CN113956327B - Polypeptide targeting human APC protein and application thereof in preparation of medicines - Google Patents
Polypeptide targeting human APC protein and application thereof in preparation of medicines Download PDFInfo
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/03—Fusion polypeptide containing a localisation/targetting motif containing a transmembrane segment
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to the field of biological medicine, in particular to polypeptide targeting human APC protein and application thereof in preparing medicines for treating colorectal cancer. The polypeptide fragment of human APC protein can target inhibition of nuclear emergence of truncated APC protein, so that the polypeptide can inhibit the tumorigenicity and proliferation capacity of colorectal cancer cells, and is thus used for preparing and developing medicaments for treating colorectal cancer and/or familial adenomatous polyposis.
Description
Technical Field
The invention relates to the field of biological medicine, in particular to polypeptide targeting human APC protein and application thereof in preparing medicines for treating colorectal cancer and familial adenomatous polyposis.
Background
Colorectal cancer (colorectal carcinoma, CRC) is a common malignancy in humans, and is one of the most common malignant tumors in China, with the death rate in the forefront. According to the latest data published by the national cancer center, the new colorectal cancer cases in China reach 38.76 thousands of people in 2015, and account for about 9.87% of the incidence of all malignant tumors; and the death cases caused by colorectal cancer reach 18.71 thousands of people, accounting for 8% of all malignant tumors, and serious social burden is caused.
Colorectal cancer is largely divided into sporadic and familial, with the vast majority of colorectal cancers being sporadic colorectal cancers. Familial adenomatous polyposis (Familial adenomatous polyposis, FAP) accounts for about 1% of all colorectal cancers. FAP incidence is probably 1 person per 30,000 people suffering from FAP. Typical FAP is mainly clinically manifested as: adenomatous polyps and microadenomas are present throughout the colon and rectum in numbers exceeding 100. About 90% of FAP patients have visible polyps before age 30 and as the volume and number of polyps increase, most patients develop symptoms such as bloody stool, altered bowel habits, abdominal pain, and wasting. If surgical intervention is not performed early, the probability of FAP developing colorectal cancer is 100% and the average age of cancer is 40 years.
Because of the hidden onset of colorectal cancer and the difficulty in early diagnosis, most colorectal cancer patients have lymphatic metastasis or distant organ metastasis at the time of initial diagnosis, which is one of the most leading causes of death. For advanced and recurrent colorectal cancer that is not resectable, fluorouracil+platinum based chemotherapy remains the primary palliative treatment and has low efficacy. In recent years, targeting drugs such as cetuximab, bevacizumab, trastuzumab, apatinib and immunotherapy have improved the survival prognosis of colorectal cancer patients to some extent, but only a small fraction of patients benefit. Thus, there is a need to explore new therapeutic strategies and targets to benefit more patients.
It is well known that the development of colorectal cancer is a complex process of multimolecular abnormalities and multistage progression. It is currently accepted that: mutations in the APC (adenomatous polyposis coli) gene, which lead to abnormal protein function or abnormal expression thereof, are key priming steps in the malignant progression of colorectal cancer "adenoma-adenocarcinoma". Wherein, the germline mutation of the APC gene can result in FAP; and somatic mutations are closely related to the occurrence and prognosis of more than 80% of sporadic colorectal adenomas and colorectal cancers. And the mouse animal model found in the early stage of APC gene research also confirms the driving role of APC gene mutation in FAP and colorectal cancer onset and progression.
The APC gene is located in the q21-22 segment of chromosome 5, the coded protein contains 2843 amino acids, the molecular weight of the protein reaches 311.8KD, and the protein contains a plurality of structural domains. The canonical role of APC proteins is a key negative regulator in the Wnt signaling pathway. It binds to the complex composed of Axin (Axin), GSK3 beta and the like and inhibits the stability of beta-catenin (beta-catenin). Mutations in 95% of APCs are nonsense mutations that lead to premature termination of their translation and expression of truncated APC proteins. This truncated protein lacks the binding site for β -catenin and axin and the GSK3 phosphorylation site, resulting in elevated intracellular β -catenin levels and promotion of tumor formation. In addition, the APC protein can directly regulate the movement and the adhesion capacity of cells by combining with actin, cell adhesion molecule related proteins alpha-catenin, beta-catenin and the like, thereby regulating the growth, the differentiation and the chromosome stability of the cells.
