the use of high-energy nuclides. Since tumors can be detected five days after administration, it takes time to detect the tumor (Non-Patent Document 10). Furthermore, in treatment, the long blood half-life of the antibody also leads to prolonged thrombocytopenia caused by RI, making repeated administration difficult. In fact, in a phase II clinical trial, thrombocytopenia did not resolve, making three repeated administrations impossible (Non-Patent Document 11). Therefore, there remains a need for the development of novel cancer therapeutics and diagnostic agents, such as PET imaging agents, that target CA9 and contain compounds other than antibodies as active ingredients.

[0003] Thanksgiving, smile, smile 1000000213 028(2):267−7760 Aesthetic, slim, slim slim2000 a 24284(30)020299−300000 Emotion, snowflake 217 zero 78(6):10225−10237722 00,000,000,000,000,000,000,000,000,000,000,000,000,0 206:68 4 LIKE,N 2 EXPERIENCE 0,000000000000000000000000 15S60(24):7075−83SIGNIFICANCE THIS, THIS, THIS IS THIS 203 99(2):802−11FINANCIAL THIS, THIS, THIS IS THIS 2023 DAY 3024(3)025815 THIS, THIS, THIS IS 2013 P45(8):860−4000000,000,000,000,000,000,000,000,000,000,000,000,000,000,0 DAYN2017 20000000000000000000000000000000000000 THIS IS YOUR LIFE 3 YOU PLEASE−JOY−GENERAL FIGURE PLAY CHASE ANALYSIS The snow snow snow FASHION(SYS)203 SHY The scientists are the scientists Aesthetic aesthetics Emotional, scientific, scientific 2016 N969(5):767−7

[0004] The present inventors have conceived the present invention as a result of extensive research aimed at creating a compound having CA9 binding activity. The present inventors have also discovered a conjugate of a compound having CA9 binding activity with a payload such as a radioactive substance or a fluorescent substance. The present invention relates to a novel peptide having CA9 binding activity, a conjugate of the peptide with a payload, a composition (pharmaceutical composition, diagnostic composition, research composition) containing the peptide or the conjugate, and use of the peptide or the conjugate.

[0005] This application includes, but is not limited to, the following inventions: [1] A peptide comprising the following amino acid sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-S-3Py6NH2-HseMe-dk-Y (SEQ ID NO: 1), or an amino acid sequence having a substitution, addition, deletion, or insertion at 1 to 10 amino acid residues selected from the group consisting of the 1st, 2nd, 3rd, 4th, 5th, 7th, 8th, 9th, 10th, and 11th amino acid residues of the above amino acid sequence. [2] The peptide according to [1], wherein (1) MeC, C, or MeCt is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1; or (2) MeA, MeS, MeN, Hpr, G, or P is added as the 13th amino acid residue and further MeG, G, da, or Meda is added as the 14th amino acid residue to the amino acid sequence of SEQ ID NO: 1. [3] The peptide according to [1] or [2], comprising an amino acid sequence having substitutions, additions, deletions, or insertions in 1 to 7 amino acid residues selected from the group consisting of the 1st, 4th, 7th, 8th, 9th, 10th, and 11th amino acid residues of the amino acid sequence of SEQ ID NO: 1.[4] The first amino acid residue is da, dq, de, dhgl, or dk; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is S, Hgl, Hgl(PEG8Me), alT, Hgn, SMe, KCOpipzaa, or DabAc; and the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa. the seventh amino acid residue is PeG, pMeOPeG, MsMeapG, 30MePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 40MePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the eighth amino acid residue is H, S, P, D, KCOpipzaa, Q(PEG8Me), P4Sh, Hse, SMe, Qmm, or Qdm; the ninth amino acid residue is 3Py6NH2, 5Inda, Y, or F40Me; the tenth amino acid residue is Ahp, HseMe, or E; and The peptide according to any one of [1] to [3], which satisfies one or more of the following requirements: the 11th amino acid residue is dk, G, da, dq, dkCOpipzaa, dk(t4amCh), de, Acb, or dkAc. [5] The peptide according to any one of [1] to [4], which satisfies one or more of the following requirements: the 2nd amino acid residue is Tbg; the 3rd amino acid residue is 3Py6NH2; the 5th amino acid residue is Meda; the 7th amino acid residue is PeG or pHPeg; the 9th amino acid residue is 3Py6NH2 or 5Inda; and the 10th amino acid residue is HseMe. [6] The peptide according to any one of [1] to [4], wherein the second amino acid residue is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe.[7] The peptide according to any one of [1] to [6], which comprises or consists of an amino acid sequence set forth in any one of SEQ ID NOs: 2 to 54. [8] The peptide according to any one of [1] to [7], further having an additional amino acid residue. [9] The peptide according to any one of [1] to [8], wherein the peptide is a cyclic peptide.

[10] The peptide according to any one of [1] to [9], wherein the peptide has a cyclic structure in which the chloroacetylated first amino acid residue of the amino acid sequence of SEQ ID NO: 1 is bonded to a cysteine ​​residue contained in the peptide.

[11] The peptide according to any one of [1] to [9], wherein the peptide has a cyclic structure in which the amino group of the first amino acid residue of the amino acid sequence of SEQ ID NO: 1 contained in the peptide is bonded to the carboxy group of the 14th amino acid residue.

[12] The peptide according to any one of [1] to

[11] , wherein: (a) a linker and / or a payload can be bonded to the C-terminus of the peptide; or (b) the 1st, 4th, 8th, 11th, or 13th amino acid residue of the amino acid sequence of SEQ ID NO: 1 is an amino acid residue in which a linker and / or a payload can be bonded.

[13] A conjugate comprising the peptide according to any one of [1] to

[12] and a payload, wherein (i) any payload is bound to the 13th amino acid residue of SEQ ID NO: 1, with or without a linker; or (ii) a payload is bound to the 1st, 4th, 8th or 11th amino acid residue of SEQ ID NO: 1, as shown in the following formula (I): [In formula (I), R １ is H or a C alkyl group; R ２ is C alkyl-NH-, C alkyl-C aryl-O-C alkyl-NH-, C alkyl-NH(=O)-CH(C alkylphenyl)-NH-, C alkyl-NH(=O)-CH(C alkyl)-NH-, or C alkyl-NH(=O)-C cycloalkyl-C alkyl-NH-; and X is any payload. ２is C1-6 alkyl-NH-.

[15] The conjugate according to

[13] or

[14] , wherein X is a chelating agent.

[16] The conjugate according to

[15] , wherein the chelating agent is bound to a radioactive substance.

[17] The conjugate according to

[15] or

[16] , wherein the chelating agent is DOTA, DOTAGA, or NODAGA.

[18] A pharmaceutical composition comprising the peptide according to any one of [1] to

[12] .

[19] A pharmaceutical composition for preventing or treating a CA9-related disease, comprising the peptide according to any one of [1] to

[12] .

[20] A pharmaceutical composition comprising the conjugate according to any one of

[13] to

[17] .

[21] A pharmaceutical composition for preventing or treating a CA9-related disease, comprising the conjugate according to any one of

[13] to

[17] .

[22] A diagnostic or research composition comprising the peptide according to any one of [1] to

[12] .

[23] A diagnostic or research composition for diagnosing a CA9-related disease, comprising the peptide according to any one of [1] to

[12] .

[24] A diagnostic or research composition comprising the conjugate according to any one of

[13] to

[17] .

[25] A diagnostic or research composition for diagnosing a CA9-related disease, comprising the conjugate according to any one of

[13] to

[17] .

[26] An imaging agent comprising the conjugate according to any one of

[13] to

[17] .

[27] An imaging agent used for tumor diagnosis, comprising the conjugate according to any one of

[13] to

[17] .

[28] A radioligand imaging agent used in positron emission tomography, comprising the conjugate according to any one of

[13] to

[17] .

[29] A method for testing a peptide, the method comprising testing at least one of a) solubility in a solvent, b) CA9 binding activity, c) toxicity to cells and / or tissues, or d) toxicity to experimental animals, wherein the peptide is a peptide according to any one of [1] to

[12] .

[30] A method for testing a conjugate, the method comprising testing at least one of: a) solubility in a solvent; b) CA9 binding activity; c) toxicity to cells and / or tissues; or d) toxicity to experimental animals, wherein the conjugate is the conjugate according to any one of

[13] to

[17] .

[31] The following: the first amino acid residue is de(PEG8Me), dk, dyae, or dkCOpipzaa; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is K, KCOpipzaa, Hgn(Qglucamine-NH2), Hgn(KCOpipzaa-NH2), or Qglucamine; and the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa; The peptide according to any one of [1] to [3], which satisfies one or more of the following requirements: the seventh amino acid residue is PeG, pMeOPeG, MsMeapG, 30MePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 40MePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the eighth amino acid residue is K; the ninth amino acid residue is 3PyNH, 5Inda, Y, or F40Me; the tenth amino acid residue is Ahp, HseMe, or E; and the eleventh amino acid residue is dk(F) or dk(PEG8c).

[32] The peptide according to any one of [1] to [6], comprising or consisting of an amino acid sequence set forth in any one of SEQ ID NOs: 55 to 103.

[33] A conjugate comprising the peptide according to

[32] and a payload, wherein any payload is bound to the 1st, 4th, 8th, 11th, or 13th amino acid residue, with or without a linker.

[34] The conjugate according to any one of conjugate numbers 1 to 81 set forth in Table 8 or Table 18.

[0006] The peptides and conjugates according to the present invention have CA9 binding activity and are therefore useful as pharmaceutical compositions, diagnostic compositions, research compositions, and the like for preventing or treating CA9-related conditions.

[0007] FIG. 1 shows various peptides of the present invention with DOTA- ６７ 2 is a graph showing the distribution of each conjugate having Ga as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 4 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６７ 3 is a graph showing the distribution of each conjugate having Ga as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 24 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６７ 4 is a graph showing the distribution of each conjugate having Ga as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 72 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６４ 5 is a graph showing the distribution of the conjugate having Cu as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 4 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６４ 6 is a graph showing the distribution of each conjugate having Cu as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 24 hours after administration. The horizontal axis represents each tissue, and the vertical axis represents the radioactivity concentration (% ID / g) in each tissue. ６４ Cu, DOTAGA- ６４ Cu or NODAGA- ６４7 is a graph showing the distribution of the conjugate having Cu as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 4 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６４ Cu, DOTAGA- ６４ Cu or NODAGA- ６４ 8 is a graph showing the distribution of each conjugate having Cu as a payload in the body of a female BALB / cSlc-nu / nu tumor-implanted mouse model 24 hours after administration. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ６４ Conjugate No. 64- having Cu as a payload ６４ 9 shows representative PET / CT images of female BALB / cSlc-nu / nu tumor-implanted model mice 1, 4, and 23.5 hours after Cu administration. The white arrows in the figures indicate the location of the implanted tumor. ６４ Conjugate No. 62- having Cu as a payload ６４ 10 shows representative PET / CT images of female BALB / cSlc-nu / nu tumor-implanted model mice 1, 4, and 23.5 hours after Cu administration. The white arrows in the figures indicate the location of the implanted tumor. ６４ Conjugate No. 2 having Cu as a payload ６４ 11 shows representative PET / CT images of female BALB / cSlc-nu / nu tumor-implanted model mice 1, 4, and 23.5 hours after Cu administration. The white arrows in the figures indicate the location of the implanted tumor. ６４ Conjugate No. 56- having Cu as a payload ６４12 shows representative PET / CT images of female BALB / cSlc-nu / nu tumor-implanted model mice 1, 4, and 23.5 hours after Cu administration. The white arrows in the figures indicate the location of the implanted tumor. ６４ Conjugate No. 58- having Cu as a payload ６４ 13 shows representative PET / CT images of female BALB / cSlc-nu / nu tumor-implanted model mice 1, 4, and 23.5 hours after Cu administration. The white arrows in the figures indicate the location of the implanted tumor. １７７ 1 is a graph showing the time course of the average tumor volume in female BALB / cSlc-nu / nu tumor-implanted model mice administered with a conjugate having Lu as a payload, saline, or cabozantinib. The horizontal axis represents the number of days after administration, and the vertical axis represents the tumor volume (mm ３ The short dashed black circle indicates saline, the solid black triangle indicates cabozantinib, and the long dashed black circle indicates Conjugate No. 64- １７７ Lu (administered three times), and the solid white circle indicates Conjugate No. 62- １７７ Lu (3 doses), solid X indicates Conjugate No. 64- １７７ Lu (single administration), the solid black square indicates Conjugate No. 62- １７７ Lu (single administration), solid black circle indicates Conjugate No. 65- １７７ Figure 14 shows the effect of various peptides of the present invention on DOTA-Lu (60 MBq administered once). １７７ 1 is a graph showing the average weight change rate in female BALB / cSlc-nu / nu tumor-implanted mouse models administered with a conjugate having Lu as a payload, saline, or cabozantinib. The horizontal axis represents the number of days after administration, and the vertical axis represents the weight change rate (%). The short dashed black circle line represents saline, the solid black triangle line represents cabozantinib, and the long dashed black circle line represents Conjugate No. 64- １７７ Lu (administered three times), and the solid white circle indicates Conjugate No. 62- １７７ Lu (3 doses), solid X indicates Conjugate No. 64- １７７Lu (single administration), the solid black square indicates Conjugate No. 62- １７７ Lu (single administration), solid black circle indicates Conjugate No. 65 １７７ Figure 15 shows the effect of the peptide of the present invention on DOTA-Lu (60 MBq administered once). ６４ Conjugate No. 62- having Cu as a payload ６４ 16 is a graph showing the distribution of Cu in the body of VMRC-RCW tumor-bearing mice at 4, 24, and 48 hours after administration. The horizontal axis represents each tissue, and the vertical axis represents the radioactivity concentration (% ID / g) in each tissue. １７７ Conjugate No. 62- having Lu as a payload １７７ 17 is a graph showing the distribution of DOTA-Lu in the body of VMRC-RCW tumor-bearing mice at 1, 24, and 48 hours after administration. The horizontal axis represents each tissue, and the vertical axis represents the radioactivity concentration (% ID / g) in each tissue. ６４ Conjugate No. 62- having Cu as a payload ６４ Representative PET / CT images of VMRC-RCW tumor-bearing mice at 1, 4, 23.5, and 47.5 hours after Cu administration. １７７ Conjugate No. 62- having Lu as a payload １７７ 1 is a graph showing the average tumor volume in VMRC-RCW tumor-bearing mice administered with Lu, saline, or cabozantinib. The horizontal axis represents the number of days after administration, and the vertical axis represents the tumor volume (mm ３ ) In addition, black circles indicate group 1: saline, X indicates group 2: cabozantinib, and checkered triangles indicate group 3: Conjugate No. 62- １７７ Lu (30 MBq administered once), vertical striped triangle indicates group 4: Conjugate No. 62- １７７ Lu (30 MBq administered twice), horizontal striped triangle indicates group 5: Conjugate No. 62- １７７ Lu (30 MBq administered three times), black triangles indicate group 6: Conjugate No. 62- １７７Lu (30 MBq administered four times), checkered pattern square indicates group 7: Conjugate No. 62- １７７ Lu (60 MBq administered once), vertical striped square indicates group 8: Conjugate No. 62- １７７ Figure 19 shows the effect of the peptide of the present invention on DOTA-Lu (60MBq administered twice). １７７ Conjugate No. 62- having Lu as a payload １７７ 1 is a graph showing the average weight change rate in VMRC-RCW tumor-bearing mice administered with Lu, saline, or cabozantinib. The horizontal axis represents the number of days after administration, and the vertical axis represents the weight change rate (%). Furthermore, black circles represent Group 1: saline, X represents Group 2: cabozantinib, and checkered triangles represent Group 3: Conjugate No. 62- １７７ Lu (30 MBq administered once), vertical striped triangle indicates group 4: Conjugate No. 62- １７７ Lu (30 MBq administered twice), horizontal striped triangle indicates group 5: Conjugate No. 62- １７７ Lu (30 MBq administered three times), black triangles indicate group 6: Conjugate No. 62- １７７ Lu (30 MBq administered four times), checkered pattern square indicates group 7: Conjugate No. 62- １７７ Lu (60 MBq administered once), vertical striped square indicates group 8: Conjugate No. 62- １７７ Figure 20 shows the effect of the peptide of the present invention on DOTA-Lu (60MBq administered twice). ２２５ Conjugate No. 62- having Ac as a payload ２２５ 21 is a graph showing the results of the distribution in the body of HT-29 cancer-bearing mice 4, 24, and 48 hours after administration of DOTA-Ac. The horizontal axis shows each tissue, and the vertical axis shows the radioactivity concentration (% ID / g) in each tissue. ２２５ Conjugate No. 62- having Ac as a payload ２２５ 1 is a graph showing the average tumor volume in HT-29 cancer-bearing mice administered with saline. The horizontal axis shows the number of days after administration, and the vertical axis shows the tumor volume (mm ３The black squares represent Group 1: physiological saline, and the black triangles represent Group 2: Conjugate No. 62- ２２５ Ac (30 MBq administration), white triangles indicate group 3: Conjugate No. 62- ２２５ Ac (60 MBq administration), X is group 4: Conjugate No. 62- ２２５ Ac (90 MBq administered), black circle indicates group 5: Conjugate No. 62- ２２５ Ac (120 MBq administered), white circle indicates group 6: Conjugate No. 62- ２２５ Figure 22 shows the effect of DOTA-Ac (administered 150 MBq) on the peptide of the present invention. ２２５ Conjugate No. 62- having Ac as a payload ２２５ 1 is a graph showing the change in average body weight in HT-29 tumor-bearing mice administered with saline. The horizontal axis indicates the number of days after transplantation, and the vertical axis indicates the average body weight (g). The black squares indicate Group 1: saline, and the black triangles indicate Group 2: Conjugate No. 62- ２２５ Ac (30 MBq administration), white triangles indicate group 3: Conjugate No. 62- ２２５ Ac (60 MBq administration), X is group 4: Conjugate No. 62- ２２５ Ac (90 MBq administered), black circle indicates group 5: Conjugate No. 62- ２２５ Ac (120 MBq administered), white circle indicates group 6: Conjugate No. 62- ２２５ Ac (150 MBq administered).