Several studies have found that APC gene mutations can lead to reduced cell adhesion and promote colorectal cancer cell metastasis; overexpression of truncated APC protein promotes migration of colorectal cancer cells, while inhibition of truncated APC protein or binding of it to interacting proteins such as Asef significantly reduces migration of colorectal cancer cells. This suggests that the truncated APC protein is not only a loss-of-function (loss-of-function) protein which causes a loss of binding ability with a protein such as β -catenin or actin, but also a protein which is likely to acquire a new function (gain-of-function) and exert an important oncogenic regulatory effect. Thus, targeting truncated APC proteins is likely to be a new strategy and important target for colorectal cancer treatment. However, no strong research on systematically blocking the functions of truncated APC protein molecules and low-toxicity drugs are reported at present.
In recent years, in the aspect of antitumor drugs, the targeting polypeptide has the characteristics of high affinity, strong specificity, less toxic and side effects, easiness in synthesis and the like, and is always a research hotspot in the field of tumor treatment. Polypeptides are small in size, simple in structure, but generally have biological functions similar to those of the native protein/antibody. Compared with antibody recognition, targeting polypeptide has strong penetrability, low immunogenicity, easy chemical synthesis and modification and high batch repeatability. No polypeptide research report capable of targeting truncated APC protein exists at present.
Thus, there is a need in the art for a drug targeting truncated APC proteins with little toxic side effects and high specificity for the treatment of colorectal cancer and familial adenomatous polyposis.
Disclosure of Invention
In view of the above, the present invention provides a polypeptide targeting truncated APC protein with little toxic side effect and strong specificity, thereby effectively inhibiting the tumorigenicity and proliferation ability of colorectal cancer cells.
The inventors have reviewed and searched reports summarizing truncated APC proteins, and found that truncated APC proteins are a nuclear plasma shuttle protein. Since normal localization is an important precondition for proteins to exert their biological functions, the inventors designed a plurality of polypeptides that can specifically disrupt the process of nuclear production or normal localization of truncated APC proteins, based on the amino acid sites that affect APC protein localization, thereby inhibiting the tumorigenicity and proliferation capacity of colorectal cancer cells.
Accordingly, in a first aspect, the present invention provides a polypeptide targeting a human APC protein, said polypeptide comprising the amino acid sequence of SEQ ID NO:1 (SEQ ID NO: 7) and the remaining amino acids in the presence of a complete match the amino acid sequence of the human APC protein, said polypeptide consisting of 7-25 amino acids, preferably 10-25 amino acids, more preferably 12-23 amino acids.
In a second aspect, the invention provides a fusion polypeptide comprising a polypeptide of the first aspect of the invention that targets a human APC protein, and a transmembrane peptide.
In a third aspect, the present invention provides a pharmaceutical composition comprising: (1) The polypeptide targeting the human APC protein according to the first aspect of the present invention, or the fusion polypeptide according to the second aspect of the present invention, and (2) a pharmaceutically acceptable carrier.
In a fourth aspect, the present invention provides the use of a polypeptide targeting human APC protein according to the first aspect of the present invention, or of a fusion polypeptide according to the second aspect of the present invention, in the manufacture of a medicament for the treatment of colorectal cancer, colorectal cancer metastasis and/or familial adenomatous polyposis in which there is a mutation in the APC gene.
The beneficial effects of the invention are as follows: the invention provides a polypeptide targeting human APC protein, which can disturb the process of nuclear or normal localization of truncated APC protein, thereby inhibiting the tumorigenicity and proliferation capacity of colorectal cancer cells. The polypeptide has small toxic side effect and strong specificity, so the polypeptide can be used for preparing medicaments for treating the morbidity and metastasis of rectal cancer and/or familial adenomatous polyposis.