[0008] The present invention includes, but is not limited to, the following embodiments. Unless otherwise specified herein, technical and scientific terms used herein have the same meaning as commonly understood by those skilled in the art. The substances, materials, and examples disclosed herein are merely illustrative and are not intended to be limiting. When used herein, the phrase "in one embodiment" means that the embodiment is not limited, i.e., is non-limiting. 1. Abbreviations In this specification, unless otherwise specified, the following abbreviations are used with the following meanings. Abbreviations (general) Å: Angstrom (unit); ClAc: chloroacetyl; Cy5SAlk: Sulfo-Cy5-alkyne; DCM: dichloromethane; TIPS: triisopropylsilyl; tert: tertiary; DTT: dithiothreitol; DMSO: dimethylsulfoxide; Trt: trityl; Boc: tertiary-butoxycarbonyl; DMF: N,N-dimethylformamide; DIEA or DIPEA: N,N-diisopropylethylamine; DIPCI or DIC: N,N'-diisopropylcarbodiimide; Oxyma pure: ethyl cyanohydroxyiminoacetate; DODT: 3,6-dioxa-1,8-octanedithiol; DOTA-NHS ester: 2,2',2''-(10-(2-((2,5-dioxopyrrolidin-1-yl)oxy)-2-oxoethyl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid DOTA: 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid; Fmoc: 9-fluorenylmethyloxycarbonyl; g: grams; H ２O: water; HCl: hydrogen chloride; HATU: O-(7-azabenzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate; HOSu: N-hydroxysuccinimide; HPLC: high performance liquid chromatography; LC-MS or LC / MS: liquid chromatography mass spectrometry; MeOH: methanol; mL: milliliter; M: molar; μL: microliter; mM: millimolar; μM: micromolar; mmol: millimole; mg: milligram; MeCN or CH3CN: acetonitrile; min: minute; mm: millimeter; μm: micrometer; nm: nanometer; nM: nanomolar; NMP: N-methyl-2-pyrrolidone OSu: succinimide; PEG: polyethylene glycol; rpm: revolutions per minute (units); tBu: tertiary butyl; TFA: trifluoroacetic acid; TIS: triisopropylsilane; Trt or Tr: trityl group; H-PEG4Me: 2,5,8,11-tetraoxatridecan-13-amine; H-PEG8Me: 2,5,8,11,14,17,20,23-octaoxapentacosan-25-amine; AA: amino acid; PyAOP: 7-((azabenzotriazol-1-yloxy)tripyrrolidinophosphonium hexafluorophosphate; CSA: 10-camphorsulfonic acid; Fmoc-OSu: N-(9-fluorenylmethoxycarbonyloxy)succinimide; THF: tetrahydrofuran; ClAcOSu: N-(chloroacetoxy)succinimide; Pd2(dba)3.CHCl3: tris(dibenzylideneacetone)dipalladium(0)-chloroform complex; SPhos: 2-dicyclohexylphosphino-2',6'-dimethoxybiphenyl; EDCI.HCl: 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride; Pd(PPh3)4: tetrakis(triphenylphosphine)palladium(0); ClAcOH: chloroacetic acid; conc: concentration;HFIP: 1,1,1,3,3,3-hexafluoro-2-propanol; Pbf: 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl; Alloc: allyloxycarbonyl; Allyl: allyl; Fmoc-Qglucamine-NH2: (9H-fluoren-9-yl)methyl ((S)-1-amino-1,5-dioxo-5-(((2S,3R,4R,5R)-2,3,4,5,6-pentahydroxyhexyl)amino)pentan-2-yl)carbamate; H-Qglucamine-NH2: (S)-4-amino-N1-((2S,3R,4R,5R)-2,3,4,5,6-pentahydroxyhexyl)pentanediamide H-KCOpipzaa(Mpe)-NH2: 3-methylpentan-3-yl(S)-2-(4-((5,6-diamino-6-oxohexyl)carbamoyl)piperazin-1-yl) TEA: triethylamine. Abbreviations (unnatural amino acids) The following abbreviations for unnatural amino acids include those in which the amino group in the main chain is protected with a common protecting group such as a Boc group or an Fmoc group. 2. Peptides The present invention relates to peptides or pharmaceutically acceptable salts thereof. References to "peptides" herein include references to pharmaceutically acceptable salts, isomers, or solvates thereof, unless otherwise indicated. In one aspect, the peptide of the present invention comprises the following amino acid sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-S-3Py6NH2-HseMe-dk-Y (SEQ ID NO: 1); or an amino acid sequence having a substitution, addition, deletion, or insertion of 1 to 10 amino acid residues selected from the group consisting of the 1st, 2nd, 3rd, 4th, 5th, 7th, 8th, 9th, 10th, and 11th amino acid residues of the above amino acid sequence. The peptide of the present invention may be a peptide comprising an amino acid sequence having a substitution, addition, deletion, or insertion in 1 to 9 amino acid residues selected from the group consisting of the first, second, third, fourth, fifth, seventh, eighth, ninth, and eleventh amino acid residues of the amino acid sequence of SEQ ID NO: 1. The peptide may also have a substitution, addition, deletion, or insertion in 1 to 10 amino acid residues selected from the group consisting of the first, second, third, fourth, fifth, seventh, eighth, ninth, tenth, and eleventh amino acid residues of the amino acid sequence of SEQ ID NO: 1. The number of substituted, deleted, added, and / or inserted amino acids may be 1 to 10, with the lower limit being 1. The upper limit is 10, 9, 8, 7, 6, 5, 4, 3, or 2, with the minimum being 1. Preferably, the amino acid sequence may have substitutions, additions, deletions, or insertions at 1 to 7 amino acid residues selected from the group consisting of the 1st, 4th, 7th, 8th, 9th, 10th, and 11th amino acid residues in the amino acid sequence of SEQ ID NO: 1. The number of substituted, deleted, added, and / or inserted amino acids may be 1 to 7, with the lower limit being 1. The upper limit is 7, 6, 5, 4, 3, or 2, with the minimum being 1.Preferably, the amino acid sequence may have substitutions, additions, deletions, or insertions of 1 to 6 amino acid residues selected from the group consisting of the 1st, 4th, 7th, 8th, 9th, and 11th amino acid residues of the amino acid sequence of SEQ ID NO: 1. In one embodiment, the amino acid substitution is preferably a conservative amino acid substitution. Without limitation, such amino acid substitutions are preferably conservative amino acid substitutions. A "conservative amino acid substitution" refers to a substitution with a functionally equivalent or similar amino acid. A conservative amino acid substitution in a peptide results in a static change in the amino acid sequence of the peptide. For example, one or more amino acids with similar polarity act functionally equivalently and result in a static change in the amino acid sequence of the peptide. In general, substitutions within a certain group can be considered conservative in terms of structure and function. However, as will be apparent to those skilled in the art, the role played by a particular amino acid residue can be determined by its significance in the three-dimensional structure of a molecule containing that amino acid. For example, cysteine ​​residues can adopt an oxidized (disulfide) form that is less polar than its reduced (thiol) form. The long aliphatic portion of the arginine side chain can constitute a structurally and functionally important feature. Also, side chains containing aromatic rings (tryptophan, tyrosine, phenylalanine) can contribute to ion-aromatic or cation-pi interactions. In such cases, substitution of amino acids with these side chains with amino acids belonging to acidic or nonpolar groups can be structurally and functionally conservative. Residues such as proline, glycine, and cysteine ​​(disulfide form) can have direct effects on the main-chain conformation and often cannot be substituted without structural distortion. Conservative amino acid substitutions include specific substitutions based on side chain similarity (e.g., substitutions described in L. Lehninger, Biochemistry, 2nd edition, pp. 73-75, Worth Publisher, New York (1975)) and typical substitutions, as shown below.Furthermore, conservative amino acid substitution is preferably, for example, substitution with an amino acid that belongs to the same group as a certain amino acid, where natural amino acids are divided into groups based on the properties of their common side chains, as follows: Hydrophobic (also called non-polar) amino acids: Amino acids that exhibit hydrophobicity (non-polarity), and include alanine (also written as "Ala" or simply "A"), glycine (also written as "Gly" or simply "G"), valine (also written as "Val" or simply "V"), leucine (also written as "Leu" or simply "L"), isoleucine (also written as "Ile" or simply "I"), proline (also written as "Pro" or simply "P"), phenylalanine (also written as "Phe" or simply "F"), tryptophan (also written as "Trp" or simply "W"), tyrosine (also written as "Tyr" or simply "Y"), and methionine (also written as "Met" or simply "M"). Hydrophobic amino acids can be further divided into the following groups: Aliphatic amino acids: Amino acids having a fatty acid or hydrogen in the side chain, including Ala, Gly, Val, Ile, and Leu. Aliphatic / branched-chain amino acids: Amino acids having a branched fatty acid in the side chain, including Val, Ile, and Leu. Aromatic amino acids: Amino acids having an aromatic ring in the side chain, including Trp, Tyr, and Phe. Hydrophilic (also called polar) amino acids: Amino acids that exhibit hydrophilicity (polarity), including serine (also referred to as "Ser" or simply "S"), threonine (also referred to as "Thr" or simply "T"), cysteine ​​(also referred to as "Cys" or simply "C"), asparagine (also referred to as "Asn" or simply "N"), glutamine (also referred to as "Gln" or simply "Q"), aspartic acid (also referred to as "Asp" or simply "D"), glutamic acid (also referred to as "Glu" or simply "E"), lysine (also referred to as "lysine" or simply "Lys" or simply "K"), arginine (also referred to as "Arg" or simply "R"), and histidine (also referred to as "His" or simply "H"). Hydrophilic amino acids can also be further divided into the following groups: Acidic amino acids: Amino acids whose side chains exhibit acidic properties, including Asp and Glu. Basic amino acids: Amino acids whose side chains are basic, including Lys, Arg, and His.Neutral amino acids: Amino acids with neutral side chains, including Ser, Thr, Asn, Gln, and Cys. Gly and Pro can also be classified as "amino acids that affect the direction of the main chain," while amino acids containing a sulfur molecule in the side chain, Cys and Met, can also be classified as "sulfur-containing amino acids." As used herein, "amino acid" includes not only natural amino acids but also unnatural amino acids. Unnatural amino acids include, for example, N-alkylamino acids in which the above-described natural amino acids are N-alkylated, and amino acids in which the nitrogen atom forming the peptide bond is modified with a branched or unbranched lower (e.g., C1-C5, preferably C1-C3, more preferably C1) alkyl group. N-Alkylamino acids are preferably N-ethylamino acids, N-butylamino acids, or N-methylamino acids, and more preferably N-methylamino acids. In addition, unnatural amino acids include D-amino acids (also referred to as D-amino acids), β-amino acids, γ-amino acids, amino acid mutants, chemically modified amino acids such as amino acid derivatives, and amino acids that do not become protein building blocks in vivo, such as norleucine and ornithine. Furthermore, natural amino acids include amino acids to which a functional group has been added or which have been substituted with another functional group (for example, amino acids having a substitution or addition in an arylene group, alkylene group, or other portion of the side chain, amino acids with an increased C number in the arylene group, alkylene group, or alkyl group in the side chain, amino acids having a substitution in the aromatic ring of the side chain, and heterocyclized or condensed cyclized amino acids). The addition or substitution of a structure such as a functional group to the side chain of a natural amino acid can impart properties different from those of natural amino acids. For example, Dap is an amino acid having an amino group in the side chain of alanine, and due to the addition of this amino group, it exhibits the properties of a basic polar amino acid, unlike alanine, which belongs to the nonpolar amino acid group. That is, the aforementioned groups into which natural amino acids are divided based on the properties of their common side chains can include non-natural amino acids with similar side chain properties.For example, N-methylarginine (MeR), an amino acid in which the main chain nitrogen atom of arginine, a basic amino acid, is methylated, is an unnatural amino acid, but can be classified as a basic amino acid because it exhibits basicity. Thus, unnatural amino acids that exhibit side chain properties similar to those of a certain amino acid can also be included as targets for conservative amino acid substitution. Note that D-amino acids such as de (D-glutamic acid) can be classified as D-amino acids, but can also be classified according to the properties of their side chains, and N-methylamino acids can also be classified as N-alkylamino acids, or according to the properties of the side chains of the original amino acids that are not N-methylated. Non-naturally occurring amino acids include, but are not limited to, N-methyl amino acids, D-amino acids, and the like, and more specifically, da, de, dhgl, dq, dk, dyae, df, dkCOpipzaa, Tbg, 3Py6CON, 3Py6NH2, Hgl, aIT, Hgn, SMe, DabAc, KCOpipzaa, Meda, PeG, MeG, MedkCOpipzaa, Ahp, pHPeG, pMeOPeG, MsMeapG, 30MePeG, PpG, pFPeG, mC "Pharmaceutically acceptable salts thereof" refers to salts of any of the peptides. Examples of pharmaceutically acceptable salts include salts with mineral acids such as sulfuric acid, hydrochloric acid, and phosphoric acid; salts with organic acids such as acetic acid, oxalic acid, lactic acid, tartaric acid, fumaric acid, maleic acid, methanesulfonic acid, and benzenesulfonic acid; salts with amines such as trimethylamine and methylamine; and salts with metal ions such as sodium ion, potassium ion, and calcium ion. For compounds that have come to contain water over time, such water is also included in the pharmaceutically acceptable salts. The peptide may also be an isomer, such as a stereoisomer.A peptide may have one or more stereocenters, and these stereocenters may independently exist in either the (R) or (S) configuration. As used herein, the peptide may be optically active or racemic, and "may be an isomer" refers to racemic, optically active, positional, and stereoisomers, or a combination thereof. In one embodiment, the peptide may be a mixture of one or more isomers. The term "stereoisomer of a peptide" refers to a stereoisomer of the peptide. As used herein, the term "peptide" also includes its isomers unless otherwise specified. The peptide may also be a solvate. Solvation refers to the phenomenon in which ions generated by ionization of a solute molecule (peptide or conjugate) bind to and surround solvent molecules through electrostatic forces, hydrogen bonds, or the like, thereby diffusing the solute in a solvent. The type of solvent is not particularly limited. When the solvent is water, it is specifically referred to as a "hydrate." The following peptides are examples of peptides confirmed to have CA9 binding activity in the Examples herein: da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-S-3Py6NH2-HseMe-dk-Y (SEQ ID NO: 1); a peptide in which MeC, C, or MeCt is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1; and a peptide in which MeA, MeS, MeN, Hpr, G, or P is added as the 13th amino acid residue and MeG, G, da, or Meda is added as the 14th amino acid residue to the amino acid sequence of SEQ ID NO: 1. In one aspect, the peptide of the present invention has: (1) MeC, C, or MeCt added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1; or (2) MeA, MeS, MeN, Hpr, G, or P added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1, and further MeG, G, da, or Meda added as the 14th amino acid residue. The 13th amino acid residue is different between (1) and (2).In one embodiment, when the peptide of the present invention is a cyclic peptide, the number of amino acid residues contained in the cyclic structure may be, but is not limited to, 13 or 14, or may be more if additional amino acids are present at the termini. In one embodiment, the peptide of the present invention has the following structures: (in SEQ ID NO: 1) the first amino acid residue is da, dq, de, dhgl, or dk; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is S, Hgl, Hgl(PEG8Me), alT, Hgn, SMe, KCOpipzaa, or DabAc; the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa; the 7th amino acid residue is PeG, pMeOPeG, MsMeapG, 30MePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 40MePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the 8th amino acid residue is H, S, P, D, KCOpipzaa, Q(PEG8Me), P4Sh, Hse, SMe, Qmm, or Qdm; the 9th amino acid residue is 3Py6NH2, 5Inda, Y, or F40Me; the 10th amino acid residue is Ahp, HseMe, or E; and The 11th amino acid residue is dk, G, da, dq, dkCOpipzaa, dk(t4amCh), de, Acb, or dkAc. The above-mentioned options for the 1st to 12th amino acid residues may be selected in any combination. Non-limiting examples include one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more, nine or more, ten or more, or eleven or more of the above requirements. Preferably, all 12 of the above requirements are met.In one aspect, the peptide of the present invention has one of the following amino acid residues (in SEQ ID NO: 1): the first amino acid residue is da, dq, de, dhgl, or dk; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is S, Hgl, Hgl(PEG8Me), alT, Hgn, SMe, KCOpipzaa, or DabAc; and the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa. the 7th amino acid residue is PeG, pMeOPeG, MsMeapG, 30MePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 40MePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the 8th amino acid residue is H, S, P, D, KCOpipzaa, Q(PEG8Me), P4Sh, Hse, SMe, Qmm, or Qdm; the 9th amino acid residue is 3Py6NH2, 5Inda, Y, or F40Me; the 10th amino acid residue is Ahp, HseMe, or E; and The 11th amino acid residue is dk, G, da, dq, dkCOpipzaa, dk(t4amCh), de, Acb, or dkAc, and the 13th amino acid residue is MeC, C, or MeCt. Alternatively, the 14th amino acid residue is MeA, MeS, MeN, Hpr, G, or P. The 12th amino acid residue is MeG, G, da, or Meda. The 12th amino acid residues may be selected from any combination of the above-described options. The 12th amino acid residue may be selected from any combination of the above-described options. The 12th amino acid residue may be selected from any combination of the above-described options. Preferably, all of the above 12 requirements are met.In one embodiment, the peptide of the present invention satisfies one or more of the following requirements: the second amino acid residue (in SEQ ID NO: 1) is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe. The options in the above one embodiment for the first to tenth amino acid residues may be selected in any combination. Non-limiting examples include one or more, two or more, three or more, four or more, or five or more of the above requirements. Preferably, all six of the above requirements are satisfied. In one aspect, the peptide of the present invention satisfies one or more of the following requirements: (in SEQ ID NO: 1) the second amino acid residue is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe, and (1) MeC, C, or MeCt is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1; or (2) MeA, MeS, MeN, Hpr, G, or P is added as the 13th amino acid residue, and further MeG, G, da, or Meda is added as the 14th amino acid residue to the amino acid sequence of SEQ ID NO: 1. The options in the above one aspect for the 1st to 10th amino acid residues may be selected in any combination. The peptide of the present invention may satisfy, without limitation, one or more, two or more, three or more, four or more, or five or more of the above requirements. Preferably, the peptide satisfies all of the above six requirements. In one aspect, the peptide of the present invention has the following characteristics (in SEQ ID NO: 1): the second amino acid residue is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe.In one aspect, the peptide of the present invention has the following structure: (1) the second amino acid residue (in SEQ ID NO: 1) is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe; and (1) MeC, C or MeCt is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1; or (2) MeA, MeS, MeN, Hpr, G or P is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO: 1, and further MeG, G, da or Meda is added as the 14th amino acid residue. In one embodiment, the peptide of the present invention has the following structure: (in SEQ ID NO: 1) the first amino acid residue is de(PEG8Me), dk, dyae, or dkCOpipzaa; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is K, KCOpipzaa, Hgn(Qglucamine-NH2), Hgn(KCOpipzaa-NH2), or Qglucamine; and the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa; The 7th amino acid residue is PeG, pMeOPeG, MsMeapG, 30MePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 40MePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the 8th amino acid residue is K; the 9th amino acid residue is 3PyNH, 5Inda, Y, or F40Me; the 10th amino acid residue is Ahp, HseMe, or E; and the 11th amino acid residue is dk(F) or dk(PEG8c). The options in the above one aspect for the 1st to 12th amino acid residues may be selected in any combination. Non-limiting examples include one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more, nine or more, ten or more, and eleven or more of the above requirements.Preferably, all of the above 12 requirements are satisfied. Furthermore, in one embodiment, the peptide of the present invention may further modify the amino acids contained therein. Modification, for example, refers to the attachment of another compound to the side chain terminal of an amino acid. For example, the side chain terminal of lysine, aspartic acid, glutamic acid, arginine, glutamine, tyrosine, etc. may be attached to a low-molecular-weight or medium-molecular-weight compound such as PEG or a sugar chain, or may be attached to another amino acid. In one embodiment, the peptide is a cyclic peptide. A "cyclic peptide" refers to a peptide in which two amino acids are bonded together, and all or part of the peptide is cyclic. The peptide also includes peptides in which the amino acids in the peptide form a crosslinked structure, peptides in which a cyclic structure is formed by lactam ring formation or macrocyclization, and peptides having a lasso peptide-like structure. That is, the cyclic peptide may be any peptide in which a portion thereof forms a cyclic structure, and may also have a linear portion. Peptides generally have problems such as poor metabolic stability in vivo and difficulty permeating cell membranes due to their large size. To address these issues, peptide cyclization has been proposed. Cyclization of peptides improves protease resistance and metabolic stability, and also restricts conformational changes, increasing rigidity and improving membrane permeability and affinity for target proteins. In one embodiment, the peptide has a cyclic structure formed by bonding a chloroacetylated amino acid (preferably the N-terminal amino acid (the first amino acid residue)) to a cysteine ​​residue (including cysteine ​​substitutions such as N-methylcysteine) contained in the peptide. In one embodiment, the peptide has a cyclic structure formed by bonding the N-terminal amino acid (the first amino acid residue) to a cysteine ​​residue (including an optionally substituted cysteine ​​residue or a compound containing an -SH group within the structure) contained in the peptide. In another embodiment, the peptide has a cyclic structure formed by bonding the N-terminal amino acid (the first amino acid residue) to a cysteine ​​residue (including cysteine ​​substitutions such as N-methylcysteine) contained in the peptide.In one embodiment, the peptide has a cyclic structure formed by bonding a chloroacetylated N-terminal amino acid (the first amino acid residue) to the 13th cysteine ​​residue contained in the peptide or a -SH group contained in a compound (group) having an -SH group. Examples of compounds (groups) having an -SH group include MeCt. "Chloroacetylation" may be "halogen acetylation" using another halogen. "Acetylation" may also be "acylation" using an acyl group other than an acetyl group. In one embodiment, the peptide has a cyclic structure formed by bonding a chloroacetylated first amino acid residue of the amino acid sequence of SEQ ID NO: 1 to a cysteine ​​residue contained in the peptide. In another embodiment, the peptide may have a structure formed by bonding an amino acid sequence set forth in any one of SEQ ID NOs: 1 to 103 to a cysteine ​​or a substituted cysteine ​​contained in the peptide via an acetyl group. That is, for example, in this specification, a "cyclic peptide consisting of SEQ ID NO: XX" also includes the amino acid sequence represented by SEQ ID NO: XX and a cyclic structure formed by bonding an acetyl group bound to the first amino acid in the amino acid sequence and S (sulfur atom) contained in cysteine ​​or a substituted derivative thereof and a compound having an -SH group. In this specification, some amino acids may be modified to cyclize the peptide. Such partially modified amino acids are also encompassed. For example, as described above, a chloroacetyl group (ClAc group) may be added to the N-terminal amino acid, and the modified amino acid may be bonded to a cysteine ​​residue or an amino acid residue having an -SH group in the peptide to form a cyclized peptide. Various (natural / unnatural) amino acids to which a chloroacetyl group has been added are also encompassed by the amino acids of this application. In one aspect, the peptide has a cyclic structure formed by bonding the N-terminal amino acid (the first amino acid residue) and the C-terminal amino acid (the amino acid at the most C-terminal position when an amino acid residue such as the 13th or 14th amino acid residue is added to the C-terminal side of the amino acid sequence of SEQ ID NO: 1). In one embodiment, the peptide has a cyclic structure in which the amino group of the N-terminal amino acid (the first amino acid residue) is bonded to the carboxyl group of the 13th amino acid contained in the peptide.In one embodiment, an additional amino acid may be added to the 13th amino acid residue, forming a cyclic structure in which the N-terminal amino acid (the first amino acid residue) is bonded to a structure in which an additional amino acid residue is added to the 13th amino acid residue, for example, the 14th or 15th amino acid residue. In one embodiment, the peptide has a cyclic structure in which the amino group of the first amino acid residue in the amino acid sequence of SEQ ID NO: 1 contained in the peptide is bonded to the carboxy group of the 14th amino acid residue. In another embodiment, the peptide has a cyclic structure in which the amino group of the N-terminal amino acid (the first amino acid residue) is bonded to a functional group present at the end of the side chain of the C-terminal amino acid contained in the peptide. In one embodiment, the peptide comprises or consists of an amino acid sequence set forth in any one of SEQ ID NOs: 2-54. In one embodiment, the peptide is a cyclic peptide comprising or consisting of an amino acid sequence set forth in any one of SEQ ID NOs: 2-54. The peptide is a peptide consisting of an amino acid sequence set forth in any one of SEQ ID NOS: 2-54, or a peptide consisting of an amino acid sequence in which 1-13 or 14 (preferably 1-8, 1-7, 1-6, 1-5, 1-4, 1-3, 2, or 1) amino acid residues have been substituted, deleted, inserted, or added. Regarding sequences in which amino acid residues have been added, a sequence of many additional amino acid residues (e.g., 1-14 residues) may be added as long as the additional portion is a linker. Furthermore, peptides consisting of amino acid sequences in which these amino acid residues have been substituted, deleted, inserted, or added preferably have, for example, CA9 binding activity. Furthermore, in one embodiment, the peptide comprises or consists of an amino acid sequence set forth in any one of SEQ ID NOS: 55-103. In one embodiment, the peptide is a cyclic peptide comprising or consists of an amino acid sequence set forth in any one of SEQ ID NOS: 55-103. The peptide is a peptide consisting of the amino acid sequence set forth in any one of SEQ ID NOs: 55-103, or a peptide consisting of an amino acid sequence in which 1-13 or 14 (preferably 1-8, 1-7, 1-6, 1-5, 1-4, 1-3, 2 or 1) amino acid residues have been substituted, deleted, inserted or added.In addition, as for sequences to which amino acid residues have been added, as long as the additional portion is a linker, a sequence of many amino acid residues (e.g., 1-14 residues) may be further added. Furthermore, peptides consisting of amino acid sequences in which these amino acid residues have been substituted, deleted, inserted, or added preferably have, for example, CA9 binding activity. In one aspect, the peptides of the present invention do not include peptides comprising or consisting of SEQ ID NO: 103. Furthermore, in one aspect, the peptides comprise or consist of the amino acid sequence set forth in any one of SEQ ID NOs: 55-102. In one aspect, the peptides are cyclic peptides comprising or consisting of the amino acid sequence set forth in any one of SEQ ID NOs: 55-103. The peptides may be peptides consisting of the amino acid sequence set forth in any one of SEQ ID NOs: 55-102, or peptides consisting of an amino acid sequence in which 1-13 or 14 (preferably 1-8, 1-7, 1-6, 1-5, 1-4, 1-3, 2, or 1) amino acid residues have been substituted, deleted, inserted, or added from the amino acid sequence set forth in SEQ ID NOs: 55-102. Furthermore, in one embodiment, the peptide may be a peptide consisting of the amino acid sequence set forth in SEQ ID NO: 2 or 21, or a peptide consisting of an amino acid sequence in which 1 to 13 or 14 (preferably 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 2, or 1) amino acid residues have been substituted, deleted, inserted, or added. The peptide may contain additional amino acid residues in addition to the amino acid sequence of SEQ ID NO: 1. Without limitation, the peptide may contain additional amino acid residues in addition to the amino acid sequence set forth in SEQ ID NO: 2-54, 55-102, or 55-103. The "additional amino acid residue" may be contained in a peptide forming a cyclic structure, or an additional amino acid residue may be added to the cyclic peptide in the form of a linker. In one embodiment, the additional amino acid residue may be added to the side chain of an amino acid residue contained in the cyclic peptide. The number of amide bonds (number of amino acids and length) of the peptide or peptide portion is not particularly limited. Furthermore, a linker may be added to the cyclic peptide.Examples of linkers include the aforementioned amino acid linkers (peptide linkers), chemical linkers, fatty acid linkers, nucleic acid linkers, and sugar chain linkers. They may also be complexes of chemical linkers and peptide linkers. Examples of chemical linkers include PEG linkers consisting of 1-24 ethylene glycol units. The linker may also be a fatty acid linker containing a divalent chemical moiety derived from a fatty acid. The amino acid (peptide) linker is a linker containing at least one amino acid, such as a glycine-rich peptide having the sequence [Gly-Gly-Gly-Gly-Ser]n (where n is 1, 2, 3, 4, 5, or 6) as described in U.S. Pat. No. 7,271,149, or a serine-rich peptide linker as described in U.S. Pat. No. 5,525,491. Also, amino acids such as K, dk, F, G, df, Nle, dnle, and t4amCh, or peptide linkers consisting of two or more linked amino acids, can be used. In peptide linkers, the bond between amino acids or between an amino acid and a chemical linker may be formed via the side chain of the amino acid. Addition of a linker may, without limitation, change the physical properties (e.g., solubility) of the peptide. The linker may be attached at any position. For example, it may be attached to an amino acid residue located at the C-terminus, or to an amino acid residue contained in a cyclic peptide. In one embodiment, the peptide contains a linker at its C-terminus. Preferably, it is attached to the side chain of an amino acid residue contained in a cyclic peptide, or to a compound having a Cys or —SH group or any amino acid residue located at the C-terminus, and more preferably, it is attached to the side chain of the first, fourth, eighth, or eleventh amino acid residue. In one embodiment, the peptide is a peptide to which a linker and / or a payload can be attached at the C-terminus of the peptide. In one aspect, the peptide is a peptide in which the first, fourth, eighth, or eleventh amino acid residue, or an amino acid residue or additional amino acid located on the C-terminal side is an amino acid residue to which a linker and / or a payload can be bound.The amino acid residue to which a linker and / or payload can be bound may be an amino acid residue having a functional group at the side chain terminal of the amino acid residue to which a linker and / or payload can be bound, or in the case of an amino acid residue located on the C-terminal side or an additional amino acid residue, an amino acid residue having a functional group at the side chain terminal or C-terminal of the amino acid residue to which a linker and / or payload can be bound. Payloads will be described later. In one aspect, the amino acid residue to which a linker and / or payload can be bound is represented by the following formula (II): [In formula (II), R １ is H or a C alkyl group; R ２ R2: C1-6 alkyl-NH—R ３、 C alkyl-C aryl-O—C alkyl-NH—R ３ , C alkyl-NH(═O)—CH(C alkylphenyl)-NH—R ３ , C alkyl-NH(=O)-CH(C alkyl)-NH-R ３ or C alkyl-NH(=O)-C cycloalkyl-C alkyl-NH-R ３ and R ３ , are H or any functional group. ３ is H or any functional group, including any functional group protected by a protecting group. ３Preferably, the peptide has a structure that allows a linker and / or a payload to be attached to the peptide. The structure that allows a linker and / or a payload to be attached may be, for example, a functional group such as an amide group, or may be a known functional group or compound used in binding compounds, such as an alkyne compound or an azide group used in click chemistry. The "protecting group" is not particularly limited, but includes, for example, an Fmoc (9-fluorenylmethyloxycarbonyl) group, a tertBu (tertiary butyl) group, an Alloc (allyloxycarbonyl) group, a Boc (tertiary butoxycarbonyl) group, etc. Furthermore, the peptide may form a multimer via a linker or the like. The number of peptides contained in the multimer is not limited. In one embodiment, the multimer is a dimer, trimer, tetramer, pentamer, hexamer, octamer, or higher. The multimer may contain multiple identical peptides or multiple different peptides. In one embodiment, the peptide preferably has CA9 binding activity. CA9 (Carbonic anhydrase IX, carbonic anhydrase-9) is one of 15 types of carbonic anhydrases. It is a homodimer transmembrane protein localized on the cell membrane and plays an important role in maintaining intracellular pH, etc. CA9 is known to be expressed under hypoxic conditions, particularly in tumors, cervix, uterine body, ovary, kidney, esophagus, lung, breast, brain, gastrointestinal tract, liver, pancreas, head and neck, salivary gland, body cavity, and certain cancers of the skin. Therefore, CA9 has been suggested to be a general marker for tumor hypoxia in many solid tumors. In addition, CA9 is known to be useful not only as a marker for evaluating the presence or absence of tumors and their malignancy, but also as a poor prognosis marker for cervical tumors, rectal tumors, breast tumors, lung tumors, and brain tumors. Unless otherwise specified, the term "CA9" or "CA-9" as used herein refers to carbonic anhydrase-9 found in mammals, preferably rodents such as mice, or primates such as humans. It more preferably refers to human CA9. Note that "human CA9" as used herein refers to the native CA9 found in humans (e.g., Gene ID: 768).It is known that the amino acid sequences of CA9 from humans, mice, rats, etc. are similar. As used herein, CA9 binding activity refers to specific binding to CA9, particularly human CA9. Unless otherwise specified, CA9 binding activity refers to binding activity to human CA9. The binding state of the peptide of the present invention to CA9 can be expressed, without limitation, using indicators such as the affinity constant K, dissociation constant K, binding rate constant K, and dissociation rate constant K. The affinity constant K and dissociation constant K are indicators of the binding affinity, i.e., the strength of binding, between two molecules in equilibrium, and the dissociation constant K is the reciprocal of the affinity constant K. A smaller value of the dissociation constant K indicates stronger binding. Meanwhile, the rate of binding / dissociation reaction between two molecules in equilibrium is indicated by the binding rate constant K and dissociation rate constant K determined by kinetic analysis, where K = k / k. Therefore, even when peptides exhibit the same dissociation constant KD, there are cases where they associate slowly but dissociate slowly (both k on and k off values ​​are small) and cases where they associate quickly and dissociate quickly (both k on and k off values ​​are large), and the binding retention states are completely different. The affinity constant K A , dissociation constant K D , binding rate constant k on , and dissociation rate constant k off , which indicate the binding state of the peptide to CA9, can be determined using any intermolecular interaction measurement method known to those skilled in the art. The binding state of the peptide to CA9 can be measured by known methods. For example, it can be measured by surface plasmon resonance spectroscopy (SPR). Surface plasmon resonance spectroscopy can be performed, for example, using a BIACORE system (Cytiva), a biosensor (biomolecular interaction analysis device). The K D dissociation constant is one indicator of the CA9 binding activity of the peptide. The lower the dissociation constant K D , the higher the binding activity (affinity). According to surface plasmon resonance spectroscopy, the dissociation constant KD for binding of the peptide to, for example, human CA9 is, but is not limited to, 50 nM or less, 30 nM or less, 20 nM or less, 15 nM or less, 10 nM or less, 8 nM or less, 6 nM or less, 5 nM or less, 4 nM or less, 3 nM or less, 2 nM or less, or 1 nM or less.The lower limit of the dissociation constant KD of the binding between the peptide and human CA9 is not particularly limited. Non-limiting examples of the dissociation constant KD of the peptide are 0.01 nM or more, 0.05 nM or more, 0.1 nM or more, 0.2 nM or more, 0.3 nM or more, 0.4 nM or more, and 0.5 nM or more. Non-limiting examples of the dissociation constant KD of the peptide are 0.01-50 nM, preferably 0.05-30 nM, more preferably 0.2-15 nM, particularly preferably 0.3-10 nM, and most preferably 0.4-5 nM. The binding of the peptide to CA9 can also be examined by other known methods for measuring binding ability, such as ELISA (enzyme-linked immunosorbent assay). ELISA can be performed, for example, by using CA9 beads and a peptide with an HA tag sequence added to its C-terminus to examine binding activity. Alternatively, the peptide can be examined using, for example, FACS (fluorescence-activated cell sorting). Preferably, but not exclusively, the bond between the peptide and CA9 is a non-covalent bond. In one embodiment, the peptide has a cyclic structure as shown in the peptide portion of the chemical formula in Examples 1-1 to 1-16 and 11-1 to 11-5. Peptides with CA9-binding activity are useful for evaluating, diagnosing, and treating various diseases involving CA9. In one embodiment, the present invention relates to the peptide having CA9-binding activity. In another embodiment, the present invention relates to the use of the peptide for binding to CA9. In another embodiment, the present invention relates to the peptide used for binding to CA9. In the present invention, the binding of the peptide of the present invention to CA9 is in vitro or in vivo. The matters described in other sections also apply to this section unless otherwise specified. 3. Production of Peptides The peptides of the present invention can be produced by any known method for peptide production, for example, as follows. Unless otherwise specified, the items described in other sections also apply to this section. Chemical synthesis methods such as liquid phase methods, solid phase methods, and hybrid methods that combine liquid phase and solid phase methods; genetic recombination methods, etc.The solid-phase method involves, for example, esterifying the hydroxyl group of a hydroxyl-containing resin with the carboxyl group of a first amino acid (usually the C-terminal amino acid of the target peptide) whose α-amino group is protected with a protecting group. Known dehydration condensation agents such as 1-mesitylenesulfonyl-3-nitro-1,2,4-triazole (MSNT), dicyclohexylcarbodiimide (DCC), and diisopropylcarbodiimide (DIC) can be used as the esterification catalyst. Next, the protecting group of the α-amino group of the first amino acid is removed, and a second amino acid in which all functional groups except the carboxyl group of the main chain are protected is added, activating the carboxyl group, and bonding the first and second amino acids. Furthermore, the α-amino group of the second amino acid is deprotected, and a third amino acid in which all functional groups except the carboxyl group of the main chain are protected is added, activating the carboxyl group, and bonding the second and third amino acids. This process is repeated until a peptide of the desired length is synthesized, and all functional groups are deprotected. Examples of resins for solid-phase synthesis include Merrifield resin, MBHA resin, Cl-Trt resin, SASRIN resin, Wang resin, Rink amide resin, HMFS resin, Amino-PEGA resin (Merck), and HMPA-PEGA resin (Merck). These resins can be used after washing with a solvent (dimethylformamide (DMF), 2-propanol, methylene chloride, etc.). Examples of protecting groups for α-amino groups include benzyloxycarbonyl (Cbz or Z) group, tert-butoxycarbonyl (Boc) group, 9-fluorenylmethyloxycarbonyl (Fmoc) group, benzyl group, allyl group, and allyloxycarbonyl (Alloc) group. The Cbz group can be deprotected by hydrofluoric acid, hydrogenation, etc., the Boc group can be deprotected by trifluoroacetic acid (TFA), and the Fmoc group can be deprotected by treatment with piperidine or pyrrolidine. The α-carboxy group can be protected using, for example, a methyl ester, ethyl ester, allyl ester, benzyl ester, tert-butyl ester, cyclohexyl ester, etc. The carboxy group can be activated using a condensing agent.Condensing agents include, for example, dicyclohexylcarbodiimide (DCC), diisopropylcarbodiimide (DIC), 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC or WSC), (1H-benzotriazol-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate (BOP), and 1-[bis(dimethylamino)methyl]-1H-benzotriazolium-3-oxide hexafluorophosphate (HBTU). Cleavage of the peptide chain from the resin can be achieved by treatment with an acid such as TFA or hydrogen fluoride (HF). Production of peptides by recombinant DNA (translation synthesis) can be achieved using nucleic acids encoding the peptides. The nucleic acids encoding the peptides may be DNA or RNA. The nucleic acids encoding the peptides can be prepared by known methods or methods equivalent thereto. For example, they can be synthesized using an automated synthesizer. Restriction enzyme recognition sites may be added to insert the resulting DNA into a vector. Alternatively, a base sequence encoding an amino acid sequence for excising the resulting peptide chain using an enzyme or the like may be incorporated. To prevent degradation by proteases derived from the host, a chimeric protein expression method can be used in which the peptide of interest is expressed as a chimeric peptide with another peptide. In this case, the nucleic acid used is a nucleic acid encoding the peptide of interest and a peptide that binds to it. An expression vector is then prepared using the nucleic acid encoding the peptide. The nucleic acid can be inserted downstream of the promoter of the expression vector either directly or after digestion with a restriction enzyme or after the addition of a linker.Examples of vectors include Escherichia coli-derived plasmids (pBR322, pBR325, pUC12, pUC13, pUC18, pUC19, pUC118, pBluescript II, etc.), Bacillus subtilis-derived plasmids (pUB110, pTP5, pC1912, pTP4, pE194, pC194, etc.), yeast-derived plasmids (pSH19, pSH15, YEp, YRp, YIp, YAC, etc.), bacteriophages (e phage, M13 phage, etc.), viruses (retrovirus, vaccinia virus, adenovirus, adeno-associated virus (AAV), cauliflower mosaic virus, tobacco mosaic virus, baculovirus, etc.), cosmids, etc. The promoter can be selected appropriately depending on the type of host. When the host is an animal cell, for example, a promoter derived from SV40 (simian virus 40) or a promoter derived from CMV (cytomegalovirus) can be used. When the host is Escherichia coli, a trp promoter, a T7 promoter, a lac promoter, etc. can be used. The expression vector can also incorporate, for example, a DNA replication origin (ori), a selection marker (antibiotic resistance, auxotrophy, etc.), an enhancer, a splicing signal, a poly(A) addition signal, a nucleic acid encoding a tag (FLAG, HA, GST, GFP, etc.). Next, an appropriate host cell is transformed with the expression vector. The host can be appropriately selected in relation to the vector. Examples of hosts that can be used include Escherichia coli, Bacillus subtilis, Bacillus sp., yeast, insects or insect cells, and animal cells. Examples of animal cells that can be used include HEK293T cells, CHO cells, COS cells, myeloma cells, HeLa cells, and Vero cells. Transformation can be performed according to known methods, such as lipofection, calcium phosphate, electroporation, microinjection, and particle gun methods, depending on the type of host. The transformant is cultured according to standard methods to express the desired peptide. Peptide purification from a culture of the transformant involves recovering the cultured cells, suspending them in an appropriate buffer, disrupting the cells by methods such as sonication or freeze-thawing, and obtaining a crude extract by centrifugation or filtration.If the peptide is secreted into the culture medium, the supernatant is collected. Purification from the crude extract or culture supernatant can also be performed by known methods or methods equivalent thereto (e.g., salting out, dialysis, ultrafiltration, gel filtration, SDS-PAGE, ion exchange chromatography, affinity chromatography, reverse-phase high-performance liquid chromatography, etc.). The obtained peptide may be converted from a free form to a salt, or from a salt to a free form, by known methods or methods equivalent thereto. In one embodiment, the translation synthesis system may be a cell-free translation system. Cell-free translation systems generally allow expression products to be obtained in a highly pure form without purification. Cell-free translation systems contain, for example, ribosomal proteins, aminoacyl-tRNA synthetases (ARS), ribosomal RNA, amino acids, rRNA, GTP, ATP, translation initiation factors (IFs), elongation factors (EFs), release factors (RFs), and ribosome recycling factors (RRFs), as well as other factors necessary for translation. Escherichia coli extract or wheat germ extract may be added to improve expression efficiency. Alternatively, rabbit erythrocyte extract or insect cell extract may be added. Continuously supplying energy to a system containing these using dialysis allows for the production of proteins in amounts ranging from several hundred μg to several mg / mL, without limitation. A system containing RNA polymerase may also be used to simultaneously perform transcription from gene DNA. Commercially available cell-free translation systems include systems derived from Escherichia coli, such as Roche Diagnostics' RTS-100 (registered trademark), GeneFrontier's PURESYSTEM, and New England Biolabs' PUREExpress In Vitro Protein Synthesis Kit, and systems using wheat germ extract, such as those from Zoigene and CellFree Sciences. In a cellular translation system, instead of the aminoacyl-tRNA synthesized by a natural aminoacyl-tRNA synthetase, an artificial aminoacyl-tRNA in which a desired amino acid or hydroxy acid is linked (acylated) to the tRNA may be used. Such an aminoacyl-tRNA can be synthesized using an artificial ribozyme.Such ribozymes include flexizymes (H. Murakami, H. Saito, and H. Suga, (2003), Chemistry & Biology, Vol. 10, 655-662; and WO 2007 / 066627, etc.). Flexizymes are also known as the original flexizyme (Fx), and modified versions thereof, such as dinitrobenzyl flexizyme (dFx), enhanced flexizyme (eFx), and aminoflexizyme (aFx). By using a tRNA produced by flexizyme to which a desired amino acid or hydroxy acid is linked, a desired codon can be translated in association with the desired amino acid or hydroxy acid. A non-standard amino acid may also be used as the desired amino acid. For example, the unnatural amino acid required for the above-mentioned cyclization can also be introduced into a binding peptide using this method. The chemical synthesis of the peptide can be performed using various methods commonly used in the art, including, for example, stepwise solid-phase synthesis, semi-synthesis of peptide fragments via conformationally assisted religation, and chemical ligation.The synthesis of the peptide is performed using various solid-phase techniques, such as those described in K. J. Jensen, P. T. Shelton, and S. L. Pedersen, Peptide Synthesis and Applications, 2nd Edition, Springer, 2013.A preferred strategy is based on the combination of an Fmoc group, which temporarily protects the α-amino group and allows selective base removal, and a protecting group, which temporarily protects side chain functional groups and is stable under Fmoc removal conditions.Selection of such general peptide side chains is described in the aforementioned Peptide Synthesis and Applications, 2nd Edition, and G. B. Fields and R. L. Noble, "Solid Phase Peptide Synthesis Utilizing 9-Fluorenylmethoxycarbonyl Amino Acids," Int. J. Peptide Protein Res. 35, 1990, 161-214, etc., and preferred peptide side chain protecting groups include, for example, a benzyl group, a tert-butyl group, and a trityl (Trt) group for the hydroxy group of serine or threonine, a 2-bromobenzyloxycarbonyl group and a tert-butyl group for the hydroxy group of tyrosine, a Boc group, a methyltetrazolethiol (Mtt) group, an Alloc group, and an ivDde group for the amino group of lysine side chain, and a methyltetrazolethiol (Mtt) group for the imidazole group of histidine. Examples of suitable protecting groups include Trt and Boc groups for the C-terminal amino acid, 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl (Pbf) group for the guanidyl group of arginine, tert-butyl, allyl, and 3-methylpentane (Mpe) groups for the carboxyl groups of glutamic acid and aspartic acid, Trt groups for the carboxamide groups of glutamine and asparagine, and Trt and monomethoxytrityl (Mmt) groups for the thiol group of cysteine. The peptides can be synthesized in a stepwise manner on the solid-phase resin described above. The α-amino protecting groups of the C-terminal amino acid and all amino acids and peptides used in the synthesis must be selectively removed during the synthesis process. Preferably, the solid-phase resin described above is used, and the process begins by converting the C-terminal carboxyl group of a peptide whose N-terminus is appropriately protected with an Fmoc group or the C-terminal carboxyl group of an amino acid protected with an Fmoc group into an activated ester with an appropriate reagent, followed by addition to an amino group on the solid-phase resin. Subsequent peptide chain elongation can be achieved by sequentially repeating the removal of the N-terminal protecting group (Fmoc group) and the condensation of a protected amino acid derivative according to the amino acid sequence of the target peptide. Note that these procedures can liberate the target peptide at the final stage.For example, the release can be achieved using a TFA solution containing water / silyl hydride / thiol as a scavenger in TFA, as described in Teixeira, W. E. Benckhuijsen, P. E. de Koning, A. R. P. M. Valentijn, J. W. Drijfhout, Protein Pept. Lett., 2002, 9, 379-385. A typical example is TFA / Water / TIS / DODT (volume ratio 92.5:2.5:2.5:2.5). The peptides described herein can be synthesized using a single- or multi-channel peptide synthesizer, such as a CEM Liberty Blue synthesizer or a Biotage Syro I synthesizer or their successors. Activation of the carboxyl group can be achieved using a condensing agent. Examples of condensing agents include dicyclohexylcarbodiimide (DCC), diisopropylcarbodiimide (DIPCDI), 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC or WSC), (1H-benzotriazol-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate (BOP), and 1-[bis(dimethylamino)methyl]-1H-benzotriazolium-3-oxide hexafluorophosphate (HBTU). Peptide cyclization can be achieved using known methods. For example, by designing a peptide to contain two or more cysteine ​​residues, a cyclic structure can be formed by a disulfide bond after translation. Alternatively, according to the method of Goto et al. (Y. Goto, et al. ACS Chem. Biol. 3 120-129 (2008)), cyclization can also be achieved by synthesizing a peptide with a chloroacetyl group at the N-terminus and placing a cysteine ​​residue containing a sulfur molecule in the peptide using genetic code reprogramming technology. This allows spontaneous nucleophilic attack of the mercapto group on the chloroacetyl group after translation, resulting in cyclization of the peptide through a thioether bond. Using genetic code reprogramming technology, other combinations of amino acids that bond to form a ring can also be placed in the peptide for cyclization.Alternatively, cyclization may be achieved by placing an L-2-aminoadipic acid residue in the peptide and bonding it to the N-terminal main chain amino group. Alternatively, cyclization may be achieved by bonding the amide group of the N-terminal amino acid residue with the carboxy group of the C-terminal amino acid residue via an amide bond. Cyclization may also be achieved by bonding the amino group of the N-terminal amino acid (the first amino acid residue) with a functional group present at the end of the side chain of the C-terminal amino acid contained in the peptide. As described above, any known cyclization method can be used without particular limitations. The matters described in other sections also apply to this section unless otherwise specified. 4. Conjugates (Complexes) The present invention relates to complexes comprising a peptide and a payload (also referred to as "peptide conjugates," "peptide complexes," or simply "conjugates"), or pharmaceutically acceptable salts thereof. As explained in "2. Peptides," the peptides in the conjugates may take any form (including salts, isomers, solvates, etc.). As used herein, reference to a "peptide conjugate," "conjugate," or "peptide complex" also includes reference to pharmaceutically acceptable salts, isomers, or solvates thereof, unless otherwise stated. In one aspect, the conjugate of the present invention refers to a complex in which the peptide of the present invention and a payload are bound, with or without a linker. In one aspect, the conjugate of the present invention is bound, with or without a linker, to the side chain of an amino acid residue contained in the peptide of the present invention. In one aspect, the conjugate of the present invention is bound to any payload, with or without a linker, to the 13th amino acid residue of SEQ ID NO: 1. In one aspect, the conjugate of the present invention is bound to the 1st, 4th, 8th, or 11th amino acid residue of SEQ ID NO: 1, as shown in the following formula (I). [In formula (I), R １ is H or a C alkyl group; R ２is C alkyl-NH—, C alkyl-C aryl-O—C alkyl-NH—, C alkyl-NH(═O)—CH(C alkylphenyl)-NH—, C alkyl-NH(═O)—CH(C alkyl)-NH—, or C alkyl-NH(═O)—C cycloalkyl-C alkyl-NH—; and X is any payload. ２ C1-6 alkyl-NH- is a residue in the residue of K and a modified form in which an alkyl chain is elongated in the side chain of K; C1-6 alkyl-C6 aryl-O-C1-3 alkyl-NH- is a residue in the residue of dyae and a modified form in which an alkyl chain is elongated in the side chain of dyae; C1-6 alkyl-NH(=O)-CH(C1-6 alkylphenyl)-NH- is a residue in a compound in which a residue of dk-df and a modified form in which an alkyl chain is elongated in the side chain of dk are combined with a modified form in which an alkyl chain is elongated in the side chain of df; C1-6 alkyl-NH (=O)-CH(C1-6 alkyl)-NH- is a residue in a compound in which a modified dk-dnle residue and a modified dk residue in which the alkyl chain is elongated in the side chain are combined with a modified dnle residue in which the alkyl group is elongated or shortened in the side chain of dnle, and C1-6 alkyl-NH(=O)-C3-8 cycloalkyl-C1-3 alkyl-NH- is a residue in a compound in which a modified dk-t4amCh residue and a modified dk residue in which the alkyl chain is elongated in the side chain are combined with a modified t4amCh residue in which the number of carbon atoms contained in the cycloalkyl structure is increased or decreased. indicates that the carboxy group or amide group is bonded to the amide group or carboxy group of an adjacent amino acid residue in the amino acid sequence. As used herein, C1-3 alkyl refers to a monovalent group derived by removing any one hydrogen atom from a linear or branched saturated aliphatic hydrocarbon having 1 to 3 carbon atoms. Specific examples include methyl, ethyl, n-propyl, isopropyl, etc. As used herein, C1-6 alkyl refers to a monovalent group derived by removing any one hydrogen atom from a linear or branched saturated aliphatic hydrocarbon having 1 to 6 carbon atoms. Specific examples include methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, t-butyl, 1-methylpropyl, n-pentyl, isopentyl, 2-methylbutyl, 1,1-dimethylpropyl, 1-ethylpropyl, hexyl, 4-methylpentyl, etc. As used herein, C alkylphenyl refers to a structure in which a phenyl group is bonded to a monovalent group derived by removing one arbitrary hydrogen atom from a linear or branched saturated aliphatic hydrocarbon having 1 to 6 carbon atoms. As used herein, C cycloalkyl refers to a monovalent group derived by removing one arbitrary hydrogen atom from a cyclic saturated aliphatic hydrocarbon having 3 to 8 carbon atoms. The term "conjugate" as used herein includes, but is not limited to, the conjugates shown in Conjugate Nos. 1-81, for example, the conjugates shown in Conjugate Nos. 1-69 and 74-81, and also includes conjugates in which the payload contained in these conjugates is replaced with a different payload.Conjugates substituted with different payloads include, for example, conjugates with Conjugate No. shown in Table 8 or Table 18. Conjugates in which the payloads in Conjugate Nos. 1-81 (in one embodiment, Conjugate Nos. 1-69 and 74-81) such as DOTA, DOTALu, SulfoCy5, DOTAZr, DOTALu-df, DOTALu-dnle, DOTALu-t4amCh, DOTALu-F, DOTALu-Nle, SulfoCy5-PEG8c, DOTACu, DOTAGA, dDOTAGA, rNOTAGA, DOTA-#Ga (representing DOTA bound to Ga (gallium)), and DOTALa (representing DOTA bound to La (lanthanum)) are replaced with different payloads may be used. For example, Conjugate Nos. In the conjugate described in Conjugate No. 1, the payload sulfoCy5 bound to the linker G-PEG10c-K may be a chelating agent such as DOTA, or a conjugate in which a radioactive element is further bound to the chelating agent such as DOTA, or a conjugate in which SulfoCy5 is bound to a payload that is not a radioisotope, such as an antibody. Furthermore, for example, in the conjugate described in Conjugate No. 2, the payload chelating agent DOTA bound via the linker K may be a conjugate in which a radioactive isotope is further bound to the chelating agent DOTA, or, for example, in the conjugate described in Conjugate No. 4, the payload chelating agent DOTA bound via the linker K may be a conjugate in which Lu (non-radioactive lutetium) is the radioactive isotope instead of non-radioactive lutetium. １７７The payload may be a conjugate to which Lu is bound. Payload In the present invention, the term "payload" refers to a known functional molecule. The term "functional molecule" is not particularly limited and refers to a molecule that exhibits a desired function by binding to or acting on a target. In one embodiment, the desired function includes a pharmacologically active function, a labeling function, or a delivery function to a target site. In this specification, the term "payload" includes pharmacologically active compounds, labeling compounds, fluorescent substances, peptides, proteins, nucleic acids, and molecules used in drug delivery systems, and the molecules may be low-molecular-weight compounds, medium-molecular-weight compounds, or high-molecular-weight compounds. In this specification, the term "pharmacologically active compound" refers to a compound having pharmacological activity. The pharmacologically active compound is preferably, for example, an antibody, protein, or nucleic acid, which is a high-molecular-weight compound having pharmacological activity, or a peptide, which is a medium-molecular-weight compound, or a low-molecular-weight compound. The payload may also be a compound in which a low-molecular-weight compound having pharmacological activity is encapsulated in a liposome, micelle, or the like. In this specification, the term "payload" also includes any cytotoxic agent that is toxic to cells and, in particular, kills cells. Examples include, but are not limited to, taxol, cytochalasin B, gramicidin D, ethidium bromide, emetine, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, doxorubicin, daunorubicin, dihydroxyanthracin dione, mitoxantrone, mithramycin, actinomycin D, 1-dehydrotestosterone, glucocorticoids, procaine, tetracaine, lidocaine, propranolol, and puromycin, and analogs or homologs thereof. Furthermore, the "payload" in this specification includes therapeutic agents having anticancer activity, for example, antimetabolites (e.g., methotrexate, 6-mercaptopurine, 6-thioguanine, cytarabine, fludarabine, 5-fluorouracil decarbazine), alkylating agents (e.g., mechlorethamine, thioepa, chlorambucil, melphalan, carmustine (BSNU) and lomustine (CCNU), cyclophosphamide, busulfan, dibromomannitol, streptozotocin, mitomycin C, and cis-dichlorodiamineplatinum(II) (DDP) cisplatin), anthracyclines (e.g.,Antibiotics include, but are not limited to, daunorubicin (formerly known as "daunomycin") and doxorubicin), antibiotics (e.g., dactinomycin (formerly known as "actinomycin"), bleomycin, mithramycin, and anthramycin (AMC), and antimitotic agents (e.g., vincristine and vinblastine). In a preferred embodiment, the therapeutic agent is a cytotoxic agent. In another embodiment, the therapeutic agent is an immunosuppressant. In yet another embodiment, the therapeutic agent is GM-CSF. In a preferred embodiment, the therapeutic agent is doxorubicin, cisplatin, bleomycin sulfate, carmustine, chlorambucil, cyclophosphamide, or ricin A. As used herein, a labeled compound refers to a compound labeled with a dye, a fluorescent substance, a tag, or a radioisotope. Among these, a compound labeled with a radioisotope refers to a compound in which a low-molecular-weight compound, a medium-molecular-weight compound, an antibody, or the like is labeled with a radioisotope. The labeled compound may also be a dye, a fluorescent substance, a tag, or the radioisotope itself. The radioisotope may be coordinately bonded to a chelating agent such as DOTA. In this specification, the radioisotope may be a known radioisotope. In one embodiment, the radioisotope is actinium-225, actinium-227 (225Ac, 227Ac), astatine-211 (211At), bismuth-212 and bismuth-213 (212Bi, 213Bi), copper-61, copper-62, copper-64 and copper-67 (61Cu, 62Cu, 64Cu, 67Cu), gallium-64, gallium-67 and gallium-68 (64Ga, 67Ga and 68Ga), indium-111 (111In), iodine-123, iodine-1 24, iodine-125 or element-131 (123I, 124I, 125I, 131I) (123I), lead-203, lead-212 (203Pb, 212Pb), ruthenium-97 (97Ru), lutetium-177 (177Lu), radium-223 (223Ra), samarium-153 (153Sm), scandium-44 and scandium-47 (44Sc, 47Sc), iron-52 (52Fe), arsenic-72, arsenic-76 (72As, 76As), erbium-169 (169Er), strontium-89, strontium-90 (89Sr, 90Sr),Technetium-99 (99mTc), Technetium-94 (94mTc), Yttrium-86 and Yttrium-90 (86Y, 90Y), Chromium-51 (51Cr), Rhenium-186, Rhenium-188 (186Re, 188Re), Zirconium-89 (89Zr), Manganese-52, Manganese-51 (52Mn, 51Mn), Terbium-149, Terbium-152, Terbium-153, Terbium-154, Terbium-155, Terbium-156, Terbium-157, Terbium-158, Terbium-159 ... Rubium-155, Terbium-161 (149Tb, 152Tb, 155Tb, 161Tb), Ytterbium-169, Ytterbium-175 (169Yb, 175Yb), Rhodium-105 (105Rh), Dysprosium-166 (166Dy), Holminium-166 (166Ho), Samarium-153 (153Sm), Promotium-149, Promotium-151 (149Pm, 151Pm), thulium-172 (172Tm), tin-121 (121Sn), praseodymium-142, praseodymium-143 (142Pr, 143Pr), gold-198, gold-199 (198Au, 199Au), bromine-75, bromine-76, bromine-77, bromine-80, bromine-82 (75Br, 76Br, 77Br, 80Br, 82Br), fluorine-18 (18F), Examples of suitable chelating agents include candium-43, scandium-44, scandium-47 (Sc, Sc, Sc), astatine-211 (At), thorium-227, thorium-226 (Th, Th), lanthanum-140 (La), rubidium-82 (Rb), phosphorus-32 (P), silver-111 (Ag), erbium-165 (Er), etc. As used herein, the term "chelating agent" refers to an organic compound that binds with metal ions to form a cyclic complex in order to stably bind a radioisotope, particularly a metallic radioisotope. In one embodiment, the chelating agent is selected from the group consisting of EDTA (ethylenediaminetetraacetic acid), DPTA (diethylenetriaminepentaacetic acid), 1,4,8,11-tetraazatetradecane, 1,4,8,11-tetraazatetradecane-1,4,8,11-tetraacetic acid, 1-oxa-4,7,12,15-tetraazaheptadecane-4,7,12,15-tetraacetic acid,DOTAGA (α-(2-carboxyethyl)-1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid) (including the racemic rDOTAGA), TMT (6,6″-bis[N,N″,N′′-tetra(carboxymethyl)aminomethyl)-4′-(3-amino-4-methoxyphenyl)-2,2′:6′,2″-terpyridine), DOTA (1,4,7,10-tetraazacyclododecane-N,N″(N′″-tetraacetic acid), T CMC (tetra-primary amide of DOTA), DO3A (1,4,7,10-tetraazacyclododecane-1,4,7-tris(acetic acid)-10-(2-thioethyl)acetamide), CB-DO2A (4,10-bis(carboxymethyl)-1,4,7,10-tetraazabicyclo[5.5.2]tetradecane), NOTA (1,4,7-triazacyclononane-triacetic acid), Diamsar (3,6,10,13,16,19-hexaazabicyclo[6.6.6]eico 1,8-diamine), DTPA (pentetic acid or diethylenetriaminepentaacetic acid), CHX-A″-DTPA ([(R)-2-amino-3-(4-isothiocyanatophenyl)propyl]-trans-(S,S)-cyclohexane-1,2-diamine-pentaacetic acid), TETA (1,4,8,11-tetraazacyclotetradecane-1,4,8), 11-tetraacetic acid, Te2A (4,11-bis(carboxymethyl)-1,4,8,11-tetraazabicyclo[6.6]methyl]- 2]hexadecane), HBED, DFO (deferoxamine), DFOsq (DFO-squaramide), HOPO (3,4,3-(LI-1,2-HOPO), NODAGA (1,4,7-triazacyclononane-1-1 glutamic acid-4,7-acetic acid) (including the racemic form rNODAGA), and modifications thereof are also included. DOTA, DOTAGA, or NODAGA is preferred. Note that, when each chelating agent has an optical isomer, it includes such an optical isomer. In one aspect, the payload is preferably a radioisotope bound to a chelating agent. For example, but not limited to, a structure in which a radioisotope of lutetium is bound to DOTA, a structure in which a radioisotope of zirconium is bound to DOTA, or a structure in which a radioisotope of copper is bound to DOTA,Examples of such a structure include a structure in which a radioactive isotope of gallium is bound to DOTA. In one embodiment, the payload may be a radioactive isotope that is not bound to a chelating agent. The payload may be a compound used in evaluation methods or imaging using a radioactive isotope, and may be, for example, but not limited to, a known compound containing a radioactive isotope that is used as a radioligand imaging agent in positron emission tomography (PET) or SPECT, which will be described later. For example, but not limited to, 18F-fluorodeoxyglucose (18F-FDG), 15O—H2O, 11C-methionine, 11C-acetic acid, 11C-choline, 11C-raclopride, 11C-flumazenil, 13N-ammonia, 18F-sodium fluoride, 82Rn+ (82RbCl), 18F-flurpiridaz, 123I-IMP, 99mTc-ECD, 99Tc-HMPAO, 123I-iomazenil, 123I- Examples of the protein include iofulpane, In-DTPA, TcO (NaTcO), TcMIBI, TI (TICI), Tc-tetrofosmin, Tc-human serum albumin, O-adosterol, Tc-phytic acid, Y-zevalin, Ga (GaCHO), In-ibritumomab tiuxetan, and In-pentetreotide.

[0023] As used herein, the term "protein" refers to any protein present in a living body or exhibiting a useful function in the body, including, for example, proteins with pharmacological activity and proteins with molecular recognition activity. Specific examples include phebronectin, avidin, antibodies, proteins with Fc regions, immune checkpoint proteins, and enzymes such as proteases. As used herein, nucleic acids may be any polymer of nucleotides. Specific examples include DNA and RNA. As used herein, nucleic acids may be modified, such as 2'-methoxyethyl (MOE) modification, use of 2'-deoxynucleosides in RNA, phosphorothioate internucleoside linkages, phosphodiester internucleoside linkages, and conversion of cytosine to 5-methylcytosine. As used herein,A drug delivery system refers to a system that delivers an active ingredient into target cells. Examples include carriers such as water-soluble polymers, nano-sized particles (nanospheres), liposomes, and micelles. Drug delivery system (DDS) molecules may further contain drugs such as small molecules, proteins, peptides, nucleic acids, and vaccines. In one aspect, the present invention relates to the conjugate having CA9 binding activity. In another aspect, the present invention relates to the use of the conjugate for binding to CA9. In another aspect, the present invention relates to the conjugate used for binding to CA9. In this invention, the binding of the conjugate of the present invention to CA9 is in vitro or in vivo. The matters described in other sections also apply to this section unless otherwise specified. 5. Compositions, etc. The present invention also relates to compositions comprising the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention. The compositions include, but are not limited to, pharmaceutical compositions (medical compositions), diagnostic compositions, and research compositions. In one aspect, the pharmaceutical composition is a composition used in radiation therapy (one aspect of a therapeutic composition). The present invention also relates to an imaging agent comprising the conjugate of the present invention. The imaging agent may also be used as a diagnostic composition. In one aspect, the diagnostic composition is an imaging agent. The matters described in other sections also apply to this section unless otherwise specified. Pharmaceutical Composition In one aspect, the present invention relates to a pharmaceutical composition comprising the peptide, conjugate, or a pharmaceutically acceptable salt thereof. In one aspect, the pharmaceutical composition has CA9 binding activity. In one aspect, the pharmaceutical composition is a pharmaceutical composition for preventing or treating a CA9-associated disease or symptom. "CA9-associated disease or symptom" includes known CA9-associated diseases or symptoms. Examples include tumors, particularly malignant tumors, and solid cancers. In one aspect, examples of CA9-related diseases include tumors of the cervix and uterine body, breast, ovary, gastrointestinal tract (including the esophagus, stomach, small intestine, colon, and rectum), kidney, liver, gallbladder and biliary system, pancreas (including the pancreatic duct and exocrine pancreas), lung, head and neck, salivary gland, bladder and urinary tract, body cavity, and epithelial origin.Examples of cancers include cancers of the ovary, fallopian tube, peritoneum, vagina, vulva, penis, cervix, myometrium, endometrium, thyroid, adrenal gland, prostate, skin, and adnexa; hematological malignancies, borderline malignancies including premalignant hematological disorders and lymphoid hematological malignancies and related diseases; hematological malignancies and related diseases of myeloid lineage; tumors of mesenchymal origin; tumors of the central or peripheral nervous system; endocrine tumors; ocular and adnexal tumors; germ cell and trophoblastic tumors; pediatric and embryonal tumors; and others. Preferred tumors include, but are not limited to, renal cell carcinoma, head and neck cancer, urothelial cell carcinoma, pancreatic ductal carcinoma, and colorectal cancer. In one embodiment, the pharmaceutical composition is a composition used in radiation therapy (one embodiment of a therapeutic composition). In this case, the component contained in the pharmaceutical composition includes a radioisotope. Preferably, the pharmaceutical composition is a conjugate containing a radioisotope as a payload. Radiation therapy is a treatment that damages intracellular DNA in tumors, particularly cancer cells, by irradiating the affected area with radiation or administering a radioactive substance to the affected area, thereby killing the cells. The pharmaceutical composition may contain the peptide or conjugate itself, or a pharmaceutically acceptable salt, isomer, or solvate thereof. As used herein, "peptide" and "conjugate" may include a pharmaceutically acceptable salt, isomer, or solvate thereof, unless otherwise specified. The pharmaceutical composition preferably contains an effective amount of the peptide or conjugate as an active ingredient. The administration route of the pharmaceutical composition is not particularly limited herein and may be oral or parenteral. Examples of parenteral administration include injections such as intramuscular injection, intravenous injection, and subcutaneous injection, transdermal administration, and transmucosal administration (nasal, oral, ocular, pulmonary, vaginal, and rectal). The pharmaceutical composition may be modified in various ways, taking into account the susceptibility of polypeptides to metabolism and excretion. For example, polyethylene glycol (PEG) or sugar chains can be added to polypeptides to increase their blood retention time and reduce their antigenicity. Biodegradable polymer compounds such as polylactic acid glycol (PLGA), porous hydroxyapatite, liposomes, surface-modified liposomes, emulsions prepared with unsaturated fatty acids, nanoparticles, nanospheres, etc. can also be used as sustained-release bases.A polypeptide may be encapsulated in the composition. For transdermal administration, a weak current may be applied to the skin surface to allow penetration through the stratum corneum (iontophoresis). The pharmaceutical composition may contain the active ingredient as is, or may be formulated by adding pharmaceutically acceptable carriers, excipients, additives, etc. Examples of dosage forms include liquids (e.g., injections), dispersions, suspensions, tablets, pills, powders, suppositories, powders, fine granules, granules, capsules, syrups, lozenges, inhalants, ointments, eye drops, nasal drops, ear drops, and poultices. Formulation can be carried out by conventional methods using, for example, excipients, binders, disintegrants, lubricants, solubilizers, solubilizers, colorants, flavorings, stabilizers, emulsifiers, absorption enhancers, surfactants, pH adjusters, preservatives, antioxidants, and the like, as appropriate. Examples of ingredients used in formulations include, but are not limited to, purified water, saline, phosphate buffer, dextrose, glycerol, ethanol and other pharmaceutically acceptable organic solvents, animal and vegetable oils, lactose, mannitol, glucose, sorbitol, crystalline cellulose, hydroxypropyl cellulose, starch, corn starch, silicic anhydride, magnesium aluminum silicate, collagen, polyvinyl alcohol, polyvinylpyrrolidone, carboxyvinyl polymer, sodium carboxymethylcellulose, sodium polyacrylate, sodium alginate, water-soluble dextran, sodium carboxymethyl starch, pectin, methylcellulose, ethylcellulose, xanthan gum, gum arabic, tragacanth, casein, agar, polyethylene glycol, diglycerin, glycerin, propylene glycol, petrolatum, paraffin, octyldodecyl myristate, isopropyl myristate, higher alcohols, stearyl alcohol, stearic acid, human serum albumin, etc. In view of the fact that peptides are generally poorly absorbed transmucosally, the pharmaceutical composition may contain an absorption enhancer that improves the absorption of poorly absorbed drugs. Examples of such absorption enhancers include surfactants such as polyoxyethylene lauryl ethers, sodium lauryl sulfate, and saponin; bile salts such as glycocholic acid, deoxycholic acid, and taurocholic acid; chelating agents such as EDTA and salicylic acids; caproic acid, capric acid, lauric acid, oleic acid, linoleic acid,Fatty acids such as mixed micelles; enamine derivatives, N-acyl collagen peptides, N-acyl amino acids, cyclodextrins, chitosans, nitric oxide donors, etc. can be used. When the pharmaceutical composition is in the form of a pill or tablet, it may be coated with a sugar coating, gastric or enteric coating material. When the pharmaceutical composition is in the form of an injection, it may contain distilled water for injection, physiological saline, propylene glycol, polyethylene glycol, vegetable oil, alcohol, etc. Furthermore, wetting agents, emulsifiers, dispersants, stabilizers, solubilizers, solubilizers, preservatives, etc. may be added. Furthermore, the pharmaceutical composition may be intended not only for humans but also for non-human mammals or birds. Examples of non-human mammals include non-human primates (monkeys, chimpanzees, gorillas, etc.), livestock animals (pigs, cows, horses, sheep, etc.), dogs, cats, rats, mice, guinea pigs, rabbits, etc. The dosage, particularly when administered to humans, varies depending on the symptoms, the patient's age, sex, body weight, sensitivity, administration method, administration interval, type of active ingredient, and type of formulation, and can be, but is not limited to, 30 μg-100 g, 100 μg-500 mg, or 100 μg-100 mg, administered once or several times. In the case of injection, 1 μg / kg-3000 μg / kg or 3 μg / kg-1000 μg / kg may be administered once or several times depending on the patient's body weight. In one aspect, the present invention relates to a method for preventing or treating CA9-related diseases or symptoms by administering the peptide or conjugate of the present invention (including pharmaceutically acceptable salts, isomers, or solvates thereof). The treatment method of the present invention includes, but is not limited to, administering the peptide or conjugate of the present invention to a subject. The subjects and administration methods are the same as those described in the "Pharmaceutical Composition" section. Furthermore, the therapeutic method of the present invention aims to deliver the medicinal ingredient of the therapeutic method to any part of the subject (affected area) using the peptide or conjugate of the present invention, and includes, but is not limited to, a step of administering the peptide or conjugate of the present invention to a subject. In one aspect, the present invention relates to the use of the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention for the prevention or treatment of CA9-related diseases or symptoms. In another aspect, the present invention relates to the use of the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention for the prevention or treatment of CA9-related diseases or symptoms.and use of the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention for the manufacture of a pharmaceutical composition for the prevention or treatment of a CA9-related disease or condition. In one aspect, the present invention relates to the use of the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention as a pharmaceutical composition for the prevention or treatment of a CA9-related disease or condition. In one aspect, the present invention relates to the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention for use in a method for the prevention or treatment of a CA9-related disease or condition. In one aspect, the present invention relates to the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention for use as a pharmaceutical composition for the prevention or treatment of a CA9-related disease or condition. Diagnostic Composition / Imaging Agent The present invention also relates to a diagnostic composition for diagnosing a CA9-related disease or condition, comprising the peptide, conjugate, or pharmaceutically acceptable salt thereof of the present invention. The peptide or conjugate of the present invention may also be used as a diagnostic composition for a CA9-related disease or condition. The diagnostic agent may be a detection agent for diagnosing whether or not a patient has a CA9-related disease or symptom, a detection agent for diagnosing the severity of the disease, or a detection agent for diagnosing a poor prognosis of the disease. When used as a detection agent, the peptide or conjugate may be detectably labeled, may be a conjugate comprising a detectable payload, or may be a conjugate comprising a known imaging agent as a payload. In one aspect, the present invention includes an imaging agent comprising a conjugate. The imaging agent may also be used as a diagnostic composition. In one aspect, the diagnostic composition is an imaging agent. As used herein, the term "imaging agent" refers to a compound having one or more properties that enable its presence and / or location to be directly or indirectly detected, thereby enabling diagnostic imaging to be performed. Examples of such imaging agents include proteins, peptides, medium-sized compounds, small-sized compounds, and radioisotopes themselves, each incorporating a label moiety that enables detection. Examples of detectable label moieties include enzymes such as peroxidase and alkaline phosphatase (which may be bound to a chelating agent),The label may be a radioisotope (which may be bound to a compound such as glucose), fluorescein isothiocyanate (FITC), rhodamine, dansyl chloride, phycoerythrin, tetramethylrhodamine isothiocyanate, fluorescein amidite (FAM), eosin, carboxyfluorescein, erythrosine, carboxytetramethylrhodamine (TAMRA), tetramethylrhodamine (TMR), sulforhodamine, or a near-infrared fluorescent material, or a luminescent substance such as luciferase, luciferin, or aequorin. Alternatively, an antibody labeled with such a luminescent substance may be used. Additionally, an antibody labeled with nanoparticles such as gold colloid or quantum dots may also be detected. For example, a complex may be prepared between the antibody and the peptide, and the antibody or peptide may be labeled to prepare a complex, which may then be administered and detected to detect the severity of a CA9-related disease or symptom. In immunoassays, the peptide can be labeled with biotin and then detected by binding avidin or streptavidin labeled with an enzyme or the like. Among immunoassays, ELISA, which uses enzyme labeling, is preferred because it allows for simple and rapid antigen measurement. For example, an antibody is immobilized on a solid support, a sample is added and reacted, and then the labeled peptide is added and reacted. After washing, the sample is reacted with an enzyme substrate to develop color, and the absorbance is measured, thereby detecting the severity of CA9-related diseases or symptoms. After reacting the antibody immobilized on the solid support with the sample, the unlabeled peptide may be added, and an antibody against the peptide may be enzyme-labeled and then added. The antibody may be immobilized on the surface of the solid support or inside the solid support. When the enzyme is peroxidase, 3,3'-diaminobenzidine (DAB), 3,3',5,5'-tetramethylbenzidine (TMB), o-phenylenediamine (OPD), etc. can be used as the enzyme substrate, and when the enzyme is alkaline phosphatase, p-nitrophenyl phosphate (pNPP), etc. can be used. As used herein, the term "solid phase carrier" is not particularly limited as long as it is a carrier capable of immobilizing an antibody, and examples thereof include microtiter plates made of glass, metal, resin, etc., substrates, beads, nitrocellulose membranes, nylon membranes, PVDF membranes, etc.Target substances can be immobilized on these solid supports by known methods. In this specification, diagnostic imaging includes imaging by immunohistochemistry, immunofluorescence staining, and the like, optical imaging such as positron emission tomography (PET, including PET-CT) and single photon emission computed tomography (SPECT), and non-invasive (molecular) diagnostic imaging including magnetic resonance imaging (MRI), iron oxide nanoparticles, and carbon-coated iron-cobalt nanoparticles. The imaging agent of the present invention can be used for any diagnostic imaging by appropriately selecting a labeling moiety that enables detection. Preferably, the imaging agent is for use in optical imaging such as PET, PET-CT, or SPECT. In one aspect, the present invention relates to a radioligand imaging agent for use in positron emission tomography, comprising the conjugate of the present invention. The present invention relates to a diagnostic kit comprising the peptide or conjugate of the present invention. The diagnostic kit includes reagents and instruments necessary for the detection (including, but not limited to, any one or all of the peptide or conjugate of the present invention, antibody, solid-phase support, buffer, enzyme reaction stop solution, microplate reader, etc.). The present invention also relates to a method for diagnosing a CA9-related disease or condition using the peptide or conjugate of the present invention. The "diagnostic method" includes in vivo and in vitro diagnostic methods. The method of the present invention includes, but is not limited to, administering the peptide or conjugate of the present invention to a subject or a sample obtained from a subject. The method of the present invention includes, but is not limited to, administering the peptide or conjugate of the present invention to a subject or a sample obtained from a subject and detecting binding between the peptide or conjugate of the present invention and CA9. The subjects and administration methods are the same as those described in the "Pharmaceutical Composition" section. The "sample obtained from a subject" includes, for example, blood, urine, stool, tears, nasal discharge, tissue sections, etc. The present invention also relates to a method for detecting a disease using the peptide or conjugate of the present invention. Disease detection is carried out, for example, in research institutions (including educational institutions such as universities), companies, etc.The method can also be performed by persons other than physicians, such as laboratory technicians or researchers. In one embodiment, the disease detection method does not involve medical practice. Preferably, it is a diagnostic method using PET, PET-CT, or SPECT. The present invention relates to the use of the peptide or conjugate of the present invention for diagnosing a CA9-related disease or condition. The present invention relates to the use of the peptide or conjugate of the present invention for producing a diagnostic composition for diagnosing a CA9-related disease or condition. The present invention relates to the use of the peptide or conjugate of the present invention as a diagnostic composition for diagnosing a CA9-related disease or condition. The present invention relates to the peptide or conjugate of the present invention for use in a method for diagnosing a CA9-related disease or condition. The present invention relates to the peptide or conjugate of the present invention for use as a diagnostic composition for diagnosing a CA9-related disease or condition. The present invention relates to a tester comprising the peptide or conjugate of the present invention. The present invention relates to a diagnostic or detection tester comprising the peptide or conjugate of the present invention. Research Composition The present invention also relates to a research composition comprising the peptide or conjugate of the present invention. "Research compositions" include those used by researchers, engineers, students, doctors, etc. in research institutions (including educational institutions such as universities), companies, hospitals, etc. The research compositions can be used, for example, for detecting CA9 and detecting CA9-related diseases or symptoms. As used herein, the carrier for immobilizing the peptide or conjugate is not particularly limited, and examples include microtiter plates made of glass, metal, resin, etc., substrates, beads, nitrocellulose membranes, nylon membranes, PVDF membranes, etc. The present invention includes methods for detecting CA9 using the peptide or conjugate of the present invention. "Detection methods" include in vivo and in vitro detection methods. Non-limiting examples of the methods of the present invention include administering the peptide or conjugate of the present invention to a subject or a sample obtained from a subject. Non-limiting examples of the methods of the present invention include administering the peptide or conjugate of the present invention to a subject or a sample obtained from a subject,The present invention also includes a step of detecting the binding of the peptide or conjugate of the present invention to CA9. The subjects and administration methods are the same as those described in the "Pharmaceutical Composition" section. "Samples obtained from a subject" include, for example, blood, urine, stool, tears, nasal secretions, tissue sections, etc. The present invention also includes the use of the peptide or conjugate of the present invention for detecting CA9. The present invention also relates to a diagnostic or detection kit comprising the peptide or conjugate of the present invention. The diagnostic or detection kit includes reagents and instruments necessary for the detection (including, but not limited to, any or all of the peptide of the present invention, antibody, solid phase support, buffer, enzyme reaction stop solution, microplate reader, etc.). In one aspect, the present invention includes a method for delivering any payload to a subject using the peptide or conjugate of the present invention. The method of the present invention includes, but is not limited to, producing a conjugate comprising the peptide of the present invention and any payload, and administering the peptide to a subject. The subjects and administration methods are the same as those described in the "Pharmaceutical Composition" section. In one aspect, the present invention relates to a method for using the peptide or conjugate of the present invention to deliver any payload to any part (affected area) of a subject.

[0013] In the method of the present invention, the method of delivery to any part of a subject includes, but is not limited to, producing a conjugate containing the peptide of the present invention and any peptide, and administering the peptide to a subject. The subjects and administration methods are the same as those described in the "Pharmaceutical Composition" section. The matters described in other sections also apply to this section unless otherwise specified. 7. Testing Method

[0014] The present invention also relates to a method for testing a peptide or a pharmaceutically acceptable salt thereof, which tests at least one of the following for the peptide or a pharmaceutically acceptable salt thereof: a) solubility in a solvent; b) CA9 binding activity; c) toxicity to cells and / or tissues; or d) toxicity to experimental animals, wherein the peptide or a pharmaceutically acceptable salt thereof is the peptide of the present invention or a pharmaceutically acceptable salt thereof. The present invention also relates to a method for testing a conjugate, which tests at least one of the following for the conjugate: a) solubility in a solvent; b) CA9 binding activity; c) toxicity to cells and / or tissues; or d) toxicity to experimental animals,The conjugate is a conjugate of the present invention. The method relates to the above. "Solubility in a solvent" can be measured using a known method. When measuring solubility, the solvent is not limited and may be freely selected depending on the purpose. Furthermore, the method for measuring solubility can be appropriately selected from known methods depending on the type of solvent. This may be, but is not limited to, the solubility when the peptide or conjugate is dissolved in a known solvent such as water, glycerol, PBS, or DMSO. "CA9 binding activity" can be measured, for example, as described in "2. Peptides." "Toxicity to cells and / or tissues" can be measured using a known method. For example, a test for toxicity to cells and / or tissues may be a known toxicity evaluation test using cells and / or tissues, or may be an in vitro method. The cells and / or tissues may be the cells and / or tissues typically used in toxicity evaluation tests for pharmaceuticals, and are not limited thereto. "Toxicity to experimental animals" can be measured using a known method. For example, the experimental animals are not particularly limited as long as they are commonly used, and examples thereof include mice, rats, guinea pigs, gerbils, hamsters, ferrets, rabbits, dogs, cats, pigs, goats, horses, cows, birds (e.g., chickens, quails, etc.), monkeys, and non-human primates (e.g., cynomolgus monkeys, marmosets, rhesus monkeys, etc.). Furthermore, the toxicity evaluation tests described above are not limited to, and may be safety tests that are commonly conducted in non-clinical studies of pharmaceuticals, and examples thereof include general toxicity tests (single-dose toxicity tests / repeated-dose toxicity tests), genotoxicity tests (Ames tests / chromosomal aberration tests / in vitro micronucleus tests), carcinogenicity tests, reproductive and developmental toxicity tests (ICH-I, II, III), local irritation tests (eye irritation tests, skin irritation tests, etc.), other toxicity tests (skin sensitization tests, phototoxicity tests, antigenicity tests), chemical analysis / biological analysis (TK / PK), etc. The matters described in other sections also apply to this section unless otherwise specified. 8. Combination The peptide or conjugate of the present invention may be used in combination with other drugs for the prevention or treatment of CA9-related diseases or symptoms. In one aspect, the present invention relates to a method for treating a disease or condition in which the peptide or conjugate is used in combination withThis invention relates to a combination with an agent for the prevention or treatment of another CA9-related disease or symptom. The peptide or conjugate and the agent for the prevention or treatment of another CA9-related disease or symptom may be administered simultaneously or sequentially. Preferably, the peptide or conjugate and the agent for the prevention or treatment of another CA9-related disease or symptom are administered so as to obtain an additive effect, preferably a synergistic effect, of both. In the case of sequential administration, the order of administration is not important. In the case of sequential administration, it is preferred, but not limited to, that both be taken within 2 hours, 1 hour, 30 minutes, 20 minutes, 15 minutes, 10 minutes, or 5 minutes. Unless otherwise specified, matters described in other sections also apply to this section.

[0009] The present invention will be described in more detail below with reference to examples, but the present invention is not limited thereto. Those skilled in the art can easily modify and alter the present invention based on the description herein, and such modifications and alterations are within the technical scope of the present invention. The compound names shown in the following Reference Examples and Examples do not necessarily conform to the IUPAC nomenclature. Abbreviations may be used for simplicity, but these abbreviations are as described above. The raw materials, building blocks, reagents, acids, bases, solid-phase resins, and solvents used in the chemical synthesis of the compounds were either commercially available products or, if otherwise specified, synthesized using organic chemistry techniques. Commercially available amino acids containing protecting groups were used as is. Peptide residues are counted by counting the amino acid residue to be ClAc-conjugated as the first residue, followed by the second and third residues toward the resin. Common amino acids used are listed below, with side chain protecting groups indicated in parentheses. Fmoc-Ile-OH, Fmoc-Ser(Trt)-OH, Fmoc-Ser(tBu)-OH, Fmoc-His(Boc)-OH, Fmoc-Pro-OH, Fmoc-Asp(OMpe)-OH, Fmoc-Glu(tBu)-OH, Fmoc-Y(tBu)-OH, Fmoc-Gly-OH, Fmoc-Cys(Trt)-OH, Boc-Phe-OH, Fmoc-Lys(Boc)-OH. The following unnatural amino acids and abbreviations were used: Fmoc-da-OH; Fmoc-de(tBu)-OH; Fmoc-dgln(Trt)-OH; Fmoc-dhgl(tBu)-OH; Fmoc-dkCOpipzaa(tBu)-OH; Fmoc-Tbg-OH; Fmoc-3Py6CON-OH; Fmoc-3Py6NH2(Boc)-OH; Fmoc-Hgl(tBu)-OH; Fmoc-alT(tBu)-OH; Fmoc-Hgn(Trt); Fmoc-SMe-OH; Fmoc-DacAc-OH; Fmoc-KCOpipzaa(tBu)-OH; Fmoc-N-Me-da-OH; Fmoc-PeG-OH; Fmoc-MeG-OH;Fmoc−MedkCOpipzaa(tBu)−OH; Fmoc−Ahp−OH; Fmoc−pHPeG(tBu)−OH; Fmoc−pMeOPeG−OH; Fmoc−MsMeapG−OH; Fmoc−3OMePeG−OH; Fmoc−PpG−OH; Fmoc−pFPeG−OH; Fmoc−mCPeG−OH; Fmoc−pCPeG−OH; Fmoc−4HPpG−OH; Fmoc−4OMePpG−OH; Fmoc−4PypG−OH; Fmoc−4COOPeG(tBu)−OH; Fmoc−3COOPeG(tBu)−OH; Fmoc−3FPeG−OH; Fmoc−Hse(Trt)−OH; Fmoc−P4Sh(tBu)−OH; Fmoc−Qmm−OH; Fmoc−Qdm−OH; Fmoc−QPEG8Me−OH; Fmoc−5Inda−OH; Fmoc−F4OMe−OH; Fmoc−HseMe−OH; Fmoc−Acb−OH; Fmoc−dkAc−OH; Boc−df−OH; Boc−dnle−OH; Fmoc−t4amCh−OH; Boc−Nle−OH; Fmoc−N−Me−Cys(Trt)−OH; Fmoc−N−Me−Ala−OH; Fmoc−N−Me−Ser(Trt)−OH; Fmoc−N−Me−Asn(Trt)−OH; Fmoc−Hpr−OH; Boc−PEG8c−OH; Fmoc−PEG10c−OH; Fmoc−dk(Boc)−OH; Fmoc−dp−OH; Fmoc−dyae(Boc)−OH: Alloc−dk(Fmoc)−OH; Boc−PEG8c−OH; Fmoc−de(Allyl)−OH; Fmoc−Hgl(Allyl)−OH; Fmoc−dk(Alloc)−OH;Fmoc-Q glucamine (acetonide)-OH. The structure of the chemically synthesized peptide was determined by ESI-MS(+) mass spectrometry, where the molecular weight was calculated based on the amino acids used according to the target sequence and the building blocks used as needed. "ESI-MS(+)" refers to electrospray ionization mass spectrometry performed in positive ion mode. The detected mass was reported in "m / z" units. Compounds with molecular weights greater than approximately 1000 were frequently detected as doubly or triply charged ions. Example 1: Synthesis of cyclic peptides and synthesis of conjugates. The chemically synthesized peptides were identified based on the retention time obtained by one of the following analytical methods (detection: UV wavelength 225 nm, Shimadzu "SPD-M20A"). Analysis Condition A Column: Kinetex® EVO C18 2.6 μm, 2.1 ID×150 mm, 100 Å Mobile phase: A=0.025% TFA in water; B=0.025% TFA in CH; ３ In CN Temperature: 60°C Flow rate: 0.5 mL / min Gradient: 20-60 / 7.15 min, 60-95 / 0.3 min Analysis condition B Column: Kinetex® EVO C18 2.6 μm, 2.1 ID x 150 mm, 100 Å Mobile phase: A = 0.025% TFA in water; B = 0.025% TFA in CH ３In CN, temperature: 60°C, flow rate: 0.5 mL / min, gradient: 5-45 / 7.15 min, 45-95 / 0.3 min. Peptide chain elongation on solid-phase resin was carried out using a commercially available resin as the starting material by the Fmoc method. Specifically, using Sieber amide resin (Watanabe Chemical Industry Co., Ltd.), the target peptide was synthesized by starting with the removal of the Fmoc group, followed by repeated introduction of each Fmoc amino acid and deprotection of the Fmoc group. Unless otherwise specified, peptide chain elongation was carried out by automated synthesis using a CEM Liberty Blue or Liberty Blue HT solid-phase synthesizer, following the manufacturer's instructions. When introducing each residue, double coupling was performed, in which the peptide coupling reaction was repeated twice, as necessary. On the other hand, introduction of some amino acids was carried out by removing the resin from the automatic synthesizer and carrying out the reaction using freshly prepared reagents (manual coupling). For example, about 4 equivalents of Fmoc amino acid, about 8 equivalents of DIC, and about 4 equivalents of Oxyma pure were added to the Fmoc-free peptide chain supported on the solid-phase resin, and the reaction was carried out by shaking once or twice under any of the reaction conditions shown in the table below, followed by washing the resin with DMF. The Fmoc group was removed, for example, by the following method: the peptide chain after introduction of the Fmoc amino acid supported on the solid phase resin was subjected to one or two shaking steps under any of the conditions shown in the table below, and then the resin was washed with DMF. Following the above-mentioned method, the introduction of each Fmoc amino acid and the deprotection of the Fmoc group were repeated to elongate the target peptide chain, after which a chloroacetyl group was introduced. The introduction method was one of the methods in the table below. After removing the Fmoc group from the solid-phase resin retaining the Fmoc-protected peptide obtained in the previous step, a solution containing about 5-10 equivalents of chloroacetic acid, about 5-10 equivalents of a condensing agent, and about 5-10 equivalents of an additive in the following solvent was added to the solid-phase resin, and the mixture was shaken at room temperature for 30-60 minutes. The side chains were deprotected and the peptide was cleaved from the solid-phase resin by using one of the following reagent cocktails (TFA / H ２The mixture was added with 0.05% ethanol (a mixture of 0.05% ethanol / TIS / DODT) and shaken at room temperature for 30-120 minutes. The reaction mixture was then filtered through a frit, and the filtrate was added to an excess of diisopropyl ether or a mixed solvent of diisopropyl ether and hexane or diethyl ether and hexane (e.g., 1 / 1, v / v) cooled to 0°C, resulting in a cloudy white precipitate. The precipitate was centrifuged to obtain a solid, and the supernatant was decanted. The resulting solid was washed again with a small amount of diethyl ether cooled to 0°C, and then dried under reduced pressure. The solid obtained above was used in a peptide cyclization reaction. The peptide cyclization reaction was carried out in DMSO or DMSO / H2SO4 at a final peptide concentration of 4 mM-5 mM based on the molar number of the solid phase resin used. ２ O, MeCN / H ２ O or DMSO / MeCN / H ２ After dissolving the product in a mixed solvent of 0, 5-35 equivalents of triethylamine was added and the mixture was shaken at room temperature for 2 hours to overnight. The resulting reaction solution was concentrated under reduced pressure and then purified. The resulting residue was purified by reverse-phase preparative HPLC according to one of the methods in the table below. The specific structures of the synthesized peptides and conjugates are shown below. Examples 1-1 to 1-3 relate to the synthesis of peptides. Example 1-1: Synthesis of peptide SEQ ID No. 45 The target peptide was synthesized using Sieber amide resin (Watanabe Chemical, 0.60 mmol / g, 1.67 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was performed according to the manufacturer's instructions. To remove the Fmoc residue from the solid-phase resin, 10% pyrrolidine (in DMF) was used and the reaction was carried out once at 75°C for 3 minutes. To introduce each residue, 0.21 M Fmoc-AA (in DMF) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used per equivalent of resin, and the reaction was carried out once at 75°C for 10 minutes. However, for the third and ninth residues, 0.21 M Fmoc-AA (in NMP) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used, and for the fourth and sixth residues, the reaction was carried out twice for 20 minutes at 75°C. For the twelfth residue, the reaction was carried out twice for 30 minutes at 75°C. For the thirteenth residue, the reaction was carried out once for 30 minutes at 50°C. To remove the Fmoc group after the introduction of each residue, the solid-phase resin carrying the Fmoc-protected peptide was reacted once for 3 minutes at 75°C using 4% pyrrolidine + 83 mM Oxyma pure (in DMF). For the fourth residue, the reaction was carried out twice for 5 minutes at room temperature using a 10% pyrrolidine solution in DMF. The 6th and 12th residues were reacted with a 10% DMF solution of pyrrolidine at room temperature for 5 minutes once and for 10 minutes once. The solid-phase resin retaining the Fmoc-protected peptide obtained in the previous step was reacted with a 10% DMF solution of pyrrolidine at 75°C for 3 minutes once to remove the Fmoc group from the α-amino group. This was then shaken with 1.0 M ClAcNHS (10 equivalents in DMF) at room temperature for 60 minutes to introduce a chloroacetyl group. To deprotect the side chain and cleave the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. The solid-phase resin was then divided into approximately halves, and each half was charged with a reagent cocktail (10 mL, TFA / H ２A mixture of 92.5 / 2.5 / 2.5 / 2.5 (volume ratio of 0.01% / TIS / DODT) was added and shaken at room temperature for 40 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. This filtrate was divided into four portions and each portion was added to 40 mL of a 1 / 1 diethyl ether / hexane mixed solvent, resulting in precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was combined and used in the subsequent cyclization reaction. The peptide was dissolved in 1 / 1 water / acetonitrile to a final concentration of 5 mM based on the molar amount of the solid-phase resin. 10 equivalents of triethylamine were then added and the mixture was stirred at room temperature for 60 minutes, allowing for the peptide cyclization reaction. The reaction was stopped by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using Genevac EZ-II elite. The resulting crude product was purified using the following conditions: (Column: Waters Xbridge® C18 5 μm 50 × 250 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 50°C; Gradient (% B): 4.2-0.0% over 0.1 min, 0.0-0.0% over 4.9 min, 0.0-4.2% over 2 min, 4.2-28.6% over 3 min, 28.6-33.7% over 15 min, 33.7-60% over 3 min; Flow rate: 118-18 mL / min over 0.1 min, 18-18 mL / min over 4.9 min, 18-118 mL / min over 2 min, then 118 mL / min). Fractions containing the target product were collected and lyophilized to give the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 96.7%. Analytical condition A: retention time = 2.86 minutes ESI-MS (+) observed value m / z = 862.37 (M + 2H) ２＋ Example 1-2 Synthesis of peptide SEQ ID No. 46 The target peptide was synthesized using Sieber amide resin (Watanabe Chemical, 0.60 mmol / g, 1.67 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was performed according to the manufacturer's instructions. To remove the Fmoc residue from the solid-phase resin, 10% pyrrolidine (in DMF) was used, and the reaction was carried out once at 75°C for 3 minutes. To introduce each residue, 0.21 M Fmoc-AA (in DMF) / 0.5 M HATU (in DMF) / 1.0 M DIPEA (in DMF) (4.2 equivalents / 4 equivalents / 8 equivalents) was used per equivalent of resin, and the reaction was carried out once at 75°C for 10 minutes. However, for the third and ninth residues, 0.21 M Fmoc-AA (in NMP) / 0.5 M HATU (in DMF) / 1.0 M DIPEA (in DMF) (4.2 equivalents / 4 equivalents / 8 equivalents) was used, and for the fourth, sixth, and twelfth residues, the reaction was carried out twice for 10 minutes at 75°C. For the thirteenth residue, the reaction was carried out once for 30 minutes at 40°C. To remove the Fmoc group after the introduction of each residue, the solid-phase resin carrying the Fmoc-protected peptide was reacted once for 3 minutes at 75°C using 4% pyrrolidine + 83 mM Oxyma pure (in DMF). For the fourth, sixth, and twelfth residues, the reaction was carried out twice for 5 minutes at room temperature using a 10% pyrrolidine solution in DMF. The solid-phase resin retaining the Fmoc-protected peptide obtained in the previous step was reacted once with a 10% DMF solution of pyrrolidine at 75°C for 3 minutes to remove the Fmoc group from the α-amino group. This was then shaken with 0.25M ClAcNHS (5 equivalents in DMF) at room temperature for 60 minutes to introduce a chloroacetyl group. To deprotect the side chain and cleave the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. The solid-phase resin was then divided into approximately two halves, and each half was charged with a reagent cocktail (20 mL, TFA / H ２A 92.5 / 2.5 / 2.5 / 2.5 volumetric mixture of 0.1% PEG / TIS / DODT was added and shaken at room temperature for 30 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. This filtrate was divided into eight portions and added to 40 mL of a 1 / 1 diisopropyl ether / hexane mixture, resulting in precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was combined and used in the subsequent cyclization reaction. The peptide was dissolved in 1 / 1 water / acetonitrile to a final concentration of 2.5 mM based on the molar amount of the solid-phase resin. Then, 10 equivalents of triethylamine were added and the mixture was stirred at room temperature for 16 hours, allowing for the peptide cyclization reaction. The reaction was terminated by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using a Genevac HT-12. The resulting crude product was purified using the following conditions: Column: Waters XSelect®, C18 5 μm, 50 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 40 °C; Gradient (% B): 5.0-5.0% over 2 min, 5.0-25.0% over 1 min, 25.0-30.0% over 8 min, 30.0-60.0% over 1 min; Flow rate: 20-20 mL / min over 1 min, 20-120 mL / min over 1 min, then 120 mL / min. The fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target substance was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target substance was 96.3%. Analytical condition A: retention time = 3.30 minutes ESI-MS (+) observed value m / z = 882.36 (M + 2H) ２＋ Example 1-3 Synthesis of peptide SEQ ID No. 47 The target peptide was synthesized using Sieber amide resin (Watanabe Chemical, 0.57 mmol / g, 0.53 g). A CEM Liberty Prime solid-phase synthesizer was used, and the synthesis was performed according to the manufacturer's instructions. To remove the Fmoc residue from the solid-phase resin, 10% pyrrolidine (in DMF) was used, and the reaction was carried out once at 110°C for 1 minute. To introduce each residue, 0.21 M Fmoc-AA (in DMF) / 2.0 M DIC (in DMF) / 0.25 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used per equivalent of resin, and the reaction was carried out once at 105°C for 2 minutes. However, for the third and ninth residues, 0.21 M Fmoc-AA (in NMP) / 2.0 M DIC (in DMF) / 0.25 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used, and the fourth residue was reacted twice at 105°C for 3 minutes. The sixth and twelfth residues were reacted twice at 90°C for 10 minutes, and the thirteenth residue was reacted once at 40°C for 30 minutes. To remove the Fmoc group after each residue introduction, the solid-phase resin carrying the Fmoc-protected peptide was reacted once at 110°C for 3 minutes using 4% pyrrolidine + 83 mM Oxyma pure (in DMF). The fourth, sixth, and twelfth residues were reacted twice at room temperature for 1 minute using a 10% pyrrolidine DMF solution. The solid-phase resin carrying the Fmoc-protected peptide obtained in the previous step was reacted once for 1 minute with a 4% pyrrolidine / 83 mM Oxyma Pure DMF solution at 110°C to remove the Fmoc group from the α-amino group. The resulting mixture was then shaken at 25°C for 30 minutes with 0.1 M ClAcOH (in DMF) / 0.1 M HATU (in DMF) / 0.2 M DIEA (in DMF) (5 equivalents / 5 equivalents / 10 equivalents) to introduce a chloroacetyl group. To deprotect the side chain and cleave the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. Subsequently, a reagent cocktail (14 mL, TFA / H) was added to the reaction vessel containing the solid-phase resin. ２A 92.5 / 2.5 / 2.5 / 2.5 volume mixture of DISO / TIS / DODT was added and shaken at room temperature for 60 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. This filtrate was divided into three portions and each portion was added to 40 mL of a 1 / 1 diisopropyl ether / hexane mixed solvent, resulting in precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was combined and used in the subsequent cyclization reaction. The peptide was dissolved in water / DMSO (1 / 9) to a final concentration of 5 mM based on the molar amount of the solid-phase resin. 10 equivalents of triethylamine were then added and the mixture was stirred overnight at room temperature to carry out the peptide cyclization reaction. The reaction was stopped by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using a Genevac HT-12. The resulting crude product was purified using the following conditions: column: Waters Xbridge® C18 5 μm 50 × 150 mm; mobile phase: A = 0.1% TFA (in water), B = 0.1% TFA (in MeCN); temperature: 40 °C; gradient (% B): 5.0-5.0% over 2 min, 5.0-27% over 1 min, 27-32% over 8 min, 32-60% over 1 min; flow rate: 20-20 mL / min over 1 min, 20-120 mL / min over 1 min, then 120 mL / min). Fractions containing the target product were collected, lyophilized, and purified again (Column: Waters XSelect® C18 5 μm 30 × 150 mm; Mobile phase: A = 1.0% AcOH (in water), B = 1.0% AcOH (in MeCN); Temperature: 40°C; Gradient (% B): 2.0-19% over 3 minutes, 19-24% over 8 minutes, 24-60% over 1 minute; Flow rate: 45 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 99.6%. Analytical condition B: Retention time = 5.71 minutes ESI-MS (+) Observed value m / z = 855.30 (M + 2H). ２＋Examples 1-4 to 1-16 relate to the synthesis of conjugates. Example 1-4: Synthesis of Conjugate No. 64 Peptide SEQ ID No. 45 (sequence: ClAc-da-Tbg-3PyCON-Hgl-Meda-Ahp-PeG-S-3PyNH-HseMe-dk-Y-MeC) (200 mg) synthesized in Example 1-1 and DIEA (225 mg) were dissolved in DMF (4.84 mL), and DOTA-NHS ester hexafluorophosphate trifluoroacetate (147 mg) was added under ice cooling. The reaction mixture was stirred at room temperature for 90 minutes. The resulting reaction mixture was purified using the following conditions: (Column: Waters XSelect® C18 5 μm 30 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 50°C; Gradient (% B): 4.0-0.0% over 0.1 min, 0.0-0.0% over 4.9 min, 0.0-4.0% over 1 min, 4.0-28.5% over 3 min, 28.5-33.6% over 9 min, 33.6-60% over 1 min; Flow rate: 44-9 mL / min over 0.1 min, 9-9 mL / min over 4.9 min, 9-44 mL / min over 1 min, then 44 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target substance was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target substance was 97.3%. Analytical condition B: Retention time = 5.74 minutes ESI-MS (+) Observed value m / z = 704.13 (M + 3H) ３＋ Example 1-5 Synthesis of Conjugate No. 62 Peptide SEQ ID No. 46 (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeC) (100 mg) synthesized in Example 1-2 and DIEA (117 mg) were dissolved in DMF (2.51 mL), and DOTA-NHS ester hexafluorophosphate trifluoroacetate (76 mg) was added under ice cooling. The reaction mixture was stirred at room temperature for 120 minutes. The resulting reaction mixture was purified using the following conditions: (Column: Waters XBridge® C18 5 μm 50 × 250 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 50°C; Gradient (% B): 4.2-0.0% over 0.1 min, 0.0-0.0% over 4.9 min, 0.0-4.2% over 2 min, 4.2-25.6% over 3 min, 25.6-30.7% over 15 min, 30.7-60% over 3 min; Flow rate: 118-18 mL / min over 0.1 min, 18-18 mL / min over 4.9 min, 18-118 mL / min over 2 min, then 118 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 96.6%. Analytical condition A: retention time = 3.27 minutes ESI-MS (+) observed value m / z = 717.38 (M + 3H) ３＋ Example 1-6 Synthesis of Conjugate No. 65 DOTA (0.42 g, CAS: 60239-18-1), DIEA (0.14 g), and N-hydroxysuccinimide (0.08 g, CAS: 6066-82-6) were dissolved in water (3.3 mL), and then 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (0.13 g, CAS: 25952-53-8) dissolved in water (1.9 mL) was added under ice cooling. The reaction mixture was stirred for 30 minutes under ice cooling. The peptide SEQ ID No. synthesized in Example 1-3 was added to DMF (561 μL). 47 (sequence: ClAc-da-Tbg-3PyCON-Hgl-MeG-Ahp-PeG-S-3PyNH-HseMe-dk-Y-MeC) (23 mg) and DIEA (13.0 mg) were dissolved, and the solution prepared above (561 μL) was added under ice cooling. The reaction mixture was stirred at room temperature for 1 hour. DIEA (13.0 mg) was added to the reaction solution and stirred for 1 hour to quench the reaction. The resulting reaction mixture was purified using the following conditions (column: Waters Xbridge® C18 5 μm 19 × 150 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50°C; gradient (% B): 5.0-28% over 3 minutes, 28-33% over 8 minutes, 33-60% over 1 minute; flow rate: 17 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 97.6%. Analytical condition A: retention time = 3.14 minutes, ESI-MS (+) observed value m / z = 699.33 (M + 3H). ３＋ Example 1-7 Synthesis of Conjugate No. 26 DOTA (0.79 g, CAS: 60239-18-1), DIEA (0.34 mL), and N-hydroxysuccinimide (0.15 g, CAS: 6066-82-6) were dissolved in water (7.2 mL), and then 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (0.25 g, CAS: 25952-53-8) dissolved in water (4.17 mL) was added under ice cooling. The reaction mixture was stirred for 60 minutes under ice cooling. The peptide SEQ ID No. synthesized in Example 1-2 was added to DMF (1.00 mL). 46 (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeC) (40 mg) and DIEA (31.6 μL) were dissolved, and the solution prepared above (1004 μL) was added under ice cooling. The reaction mixture was stirred at room temperature for 60 minutes. DIEA (31.6 μL) was added to the reaction mixture, and the mixture was stirred at room temperature for 60 minutes. Lutetium(III) chloride hexahydrate (86.0 mg, CAS: 15230-79-2) and ammonium acetate (17 mg, CAS: 631-61-8) dissolved in water (4420 μL) were added to the reaction mixture. The reaction mixture was stirred at 90 °C for 1 hour. The resulting reaction mixture was purified using the following conditions: (Column: Waters XSelect® C18 5 μm 30 × 150 mm; Mobile phase: A = 1.0% AcOH in water, B = 1.0% AcOH in MeCN; Temperature: 40°C; Gradient (% B): 5.0-27% over 3 min, 27-32% over 8 min, 32-60% over 1 min; Flow rate: 45 mL / min). Fractions containing the target compound were collected and lyophilized to obtain the target peptide. The purity of the target compound was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target compound was 99.4%. Analytical condition A: Retention time = 3.48 min, ESI-MS (+) Observed value m / z = 774.79 (M + 3H). ３＋ Example 1-8 Synthesis of Conjugate No. 51 The target peptide (sequence: ClAc-de(PEG8Me)-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeC) (SEQ ID NO: 55) was synthesized using Sieber amide resin (Watanabe Chemical, 0.60 mmol / g, 0.584 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was performed according to the manufacturer's instructions. To remove the Fmoc residue on the solid-phase resin, a reaction was performed once at 90°C for 1 minute using 10% pyrrolidine (in DMF). For the introduction of each residue, 0.21 M Fmoc-AA (in DMF) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used per equivalent of resin, and the reaction was carried out once at 90°C for 3 minutes. However, for the third residue, 0.21 M Fmoc-AA (in NMP) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used, and for the fourth, sixth, and twelfth residues, the reaction was carried out twice at 90°C for 10 minutes. For the thirteenth residue, the reaction was carried out once at 40°C for 30 minutes. For the first residue, Fmoc-de(Allyl)-OH was used. The resulting solid-phase resin was shaken with 0.19 M Fmoc-OSu (5 equivalents in DMF) at room temperature for 1 hour and then washed with DMF. The first residue side chain was deprotected using tetrakis(triphenylphosphine)palladium(0) (CAS: 14221-01-3) / phenylsilane (CAS: 694-53-1) (0.2 equivalents / 10 equivalents) in DCM (15 mL) at room temperature for 60 minutes per equivalent of resin. The side chain extension reaction was carried out by deprotecting the Allyl, washing with DCM and DMF, and then using H-PEG8Me / DIC / Oxyma pure (4.2 equivalents / 8 equivalents / 4 equivalents) in DMF (13 mL) at 75°C for 30 minutes per equivalent of resin. To remove the Fmoc group after each residue was introduced, the solid-phase resin carrying the Fmoc-protected peptide was reacted once for 1 minute with 4% pyrrolidine + 83 mM Oxyma pure (in DMF) at 90°C. The 4th, 6th, and 12th residues were reacted twice for 1 minute with a 10% pyrrolidine solution in DMF at room temperature.The solid-phase resin carrying the Fmoc-protected peptide obtained in the previous step was reacted with a 10% DMF solution at room temperature for 1 minute twice to remove the Fmoc group from the α-amino group. This was then shaken with 0.19 M ClAcNHS (5 equivalents in DMF) at room temperature for 60 minutes to introduce a chloroacetyl group. To deprotect the side chain and cleave the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. A reagent cocktail (16 mL, TFA / H2SO4) was then added to the reaction vessel. ２A 92.5 / 2.5 / 2.5 / 2.5 volumetric mixture of 0.1% PEG / TIS / DODT was added and the mixture was shaken at room temperature for 30 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. This filtrate was divided into three portions and each portion was added to 40 mL of a 1 / 1 diethyl ether / hexane mixed solvent, resulting in precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was combined and used in the subsequent cyclization reaction. The peptide was dissolved in 1 / 1 water / acetonitrile to a final concentration of 3.0 mM based on the molar amount of the solid-phase resin. 10 equivalents of triethylamine were then added and the mixture was stirred at room temperature for 15 hours to carry out the peptide cyclization reaction. The reaction was stopped by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using a Genevac EZ-II elite. The resulting crude product was purified using the following conditions: column: Waters XSelect® C18 5 μm 50 × 250 mm; mobile phase: A = 1.0% AcOH (in water), B = 1.0% AcOH (in MeCN); temperature: 50 °C; gradient (% B): 0-0% over 5.1 min, 0-4.2% over 1.9 min, 4.2-25.6% over 3 min, 25.6-30.7% over 15.5 min, 30.7-60% over 1.5 min, 60-90% over 4 min; flow rate: 18-18 mL / min over 8 min, 18-118 mL / min over 2 min, then 118 mL / min). The fractions containing the target product were collected and freeze-dried to obtain a cyclic peptide. The target peptide was obtained using the obtained cyclic peptide as a raw material under the same reaction and purification conditions as in Examples 1-7. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 98.5%. Analytical condition A: retention time = 4.12 minutes ESI-MS (+) observed value m / z = 915.83 (M + 3H) ３＋ Example 1-9 Synthesis of Conjugate No. 35 The target peptide (sequence: ClAc-da-Tbg-3PyCON-Hgl-Meda-Ahp-PeG-D-3PyNH-HseMe-dk(F)-Y-MeC) (SEQ ID NO: 56) was synthesized using Sieber amide resin (Watanabe Chemical, 0.54 mmol / g, 1.39 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was carried out according to the manufacturer's instructions. To remove the Fmoc residue on the solid-phase resin, a reaction was carried out once at 75°C for 3 minutes using 10% pyrrolidine (in DMF). For the introduction of each residue, 0.21 M Fmoc-AA (in DMF) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used per equivalent of resin, and the reaction was carried out once at 75 ° C for 10 minutes. However, for the third residue, 0.21 M Fmoc-AA (in NMP) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) was used, and for the ninth residue, 0.21 M Fmoc-AA (in NMP) / 0.5 M HATU (in DMF) / 1.0 M DIEA (in DMF) (4.2 equivalents / 4 equivalents / 8 equivalents) was used. For the third residue, the reaction was carried out once at 75 ° C for 30 minutes. The 4th, 6th, and 12th residues were reacted twice at 75°C for 10 minutes. The 13th residue was reacted once at 50°C for 15 minutes. Fmoc-dk(Alloc)-OH was used for the 11th residue. The resulting solid-phase resin was shaken with 0.38 M Fmoc-OSu (5 equivalents in DMF) at room temperature for 1 hour and then washed with DMF. The side chain of the 11th residue was deprotected once at room temperature for 60 minutes using tetrakis(triphenylphosphine)palladium(0) (CAS: 14221-01-3) / phenylsilane (CAS: 694-53-1) (0.2 equivalents / 10 equivalents) per equivalent of resin in DCM / HFIP (30 mL / 0.3 mL). The elongation reaction from the side chain was carried out by deprotecting Alloc, washing with DCM and DMF, and then reacting 1 equivalent of the resulting resin with Boc-F-OH / HATU / DIEA (4.2 equivalents / 4 equivalents / 8 equivalents) in DMF (10 mL) at 75°C for 30 minutes.To remove the Fmoc group after each residue introduction, the solid-phase resin carrying the Fmoc-protected peptide was reacted twice with 10% pyrrolidine (in DMF) at room temperature for 5 minutes. For residues 9, 10, 11, 12, and 13, the solid-phase resin was reacted once with 4% pyrrolidine + 83 mM Oxyma pure (in DMF) at 75°C for 3 minutes. The Fmoc group on the α-amino group was removed by reacting the solid-phase resin carrying the Fmoc-protected peptide obtained in the previous step with 10% piperidine in DMF once at room temperature for 1 minute. This was then shaken with 0.25 M ClAcNHS (10 equivalents in DMF) at room temperature for 60 minutes to introduce a chloroacetyl group. To deprotect the side chains and cleave them from the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. The solid-phase resin was then divided into three parts, and each part was placed in a reaction vessel with a reagent cocktail (12 mL, TFA / H. ２A 92.5 / 2.5 / 2.5 / 2.5 volume mixture of DISO / TIS / DODT was added and shaken at room temperature for 40 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. This filtrate was divided into two portions and added to 30 mL of a 1 / 1 diisopropyl ether / hexane mixed solvent, resulting in precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was combined and used in the subsequent cyclization reaction. The peptide was dissolved in DMSO / water / acetonitrile (1 / 2 / 2) to a final concentration of 5.0 mM based on the molar amount of solid-phase resin. 10 equivalents of triethylamine were then added and stirred at room temperature for 1 hour to carry out the peptide cyclization reaction. The reaction was stopped by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using Genevac EZ-II elite. The resulting crude product was purified using the following conditions: (Column: Waters XBridge® C18 5 μm 50 × 250 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 50 °C; Gradient (% B): 5.3-1.1% over 0.1 min, 1.1-1.1% over 4.9 min, 1.1-5.3% over 2 min, 5.3-30.7% over 3 min, 30.7-35.8% over 15 min, 35.8-60% over 3 min; Flow rate: 118-18 mL / min over 0.1 min, 18-18 mL / min over 4.9 min, 18-118 mL / min over 2 min, then 118 mL / min). Fractions containing the desired product were collected and lyophilized to give the cyclic peptide. The target peptide was obtained by using the obtained cyclic peptide as a raw material and subjecting it to the same reaction and purification conditions as in Examples 1-7. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 98.7%. Analytical condition A: retention time = 3.79 minutes ESI-MS (+) observed value m / z = 819.85 (M + 3H) ３＋ Example 1-10 Synthesis of Conjugate No. 38 The target peptide (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk(PEG8c)-Y-MeC) (SEQ ID NO: 57) was synthesized using Sieber amide resin (Watanabe Chemical, 0.60 mmol / g, 0.21 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was carried out according to the manufacturer's instructions. To remove the Fmoc residue on the solid-phase resin, a reaction was carried out once at 90°C for 1 minute using 10% pyrrolidine (in DMF). To introduce each residue, a reaction was carried out once for 3 minutes at 90°C using 0.21 M Fmoc-AA (in DMF) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) per equivalent of resin. However, Alloc-dk(Fmoc)-OH was used for the 11th residue. After elongation from the 13th to the 11th residue and removal of the side chain Fmoc group, Boc-PEG8c-OH was used for the elongation reaction from the side chain. Deprotection of the main chain Alloc group was carried out once for 60 minutes at room temperature using tetrakis(triphenylphosphine)palladium(0) (CAS: 14221-01-3) / dimethylamineborane (CAS: 74-94-2) (0.2 equivalents / 10 equivalents) per equivalent of resin in DCM / HFIP (5 mL / 0.1 mL). The resulting solid-phase resin was then subjected to a subsequent elongation reaction. However, for the 9th residue, 0.21 M Fmoc-AA (in NMP) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents) was used. The 4th, 6th, 7th, and 12th residues were subjected to two 10-minute reactions at 90°C. The 13th residue was subjected to one 20-minute reaction at 40°C. To remove the Fmoc group after each residue introduction, the solid-phase resin carrying the Fmoc-protected peptide was reacted twice with 10% pyrrolidine (in DMF) at room temperature for 1 minute. The side chains of the 10th and 11th residues were reacted once with 4% pyrrolidine + 83 mM Oxyma pure (in DMF) at 90°C for 1 minute.The solid-phase resin carrying the Fmoc-protected peptide obtained in the previous step was reacted with a 10% DMF solution at room temperature for 1 minute twice to remove the Fmoc group from the α-amino group. This was then shaken with 0.16 M ClAcNHS (5 equivalents in DMF / DCM = 1 / 1) at room temperature for 60 minutes to introduce a chloroacetyl group. To deprotect the side chain and cleave the solid-phase resin, the resin obtained after the chloroacetyl group introduction step was first washed once with DMF, methylene chloride, and diethyl ether, and then dried under reduced pressure. Next, a reagent cocktail (3 mL, TFA / H O ) was added to the reaction vessel. ２A mixture of 90 / 2.5 / 2.5 / 5.0 volumetric ratios of DISO / TIS / DODT was added and shaken at room temperature for 120 minutes. The reaction solution was filtered through a frit. The solid-phase resin remaining in the reaction vessel was shaken again with the excision cocktail, and the solution components were recovered through a frit and mixed with the filtrate. The filtrate was added to 35 mL of a diethyl ether / hexane (1 / 1) mixed solvent, resulting in a precipitate. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting solid (peptide) was used in the subsequent cyclization reaction. The peptide was dissolved in water / acetonitrile (1 / 1) to a final concentration of 5.0 mM based on the molar amount of solid-phase resin. 10 equivalents of triethylamine were then added and stirred at room temperature for 1 hour to carry out the peptide cyclization reaction. The reaction was stopped by adding acetic acid to the reaction solution, and the reaction solution was concentrated under reduced pressure using a Genevac EZ-II elite. The resulting residue was dissolved in DMSO / water (9 / 1) to a final concentration of 25 mM based on the molar amount of solid-phase resin. DIEA / SulfoCy5-NHS ester (5 equivalents / 1.2 equivalents) was then added and stirred at room temperature for 1 hour. The reaction was quenched by adding acetic acid to the reaction solution. The resulting reaction mixture was purified using the following conditions: Column: Waters XSelect®, C18 5 μm, 19 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 60°C; Gradient (% B): 12-37% over 3 min, 37-42% over 8 min, 42-60% over 1 min; Flow rate: 17 mL / min). The fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 96.0%. Analytical condition A: retention time = 5.12 minutes ESI-MS (+) observed value m / z = 942.68 (M + 3H) ３＋ Example 1-11 Synthesis of Conjugate No. 67 The target peptide (sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeA-MeG) (SEQ ID NO: 58) was synthesized using H-Ser(tBu)-Trt(2-Cl) resin (Watanabe Chemical, 0.78 mmol / g, 1.28 g). A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was carried out according to the manufacturer's instructions. To introduce each residue, a single reaction was carried out at room temperature for 30 minutes using 0.21 M Fmoc-AA (in DMF) / 0.5 M HATU (in DMF) / 1.0 M DIPEA (in DMF) (4.2 equivalents / 4 equivalents / 8 equivalents) per equivalent of resin. However, the third residue was prepared using 0.21 M Fmoc-AA (in NMP) / 0.5 M HATU (in DMF) / 1.0 M DIPEA (in DMF) (4.2 equivalents / 4 equivalents / 8 equivalents), and the ninth residue was prepared using 0.21 M Fmoc-AA (in NMP) / 1.0 M DIC (in DMF) / 0.5 M Oxyma pure (in DMF) (4.2 equivalents / 8 equivalents / 4 equivalents). The fourth, sixth, seventh, and twelfth residues were reacted twice at room temperature for 30 minutes. The ninth residue was reacted once at room temperature for 60 minutes. The thirteenth residue was reacted twice at room temperature for 60 minutes. To remove the Fmoc group after the introduction of each residue, the solid-phase resin carrying the Fmoc-protected peptide was reacted twice with 10% pyrrolidine (in DMF) at room temperature for 5 minutes. The first residue was reacted twice with 10% pyrrolidine (in DMF) at room temperature for 1 minute. To cleave the solid-phase resin, a reagent cocktail, HFIP / DCM (9 mL, 1 / 4), was added and the mixture was shaken at room temperature for 60 minutes. The reaction mixture was concentrated under reduced pressure using a Genevac EZ-II Elite. The residue was solidified by adding diisopropyl ether, centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting residue was dissolved in DMF to a final concentration of 5 mM based on the molar amount of the solid-phase resin. DIEA / HATU (5 equivalents / 1.2 equivalents) was then added and stirred at room temperature for 1 hour. The reaction was stopped by adding acetic acid to the reaction solution. The reaction mixture was concentrated under reduced pressure using a Genevac HT-12.The resulting residue was treated with a reagent cocktail (TFA / H. ２ A 95 / 2.5 / 2.5 volumetric mixture of PEG / TIS (95 / 2.5 / 2.5) was added to the reaction mixture and shaken at room temperature for 40 minutes. 40 mL of diisopropyl ether was added to the reaction mixture, causing precipitation. The mixture was centrifuged, and the solution was decanted. The resulting solid was washed again with diethyl ether and dried under reduced pressure. The resulting residue was purified using the following conditions: Column: Waters XSelect® C18 5 μm 50 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 40 °C; Gradient (% B): 5-5% over 2 min, 5-27% over 1 min, 27-32% over 8 min, 32-60% over 1 min; Flow rate: 20-20 mL / min over 1 min, 20-120 mL / min over 1 min, then 120 mL / min. The fractions containing the target product were collected and freeze-dried. The target peptide was obtained using the resulting cyclic peptide as a raw material under the same reaction and purification conditions as in Examples 1-7. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 99.7%. Analytical condition A: retention time = 4.27 minutes ESI-MS (+) observed value m / z = 768.69 (M + 3H) ３＋ Example 1-12 Synthesis of Conjugate No. 56 Peptide SEQ ID No. 46 (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeC) (20 mg) synthesized in Example 1-2 and DIEA (26.3 μL) were dissolved in DMSO (0.50 mL), and then 2,2′,2″-(10-(2,6-dioxotetrahydro-2H-pyran-3-yl)-1,4,7,10-tetraazacyclododecane-1,4,7-triyl)triacetic acid (8.1 mg, CAS: 1375475-53-8) was added at room temperature. The reaction mixture was stirred at room temperature for 5 hours. The resulting reaction mixture was purified using the following conditions (column: Waters XBridge® C18 5 μm 19 × 150 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50°C; gradient (% B): 5.0-27% over 3 min, 27-32% over 8 min, 32-60% over 1 min; flow rate: 17 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 97.8%. Analytical condition A: retention time = 3.40 min, ESI-MS (+) observed value m / z = 741.40 (M + 3H). ３＋ Example 1-13 Synthesis of Conjugate No. 58 Peptide SEQ ID No. 46 (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeC) (20 mg) synthesized in Example 1-2 and DIEA (26.3 μL) were dissolved in DMSO (0.50 mL), and then 2,2′-(7-(1-carboxy-4-((2,5-dioxopyrrolidin-1-yl)oxy)-4-oxobutyl)-1,4,7-triazonane-1,4-diyl)diacetic acid (14 mg, CAS: 1407166-70-4) was added at room temperature. The reaction mixture was stirred at room temperature for 7 hours. The resulting reaction mixture was purified using the following conditions (column: Waters XBridge® C18 5 μm 19 × 150 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50°C; gradient (% B): 5.0-28% over 3 minutes, 28-33% over 8 minutes, 33-60% over 1 minute; flow rate: 17 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 96.4%. Analytical condition A: retention time = 3.70 minutes, ESI-MS (+) observed value m / z = 1060.97 (M + 2H). ２＋ Example 1-14 Synthesis of Conjugate No. 21 Conjugate No. 2 (10 mg), obtained by the same synthesis method as in Examples 1-4, was dissolved in DMF (0.40 mL), followed by copper(II) chloride dihydrate (0.90 mg, CAS: 10125-13-0) and 100 mM aqueous ammonium acetate (0.20 mL). The reaction mixture was stirred at 40°C for 60 minutes. The resulting reaction mixture was purified using the following conditions: Column: Waters XSelect® C18 5 μm 30 x 150 mm; Mobile phase: A = 1.0% AcOH in water, B = 1.0% AcOH in MeCN; Temperature: 40°C; Gradient (% B): 6.0-31% over 3 minutes, 31-36% over 8 minutes, 36-60% over 1 minute; Flow rate: 45 mL / min). The fractions containing the target product were collected and freeze-dried to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 97.7%. Analytical condition A: retention time = 4.32 minutes ESI-MS (+) observed value m / z = 768.95 (M + 3H) ３＋ Example 1-15 Synthesis of Conjugate No. 22 A cyclic peptide (sequence: ClAc-da-Tbg-3PyCON-Hgl-PeG-Ahp-PeG-S-3PyNH-HseMe-G-Y-MeC-K) (SEQ ID NO: 59) (15 mg) obtained by the same synthesis method as in Example 1-1 was dissolved in DMF (0.40 mL), and DOTA-NHS ester hexafluorophosphate trifluoroacetate (7.8 mg) and DIPEA (0.018 mL) were added under ice cooling. The reaction mixture was stirred at room temperature for 120 minutes. Zirconium(IV) acetylacetonate (5.1 mg, CAS: 17501-44-9) was added to the reaction mixture, which was then stirred at 50°C for 90 minutes, followed by the addition of DOTA (10 mg). The resulting reaction mixture was purified using the following conditions: (Column: Waters XSelect® C18 5 μm 50 × 250 mm; Mobile phase: A = 1.0% AcOH in water, B = 1.0% AcOH in MeCN; Temperature: 50°C; Gradient (% B): 0-0% over 5.1 min, 0-4.2% over 1.9 min, 4.2-25.6% over 3 min, 25.6-30.7% over 15.5 min, 30.7-60% over 1.5 min, 60-90% over 4 min; Flow rate: 18-18 mL / min over 5.1 min, 18-118 mL / min over 1.9 min, then 118 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target substance was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target substance was 99.7%. Analytical condition A: retention time = 3.66 minutes ESI-MS (+) observed value m / z = 1165.62 (M+H) ２＋ Example 1-16 Synthesis of Conjugate No. 45 The target peptide (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk-Y-MeCt) (SEQ ID NO: 60) was synthesized using Cl-Trt(2-Cl) resin (Watanabe Chemical) and Fmoc-MeCt (CAS: 2932449-54-0) as starting materials, using a solid-phase resin (1.007 mmol / g, 0.500 g) supported in the same manner as in the synthesis method described in Tetrahedron Letters, 43 (2002) 3419-3421. A CEM Liberty Blue solid-phase synthesizer was used, and the synthesis was carried out according to the manufacturer's instructions. The cyclic peptide was synthesized in the same manner as in Example 1-2, and the introduction of the chelating agent and metal was carried out under the same reaction and purification conditions as in Example 1-7 to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 99.5%. Analytical condition A: retention time = 3.85 minutes ESI-MS (+) observed value m / z = 760.33 (M + 3H) ３＋ Example 2 Synthesis of Cyclic Peptides and Synthesis of Conjugates Following the general method described in Example 1, the peptides of interest and conjugates of the peptides with payloads shown in the table below were synthesized. Table 7 lists the target peptides, analytical conditions and retention times, and ESI-MS(+) observations, while Table 8 lists the target conjugates, analytical conditions and retention times, and ESI-MS(+) observations. In Table 7, terminus indicates the C-terminal functional group (in the table, "-OH" indicates COOH, and "-NH" indicates CO(NH)), and no description indicates that no functional group is present at the C-terminus. Furthermore, for "Cyclization" in the table, the description of ClAc indicates that the first amino acid to which a chloroacetyl group has been introduced is cyclized by bonding with C or MeC present at the C-terminus, and "Free" indicates that the N-terminal amino group of the first amino acid is bonded to the C-terminal carboxy group of the 13th or 14th amino acid. Furthermore, Additional / Linker in the table indicates a linker or additional amino acid not included in the cyclic structure. For example, in Ca9_No1 (SEQ ID NO: 3), the amino acid sequence of X1-X13 forms a cyclic structure, and glycine is further added as a linker from the C of X13 at the C-terminus. Table 8 also uses the same notation method as Table 7 above. Furthermore, in Table 8, the payload is what is written in parentheses (). For example, the conjugate of Conjugate No. 1 has a cyclic structure formed by the amino acid residues X1 and X13 at C, and further includes a linker structure called G-PEG10c-K from the C of X13, with SulfoCy5 bound to the side chain of the terminal K as a payload. Furthermore, Conjugate No. Conjugate No. 6 shows that the amino acid residues MeC at X1 and X13 form a cyclic structure, and the side chain of dk at X1 is bound to the payload, Lu-bound DOTA. Furthermore, conjugate No. 19 shown in Table 8 similarly shows that the amino acid residues MeC at X1 and X13 form a cyclic structure, and the side chain of dk at X1 is bound to the payload, Lu-bound DOTA, via df. Furthermore, NT in Table 8 indicates not tested.Example 3: Test for evaluating intermolecular interactions between human CA9 and peptides or conjugates by surface plasmon resonance (SPR) For the various peptides or conjugates synthesized in Examples 1 and 2, the intermolecular interactions of the peptides with human CA9 protein were tested by surface plasmon resonance (SPR) using the method shown below. The specific test method is shown below. SPR Measurement: A Protein A sensor chip (Cytiva) was inserted into a Biacore T200 (Cytiva), and the column was primed with running buffer: 1X HBS-P+ (Cytiva), 1.0% DMSO (Fujifilm Wako Pure Chemical Industries), and 50 μM zinc acetate dihydrate (Hampton Research), followed by equilibration at a flow rate of 30 μL / min. 50 nM Human CA9-Fc (SinoBiological) diluted with running buffer was reacted for 60 seconds at a flow rate of 5 μL / min and captured onto the flow cell. The peptide or conjugate solution synthesized in Example 1 or 2, prepared at 1 mM in DMSO, was diluted with running buffer to a final concentration of 100 nM, and then 25 nM or 5 nM peptide or conjugate solutions were prepared. Furthermore, depending on the affinity of the peptide or conjugate, the solution was diluted with running buffer to a final concentration of 40 nM, and then 10 nM or 2 nM peptide or conjugate solutions were prepared. The kinetics of the peptide or conjugate binding to human CA9 was measured using the above samples by SPR measurement. The kinetics evaluation model was Single Cycle Kinetics, and curve fitting was performed using Biacore T200 Evaluation Software Version 3.0 (Cytiva). The resulting sensorgrams were subjected to least-squares curve fitting, and the KD values ​​were calculated to evaluate the binding of the peptides or conjugates to human CA9. The results are shown in Tables 7 and 8. As shown in Tables 7 and 8, the peptides and conjugates of the present invention were shown to have binding activity to human CA9. Reference Example: Synthesis of Unnatural Amino Acids This Reference Example provides examples of the synthesis of various unnatural amino acids.In the Reference Examples, the following instruments, abbreviations, analytical conditions, etc. were used unless otherwise specified. Proton nuclear magnetic resonance (H-NMR) in the following Synthesis Examples was measured in a deuterated chloroform or deuterated dimethyl sulfoxide solvent using a JEOL JNM-ECP300 or a JEOL JNM-ECX300, or a Bruker Ascend™500, unless otherwise specified, and the chemical shifts are shown as δ values ​​(ppm) using tetramethylsilane as the internal standard (0.0 ppm). In the description of NMR spectra, "s" means singlet, "d" means doublet, "t" means triplet, "q" means quartet, "dd" means doublet of doublets, "dt" means doublet of triplets, "m" means multiplet, "br" means broad, "J" means coupling constant, "Hz" means Hertz, "CDCl" means deuterated chloroform, and "DMSO-d" means deuterated dimethyl sulfoxide. Unless otherwise specified, high-performance liquid chromatography / mass spectrometry was measured using either a Waters ACQUITY UPLC H-Class / QDa, a Waters ACQUITY UPLC H-Class / SQD2, or a Shimadzu LC-20AD / Triple Tof5600. In the description of high performance liquid chromatography / mass spectrometry, ESI+ refers to the positive mode of electrospray ionization, and (M+H)+ refers to the protonated ion. (M-C4H8+H)+ refers to the ion resulting from protonation and tertiary butyl group elimination. In the description of high performance liquid chromatography / mass spectrometry, ESI- refers to the negative mode of electrospray ionization, and M-H refers to the ion resulting from proton elimination. Analysis Condition C Column: ACQUITY® 1.7 μm BEH C18, 2.1 x 100 mm, Waters Mobile Phase A: 0.025% TFA in water Mobile Phase B: 0.025% TFA in CH4. ３ In CN, Column temperature: 60°C, Gradient (% B): 5-95% over 5.56 minutes, then 95% from 5.56 minutes to 7.22 minutes, Flow rate: 0.6 mL / min, Detection: UV 254 nm. Reference Example 1 Synthesis of Fmoc-4COOPeG(tBu)-OHMethyl 2-aminoacetate hydrochloride (10 g, CAS: 5680-79-5) was dissolved in MeOH (200 mL, CAS: 67-56-1) at room temperature, and triethylamine (16.12 g, CAS: 121-44-8) and tert-butyl acrylate (20.42 g, CAS: 1663-39-4) were added. The reaction mixture was stirred at room temperature for 2 hours and then concentrated under reduced pressure. The resulting residue (15 g) was dissolved in DCM (150 mL, CAS: 75-09-2), and DIPEA (35.69 g, CAS: 7087-68-5) and N-[(9H-fluoren-9-ylmethoxy)carbonyloxy]succinimide (22.12 g, CAS: 82911-69-1) were added under ice cooling. After stirring at room temperature for 2 hours, the reaction was quenched by the addition of 1M hydrochloric acid (300 mL, CAS: 7647-01-0). The mixture was extracted with DCM, and the resulting organic layer was washed with saturated brine and dried over sodium sulfate. After filtration and concentration under reduced pressure, the resulting residue was purified by silica gel column chromatography (petroleum ether / ethyl acetate = 1 / 1), and the fraction containing the target product was concentrated under reduced pressure. The product (31 g) obtained in the above reaction was dissolved in DCM (300 mL), and a 4M HCl solution in 1,4-dioxane (300 mL) was added under ice-cooling. The reaction mixture was stirred at room temperature for 2 hours and then concentrated under reduced pressure. The resulting residue (25 g) was dissolved in DCM (150 mL) at room temperature, and 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (18.75 g, CAS: 25952-53-8) and N-hydroxyphthalimide (11.70 g, CAS: 524-38-9) were added. The reaction mixture was stirred at room temperature for 2 hours, and then saturated aqueous sodium bicarbonate (200 mL) was added to quench the reaction. The resulting mixture was washed with saturated brine and dried over sodium sulfate. After filtration and concentration under reduced pressure, the resulting residue was purified by silica gel flash column chromatography (petroleum ether / ethyl acetate = 1 / 1), and the fraction containing the target product was concentrated under reduced pressure. Under a nitrogen atmosphere, nickel(II) bromide trihydrate (4.64 g, CAS: 7789-49-3) and 4,4′-di-tert-butyl-2,2′-dipyridyl (4.57 g, CAS: 72914-19-3) were added to N,N-dimethylacetamide (300 mL, CAS: 127-19-5), and the mixture was stirred at room temperature for 15 minutes.To the resulting mixture, tert-butyl 4-bromobenzoate (29.19 g, CAS: 59247-47-1) and the product from the previous reaction (30 g) were added, followed by the addition of zinc (18.56 g, CAS: 7440-66-6) over 10 minutes at room temperature. The reaction mixture was stirred at room temperature for 30 minutes. Water was added to the mixture to quench the reaction, and the insoluble matter was filtered and washed with ethyl acetate. The filtrate was extracted with ethyl acetate, and the resulting organic layer was washed with saturated brine and dried over sodium sulfate. After filtration and concentration under reduced pressure, the resulting residue was purified by silica gel flash column chromatography (petroleum ether / ethyl acetate = 1 / 1), and the fraction containing the target product was concentrated under reduced pressure. The resulting product (20 g) was dissolved in isopropyl alcohol (600 mL, CAS: 67-63-0), and an aqueous solution (150 mL) of calcium chloride (68.88 g, CAS: 10043-52-4) and an aqueous solution (50 mL) of lithium hydroxide (3.72 g, CAS: 1310-65-2) were added under ice-cooling. The reaction mixture was stirred at room temperature for 16 hours. The mixture was adjusted to pH 5 with saturated aqueous sodium dihydrogen phosphate (CAS: 7558-80-7) and then extracted with ethyl acetate. The combined organic layer was washed with saturated brine and dried over sodium sulfate. After filtration and concentration under reduced pressure, the resulting residue was purified by reverse-phase silica gel flash column chromatography (column: C18 silica gel, gradient: 10 mM aqueous ammonium bicarbonate / acetonitrile = 95 / 5-0 / 100). The fraction containing the target product was concentrated under reduced pressure to give the title compound (10.1 g). 1H NMR (500MHz, DMSO-d6) δ12.68 (br, 1H), 7.92-7.86 (m, 2H), 7.86-7.55 (m, 4H), 7.47-7.00 (m, 6H), 4.52-4. 45 (m, 1H), 4.28-4.14 (m, 2H), 4.00-3.69 (m, 2H), 3.56-3.07 (m, 2H), 2.91-2.41 (m, 2H), 1.55-1.51 (m, 9H). Analysis conditions C: retention time = 5.44 minutes; ESI-MS (+) observed value m / z = 446 (M-C4H8+H). ＋ , theoretical m / z = 501. Reference Example 2 Synthesis of Fmoc-3COOPeG(tBu)-OH Fmoc-3COOPeG(tBu)-OH was obtained by the same synthesis as in Reference Example 1 for Fmoc-4COOPeG(tBu)-OH, except that tert-butyl 3-bromobenzoate (CAS: 69038-74-0) was used as a starting material instead of tert-butyl 4-bromobenzoate. 1H NMR (500MHz, DMSO-d6) δ12.70 (br, 1H), 7.92-7.82 (m, 2H), 7.81-7.55 (m, 4H), 7.52-7.10 (m, 6H), 4.51-4. 32 (m, 1H), 4.32-4.09 (m, 2H), 4.09-3.74 (m, 2H), 3.53-3.12 (m, 2H), 2.92-2.46 (m, 2H), 1.55-1.47 (m, 9H). Analysis condition C: retention time = 5.19 minutes; ESI-MS (+) observed value m / z = 446 (M-C4H8+H) ＋ , theoretical m / z = 501. Example 4 ６７ Biodistribution of Ga-labeled conjugates to peptides ６７Ga-labeled The following conjugates were synthesized in Examples 1 and 2 or by a similar method: Conjugate No. 65, Conjugate No. 64, Conjugate No. 70 (a conjugate in which the payload portion of Conjugate No. 18 is only DOTA and no lutetium is bound (sequence: ClAc-de-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-D-3Py6NH2-HseMe-dk(DOTA)-Y-MeC) (DOTA is bound to the side chain of dk, position 11, in the amino acid sequence set forth in SEQ ID NO: 73)), Conjugate No. Conjugate No. 71 (a conjugate in which the payload portion of Conjugate No. 29 is only DOTA and no lutetium is bound (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-D-5Inda-HseMe-dk(DOTA)-Y-MeC) (DOTA is bound to the side chain of the 11th dk in the amino acid sequence set forth in SEQ ID NO: 77), Conjugate No. 72 (Conjugate Conjugate No. 15, in which the payload portion is only DOTA and no lutetium is bound (sequence: ClAc-dk(DOTA)-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-D-3Py6NH2-HseMe-dq-Y-MeC) (DOTA is bound to the side chain of the first dk in the amino acid sequence set forth in SEQ ID NO: 70), Conjugate No. 62, and Conjugate No. 73 (Conjugate Conjugate No. 31 in which the payload portion is only DOTA-t4amCh and no lutetium is bound (sequence: ClAc-da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-D-5Inda-HseMe-dk(DOTA-t4amCh)-Y-MeC (DOTA is bound to the side chain of dk at position 11 of the amino acid sequence set forth in SEQ ID NO: 77 via t4amCh)). A labeling reaction solution (Table 9) containing each conjugate was heated at 95°C for 10 minutes, ６７ Ga labeling was performed. Radio-HPLC: Each of the compounds synthesized as described above ６７After mixing the Ga-labeled conjugate (hereinafter also referred to as the test substance) with acetonitrile, the radiochemical purity was measured before and after administration using TSK gel® ODS-80Ts QA, 4.6 mm ID x 250 mm, 5 μm (Tosoh Corporation). The result was a purity of 95.61-91.27%. Radio-TLC: The test substance was spotted on TLC silica gel 60 RP-18 F. ２５４ After development with a 2 mol / L ammonium acetate solution / acetone mixture (1:1), radioactivity was measured using a radiochromator (energy range 60-350 keV, collimator 1.0 cm, V-shaped BGO crystal, measurement time 10 min). The resulting purity was 96.67-94.27%. Preparation of Evaluation Animals (HT-29 Tumor-Bearing Mice) Five-week-old female BALB / cSlc-nu / nu mice were purchased from Japan SLC (Shizuoka, Japan) and used to prepare evaluation animals. After acclimation, 5 × 10 cells were suspended in a 1:2 mixture of PBS pH 7.4 (1×) (Thermo Fisher Scientific, 10010-023) and VitroGel (The Well Bioscience, VHM01). ７ The cells were suspended in HT-29 cells / mL, which are CA9-positive cells derived from human colon cancer, and 0.1 mL of the suspension was subcutaneously implanted in the right flank of nude mice (6 weeks old) using a disposable syringe with a needle. A total of 12 groups of animals were used, with 3 animals per group. The animals weighed 18.2 g to 20.7 g and had tumor diameters of 216 to 908 mm. ３ Biodistribution Each test substance was administered intravenously once to HT-29 tumor-bearing mice. Dissection was performed 4, 24, and 72 hours after administration, and the radioactivity concentration (% ID / g) of each tissue was measured. Results ６７ The results of the biodistribution of the Ga-labeled compound are shown in Figures 1, 2, and 3. Note that "Conjugate No. XX" in the figures indicates that the payload moiety in the conjugate described in the conjugate No. is DOTA- ６７Figure 1 shows the tissue distribution % ID / g at 4 hours after administration (mean ± SD, n = 3). Figure 2 shows the tissue distribution % ID / g at 24 hours after administration (mean ± SD, n = 3). Figure 3 shows the tissue distribution % ID / g at 72 hours after administration (mean ± SD, n = 3). Example 5 ６４ Biodistribution and PET imaging of Cu-labeled conjugates to peptide conjugates ６４ Cu Labeling A labeling reaction solution (Table 10) containing each of the peptide conjugates synthesized in Example 1 or 2, i.e., Conjugate No. 64, Conjugate No. 62, Conjugate No. 2, Conjugate No. 56, and Conjugate No. 58, was heated at 95°C for 10 minutes. ６４ Cu labeling was performed. Radio-HPLC: Each of the compounds synthesized as described above ６４ After mixing the Cu-labeled conjugate (hereinafter also referred to as the test substance) with acetonitrile, the radiochemical purity was measured before and after administration using TSK gel® ODS-80Ts QA, 4.6 mm ID x 250 mm, 5 μm (Tosoh). The result was a purity of 94.14-100%. Radio-TLC: The test substance was spotted on TLC silica gel 60 RP-18 F. ２５４ After development with a 2 mol / L ammonium acetate solution / acetone mixture (1:1), radioactivity was measured using a radiochromator (energy range 60-350 keV, collimator 1.0 cm, V-shaped BGO crystal, measurement time 10 min). The resulting purity was 97.60-98.79%. Preparation of Evaluation Animals (HT-29 Tumor-Bearing Mice) Five-week-old female BALB / cSlc-nu / nu mice were purchased from Japan SLC (Shizuoka, Japan) and used to prepare evaluation animals. After acclimation, 5 × 10 cells were suspended in a 1:2 mixture of PBS pH 7.4 (1×) (Thermo Fisher Scientific, 10010-023) and VitroGel (The Well Bioscience, VHM01). ７The cells were suspended in HT-29 cells / mL, which are CA9-positive cells derived from human colon cancer, and 0.1 mL of the suspension was subcutaneously implanted into the right flank of nude mice (6 weeks old) using a disposable syringe with a needle. A total of 12 groups of animals were used, with 3 animals per group. The animals weighed 17.7 g to 21.5 g and had tumor diameters of 165 to 523 mm. ３ Biodistribution and PET Imaging Each test substance was administered intravenously to HT-29 tumor-bearing mice at a single dose of 80 μL / head. Dissections were performed 4 and 24 hours after administration, and the radioactivity concentration (% ID / g) of each tissue was measured to evaluate biodistribution. In addition, PET imaging was performed by collecting PET / CT images under isoflurane gas anesthesia using Si78 (Bruker BioSpin MRI GmbH) at 1, 4, and 23.5 hours after administration. Results ６４ The results of biodistribution of Cu-labeled compounds are shown in Figures 4 to 7. Figure 4: Tissue distribution % ID / g 4 hours after administration (mean ± SD, n = 3) Figure 5: Tissue distribution % ID / g 24 hours after administration (mean ± SD, n = 3) Figure 6: Tissue distribution % ID / g 4 hours after administration (mean ± SD, n = 3) Figure 7: Tissue distribution % ID / g 24 hours after administration (mean ± SD, n = 3) PET / CT imaging ６４ PET / CT images were collected under isoflurane gas anesthesia 1, 4, and 23.5 hours after administration of the Cu-labeled compound (4.62-4.72 MBq / head). These images are shown in Figures 8-13. Accumulation of each compound in the tumor was confirmed. Each column represents the same individual. For example, the left column shows the results of the same individual 1 hour, 4 hours, and 23.5 hours after administration. The white arrow indicates the transplanted tumor. Figure 8: ６４ Cu-labeled conjugate Conjugate No. 64- ６４ Cu Figure 9: ６４ Cu-labeled conjugate Conjugate No. 62- ６４ Cu Figure 10: ６４ Cu-labeled conjugate Conjugate No. 2 ６４ Cu Figure 11: ６４ Cu-labeled conjugate Conjugate No. 56- ６４ Cu Figure 12: ６４Cu-labeled conjugate Conjugate No. 58- ６４ Cu Example 6 １７７ Efficacy test of Lu-labeled conjugates to peptides １７７ Lu Labeling: A labeling reaction solution (Table 11) containing each of the conjugates synthesized in Example 1 or 2, Conjugate No. 64, Conjugate No. 62, and Conjugate No. 65, was heated at 95°C for 10 minutes. １７７ Lu labeling was performed. Radio-HPLC: Each of the compounds synthesized as described above １７７ The Lu-labeled conjugate (hereinafter also referred to as the test substance) was mixed with acetonitrile, and the radiochemical purity was measured before and after administration using TSK gel® ODS-80Ts QA, 4.6 mm ID x 250 mm, 5 μm (Tosoh). The result was a purity of 90.31-100%. Radio-TLC: The test substance was spotted on TLC silica gel 60 RP-18 F. ２５４After development with a 2 mol / L ammonium acetate solution / acetone mixture (1:1), radioactivity was measured using a radiochromator (energy range 60-350 keV, collimator 1.0 cm, V-shaped BGO crystal, measurement time 10 minutes). The resulting purity was 97.25-98.23%. Preparation of Cabozantinib: As a comparative example, cabozantinib, a known therapeutic agent for renal cell carcinoma and hepatocellular carcinoma, and also known to be effective against colon cancer, was used. Cabozantinib (Selleckchem; No. S1119) was dissolved in DMSO to a concentration of 100 mg / mL, dispensed, and then cryopreserved. This was designated as a cabozantinib DMSO solution. On the day of administration, the cabozantinib DMSO solution was thawed and water for injection was added to achieve a dosing concentration of 30 mg / mL. This was used as the cabozantinib solution. Preparation of Evaluation Animals: Five-week-old female BALB / cSlc-nu / nu mice were purchased from Japan SLC (Shizuoka, Japan) and used to prepare the evaluation animals. After acclimatization, 5 x 10 mice were suspended in a 1:2 mixture of PBS pH 7.4 (1x) (Thermo Fisher Scientific, 10010-023) and VitroGel (The Well Bioscience, VHM01). ７ The cells were suspended in HT-29 derived from human colon cancer at 1000x1000x1000 cells / mL, and 0.1 mL of the suspension was subcutaneously implanted into the right flank of nude mice (6 weeks old) using a disposable syringe with a needle. There were 9 groups of animals, 6 animals per group. The animals weighed 16.28 g to 20.05 g and had tumor diameters of 88 to 229 mm. ３ Drug efficacy evaluation Physiological saline and １７７Lu-labeled peptide was administered intravenously to HT-29 tumor-bearing mice at 30 MBq / head or 60 MBq / head on days 0, 11, and 18. Cabozantinib was administered orally daily from day 0 to day 27 at a dose calculated to be 30 mg / kg based on the body weight data on the day of administration. Body weight and tumor volume were measured twice a week until day 49, and all surviving individuals were euthanized on the final day of measurement. Tumor size results: The progression of tumor size in each group is shown in Figure 13. Conjugate No. 64- １７７ Lu (30 MBq / head, 3 doses), Conjugate No. 62- １７７ Lu (30 MBq / head, 3 doses), Conjugate No. 65- １７７ Conjugate No. 64-Lu (60 MBq / head, single administration) showed excellent antitumor effects. Body weight results The changes in body weight for each group are shown in Figure 14. Conjugate No. 64-Lu (60 MBq / head, single administration) showed excellent antitumor effects. １７７ Lu (30 MBq / head, 3 doses), Conjugate No. 62- １７７ Lu (30 MBq / head, 3 doses) and Conjugate No. 65- １７７ No significant weight loss was observed in the case of Lu (60 MBq / head, single administration). ６４ Cu or １７７ Biodistribution of Lu-labeled conjugates (VMRC-RCW xenograft model) ６４ Cu or １７７ Lu-labeled Conjugate No. 62, ６４ Cu labeling reaction mixture (Table 12) or １７７ The Lu labeling reaction solution (Table 13) was heated at 95°C for 10 minutes to label the peptide. ６４ Cu) Composition of labeling reaction solution (Conjugate No. 62- １７７ Lu) Radio-HPLC Conjugate No. 62-, synthesized as described above ６４ Cu or Conjugate No. 62- １７７After mixing Lu and acetonitrile, the radiochemical purity was measured before and after administration using TSK gel (registered trademark) ODS-80Ts QA, 4.6 mm ID x 250 mm, 5 μm (Tosoh). The result was 100% purity. Radio-TLC for each test substance (Conjugate No. 62- ６４ Cu or Conjugate No. 62- １７７ Lu) spotted on TLC silica gel 60 RP-18 F ２５４ s (Merck, 115389) was developed in a 2 mol / L ammonium acetate solution / acetone mixture (1:1), and radioactivity was measured using a radiochromatizer (measurement time: 10 min). The result showed a purity of 98.26-99.27%. Preparation of Evaluation Animals (VMRC-RCW Tumor-Bearing Mice) Five-week-old female BALB / c-nu mice were purchased from Jackson Laboratory Japan (Kanagawa, Japan) and used to prepare the evaluation animals. After acclimatization, 5 x 10 cells were suspended in EMEM (Fujifilm Wako Pure Chemical Industries, Osaka, Japan). ７ The test substance was suspended in human renal cell carcinoma-derived VMRC-RCW cells at 0.1 mL / mL, and 0.1 mL of the solution was subcutaneously implanted into the right flank of nude mice (6 weeks old) using a disposable syringe with a needle. The animals used for evaluation had a body weight of 18.2 g to 21.0 g and a tumor diameter of 80 to 386 mm. ３ Biodistribution Each test substance was administered intravenously to VMRC-RCW tumor-bearing mice in a single dose. Dissection was performed 4, 24, and 48 hours after administration, and the radioactivity concentration (% ID / g) of each tissue was measured. Results Conjugate No. 62- ６４ The results of Cu distribution in the body are shown in Figure 15. １７７ The results of Lu biodistribution are shown in Figure 16. PET / CT Imaging Conjugate No. 62- ６４ PET / CT images were collected under isoflurane gas anesthesia at 1, 4, 23.5, and 47.5 hours after Cu administration, and it was confirmed that the tumor was clearly detected. Images at each time point are shown in Figure 17. Each column shows the same individual; for example, the left column shows the results of the same individual at 1 hour, 4 hours, 23.5 hours, and 47.5 hours after administration. Example 8 １７７Efficacy test of Lu-labeled peptide (VMRC-RCW xenograft model) １７７ Contains Lu-labeled Conjugate No. 62 １７７ Lu labeling reaction solution for 30 MBq / head administration or 60 MBq / head administration (Table 14) was prepared and heated at 95°C for 10 minutes to perform labeling. １７７ Lu composition Radio-HPLC Conjugate No. 62- synthesized as above １７７ After mixing Lu with acetonitrile, the radiochemical purity was measured before and after administration using TSK gel (registered trademark) ODS-80Ts QA, 4.6 mm ID x 250 mm, 5 μm (Tosoh). The result was a purity of 99.6-100%. Radio TLC Conjugate No. 62- １７７ Lu spotted TLC silica gel 60 RP-18 F ２５４ After development with a 2 mol / L ammonium acetate solution / acetone mixture (1:1), radioactivity was measured using a radiochromator (energy range 13-250 keV, collimator 1.0 cm, V-shaped BGO crystal, measurement time 10 minutes). The resulting purity was 98.1-98.6%. Preparation of Cabozantinib: As a comparative example, cabozantinib (SelleckChem; No. S1119) was dissolved in DMSO to a concentration of 100 mg / mL, dispensed, and then cryopreserved. This was designated the cabozantinib DMSO solution. On the day of administration, the cabozantinib DMSO solution was thawed and water for injection was added to achieve an administration concentration of 12.3 mg / mL. This was designated the cabozantinib solution. Preparation of evaluation animals (VMRC-RCW tumor-bearing mice) Five-week-old female BALB / c-nu mice were purchased from Jackson Laboratory Japan (Kanagawa, Japan) and used to prepare evaluation animals. After acclimatization, 5 × 10 cells were suspended in EMEM (Eagle's minimum essential medium, Fujifilm Wako Pure Chemical Industries, Osaka, Japan). ７The test substance was suspended in human renal cell carcinoma-derived VMRC-RCW cells at 1000x1000 cells / mL, and 0.1 mL of the suspension was subcutaneously implanted into the right flank of nude mice (6 weeks old) using a disposable syringe with a needle. The animals used for evaluation had a body weight of 19.3 g to 21.9 g and a tumor diameter of 216 to 445 mm. ３ Evaluation of efficacy Physiological saline (SAline) and Conjugate No. 62- prepared as above were used. １７７ Lu was administered once (80 μL / head) via the tail vein to mice of each group (8 weeks old on Day 0) as shown in Table 15 below. Cabozantinib was orally administered daily from Day 0 to Day 27 at a dose calculated to be 12.3 mg / kg based on the body weight data on the day of administration. Tumor size results The changes in tumor size in each group are shown in Figure 18. Conjugate No. 62- １７７ Conjugate No. 62-Lu showed excellent antitumor effects. Weight Results The average weight change rate for each group is shown in Figure 19. １７７ No significant weight loss was observed in any of the groups administered with Lu. ２２５ Drug efficacy test and biodistribution of Ac-labeled peptides ２２５ Ac labeling: A labeling reaction solution (Table 16) containing Conjugate No. 62 was heated at 95°C for 20 minutes to perform labeling. ２２５ The Ac-labeled compound was obtained. Composition of the labeling reaction solution (50 μL) Radio-HPLC: After mixing the test substance with acetonitrile, the radiochemical purity before administration was measured using a TSK gel® ODS-80Ts QA, 4.6 mm ID x 150 mm, 5 μm (Tosoh). The result was 97.9% purity. Radio-TLC: After spotting the test substance on TLC silica gel 60 RP-18 F254s (Merck, 115389) and developing it with a 2 mol / L ammonium acetate solution / acetone mixture (1:1), the radioactivity was measured using a radiochromatizer (energy range 180-500 keV, collimator 1.0 cm, V-shaped BGO crystal, measurement time 10 min). The result was 97.7% purity. Preparation of Evaluation Animals (HT-29 Tumor-Bearing Mice) Six-week-old female BALB / cSlc-nu / nu mice were purchased from Japan SLC (Shizuoka, Japan) and used to prepare the evaluation animals. After acclimatization, 5 x 107 cells / mL of human colon cancer-derived HT-29 cells were suspended in a 1:2 mixture of PBS pH 7.4 (1x) (Thermo Fisher Scientific, 10010-023) and VitroGel (The Well Bioscience, VHM01). 0.1 mL of the suspension was implanted subcutaneously into the right flank of nude mice (7 weeks old) using a disposable syringe with a needle. Three groups of evaluation animals were used, with three animals per group. The animals used for evaluation had body weights of 17.8g to 19.63g and tumor diameters of 151 to 275mm3. ２２５ The Ac-labeled compound was administered intravenously once to HT-29 tumor-bearing mice (9 weeks old). Dissection was performed 4, 24, and 48 hours after administration, and the radioactivity concentration (% ID / g) of each tissue was measured. ２２５ The results of biodistribution of Ac-labeled compounds are shown in Figure 20. Example 10 ２２５ Drug efficacy test of Ac-labeled peptide ２２５ Ac Labeling: The labeling reaction solution (Table 17) containing Conjugate No. 62 was heated at 95°C for 20 minutes to perform labeling, thereby obtaining the test substance. Radio-HPLC: The radiochemical purity of the test substance was measured before administration using a Jupiter® C18 5 μm 4.6 x 150 mm (Phenomenex). The result was 97.25% purity. Radio-TLC: The test substance was spotted on TLC-SG Paper (Agilent, SGI0001) and developed with 25 mM EDTA and 0.1 mol / L ammonium acetate solution. Radioactivity was measured using a Bioscan AR-2000 (Eckert & Ziegler). The result was a purity of 99% or more. Preparation of Evaluation Animals (HT-29 Tumor-Bearing Mice): Five-week-old female BALB / cSlc nude mice were purchased from Charles River Laboratories (Wilmington, USA) and used to prepare the evaluation animals. After acclimatization, the cells were suspended in a 1:2 mixture of PBS pH 7.4 (1x) (Thermo Fisher Scientific, 10010-023) and VitroGel (The Well Bioscience, VHM01) at 5x107 cells / mL of human colon cancer-derived HT-29 cells, and 0.1 mL of the suspension was implanted subcutaneously into the right flank of nude mice (7 weeks old) using a disposable syringe with a needle. Six groups of 10 animals were used for evaluation. ２２５ The animals evaluated on the day before administration of Ac-labeled peptide had a body weight of 16.95 g to 17.83 g and a tumor diameter of 189.08 to 201.72 mm3. ２２５ Ten days after HT-29 cell transplantation, Ac-labeled peptide was administered intravenously to HT-29 tumor-bearing mice at 30 kBq / head, 60 MBq / head, 90 MBq / head, 120 MBq / head, or 150 MBq / head. Body weight and tumor volume were measured twice a week until Day 70, and all surviving mice were euthanized on the final day of measurement. Tumor size results: The progression of tumor size in each group is shown in Figure 21. ２２５ Ac-labeled Conjugate No. 62 exhibited an excellent antitumor effect in a radioactivity-dependent manner. Body Weight Results Figure 22 shows the changes in body weight for each group. ２２５No significant weight loss was observed due to the administration of Ac-labeled Conjugate No. 62. Example 11 Synthesis of Cyclic Peptides and Conjugates Example 11-1 Conjugate Synthesis of Conjugate No. 74 The peptide conjugate Conjugate No. 62 (10 mg) obtained in Example 1-5 was dissolved in 100 mM aqueous sodium acetate solution (0.465 mL), and lanthanum(III) chloride heptahydrate (25.9 mg, CAS: 10025-84-0) was then dissolved in the solution. The reaction mixture was stirred at 45° C. for 60 minutes. The resulting reaction mixture was purified using the following conditions: (Column: Waters XSelect® C18 5 μm 50 × 250 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 50°C; Gradient (% B): 0-0% over 5 min, 0-4.2% over 2 min, 4.2-24.6% over 3 min, 24.6-29.7% over 15.5 min, 29.7-60% over 1.5 min, 60-90% over 4 min; Flow rate: 18-18 mL / min over 5.0 min, 18-118 mL / min over 2 min, then 118 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target substance was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target substance was 96.5%. Analytical condition A: retention time = 3.54 minutes ESI-MS (+) observed value m / z = 1143.45 (M + 2H) ２＋ Example 11-2 Synthesis of Conjugate No. 75 Peptide SEQ ID No. 46 (10 mg) obtained in Example 1-2, DIEA (15.7 μL), and DOTA-NHS ester hexafluorophosphate trifluoroacetate (5.04 mg) were dissolved in DMF (0.50 mL) at 0°C. The reaction mixture was stirred at room temperature for 60 minutes, after which gallium(III) chloride (3.52 mg, CAS: 13450-90-3) and 50 mM aqueous sodium acetate solution (0.40 mL) were added to the reaction mixture. The reaction mixture was stirred at 90°C for 1 hour. The resulting reaction mixture was purified using the following conditions (column: Waters XBridge® C18 5 μm 30 × 150 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50°C; gradient (% B): 5.0-27% over 3 min, 27-32% over 8 min, 32-60% over 1 min; flow rate: 45 mL / min). Fractions containing the target product were collected and lyophilized to obtain the target peptide. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target product was 99.5%. Analytical condition A: retention time = 3.24 min, ESI-MS (+) observed value m / z = 1108.94 (M + 2H). ２＋ Example 11-3 Synthesis of Conjugate No. 78 A cyclic peptide (sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk(Alloc)-Y-MeA-MeG (SEQ ID NO: 103)) was synthesized in a similar manner to Conjugate No. 67. Fmoc-dk(Alloc)-OH was used instead of Fmoc-dk(Boc)-OH. Purification was carried out under the following conditions: Column: Waters XBridge® C18 5 μm 50 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 40°C; Gradient (% B): 8-8% over 2 min, 8-33% over 1 min, 33-38% over 8 min, 38-60% over 1 min; Flow rate: 20-20 mL / min over 1 min, 20-120 mL / min over 1 min, then 120 mL / min. Fractions containing the desired product were collected and lyophilized. The cyclic peptide (38 mg) obtained by the above method was dissolved in DMF (0.65 mL), and 2,4,6-trimethylpyridine (25.8 μL, CAS: 108-75-8) and a 0.5 M HATU DMF solution (58.7 μL) were added and stirred at 25 °C for 5 minutes. Fmoc-Qglucamine-NH (50 mg) was dissolved in DMSO (0.94 mL), and TEA (0.20 mL) was added. The mixture was stirred at 60 °C for 1 hour, then concentrated under reduced pressure using a Biotage V-10 tube. A DMSO solution (0.50 mL) of H-Qglucamine-NH (7.9 mg), synthesized by trituration with methyl tertiary butyl ether, was added to the cyclic peptide reaction solution and stirred for 2 hours. Water (50 μL) was added, and the mixture was concentrated under reduced pressure using a Biotage V-10 tube. The resulting mixture was dissolved in DMF (0.67 mL), and phenylsilane (25 μL, CAS: 694-53-1) and Pd(PPh3)4 (4.6 mg, CAS: 14221-01-3) were added. The mixture was stirred at room temperature for 50 minutes. DIPEA (68 μL) and DOTA-NHS TFA salt (36 mg, CAS: 2832911-57-4) were added to the resulting mixture, and the mixture was stirred overnight at 25 °C. After adding water (100 μL), half of the resulting mixture was diluted with DMSO (1 mL) and water (1 mL) and then stirred with 0.5 M lutetium(III) chloride in ammonium acetate (2.4 mL, pH 5.0) at 90 °C for 1 hour.The resulting suspension was concentrated under reduced pressure using a Biotage V-10 column and dissolved in DMSO / water (9 / 1, 4 mL). The resulting aqueous solution was purified using the following conditions: column: Waters XSelect® C18 5 μm 50 × 250 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50 °C; gradient (% B): 0-0% over 5 min, 0-4.2% over 2 min, 4.2-19.5% over 3 min, 19.5-24.6% over 15.5 min, 24.6-60% over 1.5 min; flow rate: 18-18 mL / min over 5 min, 18-118 mL / min over 2 min, then 118 mL / min). The fractions containing the target product were collected and lyophilized. The purity of the target substance was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under the analytical conditions. The purity of the target substance was 97.7%. Analytical condition B: retention time = 5.72 minutes ESI-MS (+) observed value m / z = 865.85 (M + 3H). ３＋ Example 11-4 Synthesis of Conjugate No. 79 A cyclic peptide (sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-pHPeG-S-5Inda-HseMe-dk(Alloc)-Y-MeA-MeG (SEQ ID NO: 103)) was synthesized in a similar manner to Conjugate No. 67. Fmoc-dk(Alloc)-OH was used instead of Fmoc-dk(Boc)-OH. Purification was carried out under the following conditions: Column: Waters XBridge® C18 5 μm 50 × 150 mm; Mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; Temperature: 40°C; Gradient (% B): 8-8% over 2 min, 8-33% over 1 min, 33-38% over 8 min, 38-60% over 1 min; Flow rate: 20-20 mL / min over 1 min, 20-120 mL / min over 1 min, then 120 mL / min. Fractions containing the desired product were collected and lyophilized. The cyclic peptide (38 mg) obtained by the above method was dissolved in DMF (0.65 mL), and 2,4,6-trimethylpyridine (25.8 μL, CAS: 108-75-8) and a 0.5 M HATU DMF solution (58.7 μL) were added at 25°C and stirred for 5 minutes. A DMSO solution (0.50 mL) of H-KCOpipzaa(Mpe)-NH2 (10.2 mg) was added to the cyclic peptide reaction solution and stirred for 1.5 hours. After adding water (50 μL), the mixture was concentrated under reduced pressure using a Biotage V-10 column. The resulting mixture was dissolved in TFA / TIS / HO (95 / 2.5 / 2.5, 0.5 mL) and stirred for 30 minutes. The resulting mixture was added to diisopropyl ether / heptane (1 / 1, 5 mL) and the resulting solid was centrifuged. The supernatant was removed and washed with diisopropyl ether / heptane (1 / 1, 5 mL). After drying under reduced pressure, the residue was dissolved in DMF (0.67 mL), and phenylsilane (25 μL, CAS: 694-53-1) and Pd(PPh3)4 (4.6 mg, CAS: 14221-01-3) were added, followed by stirring at room temperature for 50 minutes. DIPEA (68 μL) and DOTA-NHS TFA salt (36 mg, CAS: 2832911-57-4) were added to the resulting mixture, followed by stirring at 25 °C overnight.After adding water (100 μL), half of the resulting mixture was diluted with DMSO (1 mL) and water (1 mL) and then stirred with 0.5 M lutetium(III) chloride in ammonium acetate (2.4 mL, pH 5.0) for 1 hour at 90° C. The resulting suspension was concentrated under reduced pressure using a Biotage V-10 and then dissolved in DMSO / water (9 / 1, 4 mL). The resulting aqueous solution was purified under the following conditions (column: Waters XSelect® C18 5 μm 50 × 250 mm; mobile phase: A = 0.1% TFA in water, B = 0.1% TFA in MeCN; temperature: 50 °C; gradient (% B): 0-0% over 5 min, 0-4.2% over 2 min, 4.2-19.5% over 3 min, 19.5-24.6% over 15.5 min, 24.6-60% over 1.5 min; flow rate: 18-18 mL / min over 5 min, 18-118 mL / min over 2 min, then 118 mL / min). The fractions containing the target product were collected and lyophilized. The purity of the target product was calculated from the area ratio of the LC / MS (UV wavelength 225 nm) chromatogram under analytical conditions. The purity of the target product was 96.6%. Analysis conditions B: Retention time = 5.70 minutes ESI-MS (+) Observed value m / z = 867.91 (M+3H). ３＋ Example 11-5 Synthesis of Conjugates According to the general methods described in Examples 1 and 11-1 and 11-2, the target peptides and conjugates of the peptides and payloads shown in the table below were synthesized. Table 18 lists the target conjugate, analytical conditions, retention time, and ESI-MS+ observations. In Table 18, terminus indicates the C-terminal functional group (in the table, "-OH" indicates COOH, and "-NH" indicates CO(NH)), and the absence of a description indicates the absence of a functional group at the C-terminus. Furthermore, for "Cyclization" in the table, the presence of ClAc indicates that the first amino acid to which a chloroacetyl group has been introduced is cyclized by binding with C or MeC present at the C-terminus, and "Free" indicates that the N-terminal amino group of the first amino acid is bound to the C-terminal carboxy group of the 13th or 14th amino acid. Furthermore, for example, the conjugate of Conjugate No. 75 indicates that the amino acid residues C of X1 and X13 form a cyclic structure, and further, the side chain of dk of X11 is bound to Ga-bound DOTA, which is the payload. Furthermore, Conjugate No. 76 shown in Table 8 similarly shows that the amino acid residues MeG at X1 and X14 form a cyclic structure, and the side chain of dk at X11 is bound to the payload, Lu-bound DOTA. Table 19 shows only the amino acid sequences of the peptide portions contained in the peptides and conjugates synthesized in Examples 2 and 11-3. Table 20 also shows a comparison table of the conjugates synthesized and evaluated in these Examples with the SEQ ID No. of the amino acid sequence contained in the cyclic structure portion of the conjugate. Note that for Conjugate Nos. 2-5, 21, 22, 35, 38, and 49, the amino acid sequences are listed as 4 (59), 4 (62), 76 (55), 46 (57), and 88 (86), respectively. This indicates that, for example, in Conjugate No. 2, the amino acid sequence contained in the cyclic structure portion is the amino acid sequence listed in SEQ ID No. 4, and the peptide-linker complex in which K (lysine) is attached to the C-terminus as a linker for attaching the payload, DOTA, is the amino acid sequence represented by SEQ ID No. 59. In addition, in Conjugate No. 35, the amino acid sequence contained in the cyclic structure portion is the amino acid sequence set forth in SEQ ID No. 76, and the peptide-linker complex in which F (phenylalanine) as a linker for binding the payload DOTALu is bound to the side chain of the 11th dk in the amino acid sequence contained in the cyclic structure portion is the amino acid sequence set forth in SEQ ID No. 56. Similarly, in Conjugate No. 38, the amino acid sequence contained in the cyclic structure portion is the amino acid sequence set forth in SEQ ID No. 46, and the peptide-linker complex in which the linker PEG8c for binding the payload SulfoCy5 is bound to the side chain of the 11th dk in the amino acid sequence contained in the cyclic structure portion is the amino acid sequence set forth in SEQ ID No. 57. That is, the numbers shown in parentheses in Table 20 indicate the amino acid sequence SEQ ID No. when a linker or additional amino acid is bound. For example, Conjugate No. 1 is a conjugate having the amino acid sequence shown in SEQ ID No. 2 as a cyclic structural portion, and further having SulfoCy5 as a payload bound via linkers of G, PEG10c, and K added to the C-terminus.Here, both conjugates containing only the cyclic amino acid sequence portion as shown in Table 7 and conjugates containing a payload as shown in Table 8 have the ability to bind to CA9. Furthermore, there are several conjugates (Conjugate Nos. 14, 37, 55, 57, and 64) that contain the amino acid represented by SEQ ID No. 45 as the cyclic structural portion and differ only in the payload. However, even conjugates containing SEQ ID No. 45 without a payload, various chelating agents such as DOTA, structures in which metal ions are bound to such chelating agents, and low molecular weight substances such as SulfoCy5 all have the ability to bind to CA9. In other words, if a certain conjugate has the ability to bind to CA9, it is clear that a cyclic peptide having the amino acid sequence of the cyclic structural portion contained in the conjugate but not containing a payload, or a conjugate with a different payload, also has the ability to bind to CA9. Thus, the peptides of the present invention have the ability to bind to CA9 regardless of the presence or absence of a payload and the type of payload. Reference Example 3: Synthesis of Fmoc-Qglucamine-NH2. To a DMF solution (3.3 mL) of N2-(((9H-fluoren-9-yl)methoxy)carbonyl)-N5-((2S)-2-hydroxy-2-((4'R,5S)-2,2,2',2'-tetramethyl-[4,4'-bi(1,3-dioxolane)]-5-yl)ethyl)-L-glutamine (200 mg, CAS: 1227510-37-3) and ammonium chloride (34.9 mg, CAS: 12125-02-9), DIPEA (0.14 mL) and HATU (0.19 mg) were added and stirred at 0°C for 1 hour. The mixture was purified by silica gel flash column chromatography (DCM / MeOH = 100 / 0 to 80 / 20), and the fraction containing the target product was collected. A portion of the obtained compound (111 mg) was dissolved in DCM (2.7 mL) and ethanol (1.8 mL) and stirred with TFA (1 mL) at 25° C. for one week. The obtained suspension was diluted with methyl tert-butyl ether and centrifuged. After removing the supernatant, the mixture was triturated with methyl tert-butyl ether to obtain the title compound. ESI-MS (+) Observed value m / z = 532.2 (M+H) ＋Reference Example 4: Synthesis of H-KCOpipzaa(Mpe)-NH To a DMF solution (3.2 mL) of N2-(((9H-fluoren-9-yl)methoxy)carbonyl)-N6-(4-(2-((3-methylpentan-3-yl)oxy)-2-oxoethyl)piperazine-1-carbonyl)-L-lysine (200 mg, CAS: 2973753-38-5) and ammonium chloride (34.4 mg, CAS: 12125-02-9), DIPEA (0.14 mL) and HATU (0.18 mg) were added and stirred at 25°C for 2 hours. The mixture was purified by silica gel flash column chromatography (DCM / MeOH = 100 / 0 to 90 / 10), and the fraction containing the target product was collected. A portion of the obtained compound (100 mg) was dissolved in DMSO (1.6 mL), TEA (0.34 mL) was added, and the mixture was stirred at 60°C for 1 hour. The mixture was concentrated under reduced pressure using a Biotage V-10 column and triturated with methyl tertiary butyl ether to give the title compound. ESI-MS (+) observed value m / z = 400.3 (M+H). ＋

[0010] The peptides and conjugates according to the present invention have CA9 binding activity and can be used as pharmaceutical compositions, diagnostic compositions, research compositions, etc. for the prevention or treatment of CA9-related conditions.

Claims

1. A peptide comprising the following amino acid sequence: da-Tbg-3Py6CON-Hgl-Meda-Ahp-PeG-S-3Py6NH2-HseMe-dk-Y (SEQ ID NO: 1); or an amino acid sequence having a substitution, addition, deletion or insertion at 1 to 10 amino acid residues selected from the group consisting of the 1st, 2nd, 3rd, 4th, 5th, 7th, 8th, 9th, 10th and 11th amino acid residues of the above amino acid sequence.

2. The peptide according to claim 1, wherein: (1) MeC, C or MeCt is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO:1; or (2) MeA, MeS, MeN, Hpr, G or P is added as the 13th amino acid residue to the amino acid sequence of SEQ ID NO:1, and further MeG, G, da or Meda is added as the 14th amino acid residue to the amino acid sequence of SEQ ID NO:

1.

3. The peptide described in claim 1 or 2, comprising an amino acid sequence having substitutions, additions, deletions or insertions in 1 to 7 amino acid residues selected from the group consisting of the 1st, 4th, 7th, 8th, 9th, 10th and 11th amino acid residues of the amino acid sequence of SEQ ID NO:

1.

4. The following: the first amino acid residue is da, dq, de, dhgl, or dk; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is S, Hgl, Hgl(PEG8Me), alT, Hgn, SMe, KCOpipzaa, or DabAc; the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa; the 7th amino acid residue is PeG, pMeOPeG, MsMeapG, 3OMePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 4OMePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the 8th amino acid residue is H, S, P, D, KCOpipzaa, Q(PEG8Me), P4Sh, Hse, SMe, Qmm, or Qdm; the 9th amino acid residue is 3Py6NH2, 5Inda, Y, or F4OMe; the 10th amino acid residue is Ahp, HseMe, or E; and The peptide according to any one of claims 1 to 3, which satisfies one or more of the following requirements: the 11th amino acid residue is dk, G, da, dq, dkCOpipzaa, dk(t4amCh), de, Acb, or dkAc.

5. A peptide according to any one of claims 1 to 4, which satisfies one or more of the following requirements: the second amino acid residue is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe.

6. A peptide according to any one of claims 1 to 4, wherein the second amino acid residue is Tbg; the third amino acid residue is 3Py6NH2; the fifth amino acid residue is Meda; the seventh amino acid residue is PeG or pHPeg; the ninth amino acid residue is 3Py6NH2 or 5Inda; and the tenth amino acid residue is HseMe.

7. A peptide according to any one of claims 1 to 6, comprising or consisting of an amino acid sequence set forth in any one of SEQ ID NOs: 2 to 54.

8. A peptide according to any one of claims 1 to 7, further comprising additional amino acid residues.

9. The peptide of any one of claims 1-8, wherein the peptide is a cyclic peptide.

10. A peptide described in any one of claims 1 to 9, having a cyclic structure in which the first amino acid residue of the chloroacetylated amino acid sequence of SEQ ID NO: 1 is bonded to a cysteine ​​residue contained in the peptide.

11. A peptide according to any one of claims 1 to 9, having a cyclic structure formed by bonding the amino group of the first amino acid residue and the carboxy group of the 14th amino acid residue in the amino acid sequence of SEQ ID NO:1 contained in the peptide.

12. A peptide described in any one of claims 1 to 11, wherein: (a) a linker and / or a payload can be attached to the C-terminus of the peptide; or (b) the 1st, 4th, 8th, 11th or 13th amino acid residue of the amino acid sequence of SEQ ID NO: 1 is an amino acid residue to which a linker and / or a payload can be attached.

13. A conjugate comprising a peptide according to any one of claims 1 to 12 and a payload, (i) any payload is linked to the 13th amino acid residue of SEQ ID NO:1, with or without a linker; or (ii) a payload is linked to the 1st, 4th, 8th or 11th amino acid residue of SEQ ID NO:1, as shown in the following formula (I): [In formula (I), R １ is H or a C alkyl group; R ２ is C alkyl-NH-, C alkyl-C aryl-O-C alkyl-NH-, C alkyl-NH(=O)-CH(C alkylphenyl)-NH-, C alkyl-NH(=O)-CH(C alkyl)-NH-, or C alkyl-NH(=O)-C cycloalkyl-C alkyl-NH-; and X is any payload.

14. R ２ The conjugate of claim 13, wherein is C1-6 alkyl-NH-.

15. The conjugate of claim 13 or 14, wherein X is a chelating agent.

16. The conjugate of claim 15, wherein the chelating agent is bound to a radioactive material.

17. The conjugate of claim 15 or 16, wherein the chelating agent is DOTA, DOTAGA, or NODAGA.

18. A pharmaceutical composition comprising a peptide according to any one of claims 1-12.

19. A pharmaceutical composition for preventing or treating a CA9-related disease, comprising a peptide according to any one of claims 1 to 12.

20. A pharmaceutical composition comprising a conjugate according to any one of claims 13-17.

21. A pharmaceutical composition for preventing or treating a CA9-related disease, comprising a conjugate according to any one of claims 13 to 17.

22. A diagnostic or research composition comprising a peptide according to any one of claims 1-12.

23. A diagnostic or research composition for diagnosing a CA9-related disease comprising a peptide according to any one of claims 1-12.

24. A diagnostic or research composition comprising a conjugate according to any one of claims 13-17.

25. A diagnostic or research composition for diagnosing a CA9-related disease comprising a conjugate according to any one of claims 13-17.

26. An imaging agent comprising a conjugate according to any one of claims 13-17.

27. An imaging agent for use in tumor diagnosis, comprising a conjugate according to any one of claims 13 to 17.

28. A radioligand imaging agent for use in positron emission tomography, comprising a conjugate according to any one of claims 13-17.

29. A method for testing a peptide, the method comprising testing at least one of: a) solubility in a solvent; b) CA9 binding activity; c) toxicity to cells and / or tissues; or d) toxicity to experimental animals, wherein the peptide is a peptide according to any one of claims 1-12.

30. A method for testing a conjugate, the method comprising testing at least one of: a) solubility in a solvent; b) CA9 binding activity; c) toxicity to cells and / or tissues; or d) toxicity to experimental animals, the conjugate being a conjugate according to any one of claims 13-17.

31. The following: the first amino acid residue is de(PEG8Me), dk, dyae, or dkCOpipzaa; the second amino acid residue is I or Tbg; the third amino acid residue is 3Py6NH2 or 3Py6CON; the fourth amino acid residue is K, KCOpipzaa, Hgn(Qglucamine-NH2), Hgn(KCOpipzaa-NH2), or Qglucamine; the fifth amino acid residue is PeG, MeG, Meda, or MedkCOpipzaa; The peptide of any one of claims 1 to 3, which satisfies one or more of the following requirements: the 7th amino acid residue is PeG, pMeOPeG, MsMeapG, 3OMePeG, pHPeG, PpG, pFPeG, mCPeG, pCPeG, 4HPpG, 4OMePpG, 4PypG, 4COOPeG, 3COOPeG, or 3FPeG; the 8th amino acid residue is K; the 9th amino acid residue is 3Py6NH2, 5Inda, Y, or F4OMe; the 10th amino acid residue is Ahp, HseMe, or E; and the 11th amino acid residue is dk(F) or dk(PEG8c).

32. A peptide according to any one of claims 1-6, comprising or consisting of an amino acid sequence set forth in any one of SEQ ID NOs:55-103.

33. A conjugate comprising the peptide of claim 32 and a payload, wherein the payload is attached to the 1st, 4th, 8th, 11th or 13th amino acid residue with or without a linker.

34. A conjugate according to any one of conjugate numbers 1-81 in Table 8 or Table 18.