Drawings
In order to more clearly illustrate the examples of the invention or the technical solutions of the prior art, the drawings used in the examples will be briefly described below, it being obvious that the drawings in the following description are only examples of the invention and that other embodiments can be obtained according to these drawings without inventive effort for a person skilled in the art.
Figure 1 shows that knockout of an endogenous mutated APC gene can significantly inhibit the tumorigenicity and proliferative capacity of colon cancer cells in nude mice. Wherein, FIG. 1A is a schematic diagram of the knockout of APC genes in tumor cell SW480 and DLD-1 cell lines by CRISPR/Cas9 method; FIG. 1B is a graph showing the results of APC protein expression by Western blotting of different clones; FIG. 1C shows the size of formed subcutaneous tumors and HE stained sections of SW480 cell lines in nude mice; FIG. 1D shows the size of formed subcutaneous tumors and HE stained sections of the DLD-1 cell line in nude mice. NC: a negative control; KO: knocking out; c1, C2, C3 and C4 represent different APC knock-out cell lines, respectively.
FIG. 2 shows the results of immunofluorescence experiments of a number of polypeptides (TruneP-NEIP 1, truneP-NEIP 2, truneP-NEIP 3, truneP-NEIP 4, truneP-NEIP 5, truneP-NEIP 6) designed by the inventors to target human APC proteins and TruneP-NEIP 1 mut in which leucine of TruneP-NEIP 1 was mutated to alanine. NC: negative control. The experimental results show that the truncated APC protein can not be uniformly distributed in the cytoplasm but aggregate in the perinucleuses due to the trunk APC-NEIP 1. Whereas mutation of leucine in trunk APC-NEIP1 to alanine (trunk APC-NEIP1 mut) significantly attenuated the nuclear-export blocking function of trunk APC-NEIP 1. Shortening the amino acids of Trunepc-NEIP 1 from both ends (sequences Trunepc-NEIP 3 to Trunepc-NEIP 5) resulted in a decrease in blocking effect over Trunepc-NEIP 1, whereas increasing the amino acid length at both ends of Trunepc-NEIP 1 (sequence Trunepc-NEIP 6, amino acids 58-80 of the APC protein) did not increase the blocking effect.
FIG. 3 shows the effect of tail vein injection of TrunedAPC-NEIP 1 polypeptide on proliferation capacity of colon cancer cells in nude mice and the effect of the polypeptide on important viscera of nude mice. Wherein, figure 3A shows the size of subcutaneous tumors in a nude mouse model of colorectal cancer cells; FIG. 3B is a plot of HE stained sections of subcutaneous tumors in a nude mouse model of colorectal cancer cells; NC: negative control. FIG. 3C is a graph of HE staining of cells of the vital organs (lung, liver, kidney and spleen) of the mice. Experimental results show that the tail vein injection TrunenAPC-NEIP 1 polypeptide has no obvious damage to important organs of mice.
Detailed Description
The present invention will now be described more fully hereinafter with reference to the accompanying drawings, in which embodiments of the invention are shown. It will be apparent that the described embodiments are only some, but not all, embodiments of the invention. All other embodiments that can be obtained by a person skilled in the art based on the embodiments of the present invention are within the scope of the present invention.
As described above, the present invention aims to provide a polypeptide targeting truncated APC protein with little toxic side effect and strong specificity, which can effectively inhibit the tumorigenicity and proliferation capacity of colorectal cancer cells, and thus can be used for preparing a medicament for treating the onset and metastasis of colorectal cancer and/or familial adenomatous polyposis.
As described in the background section, the term "familial adenomatous polyposis" refers to an autosomal dominant hereditary disease whose clinical condition is manifested mainly as adenomas of varying size throughout the colorectal (large intestine). Patients do not have colorectal polyps at birth, and polyps appear around age 15, with few at the beginning and increasing with age. Symptoms such as abdominal discomfort, abdominal pain, bloody stool or increased stool frequency can occur. The polyp of the large intestine of the FAP patient is adenomatous polyp, belongs to precancerous lesions, and is 100 percent of cancerous changes if the treatment is not carried out in time.
The pre-cancerous lesions of the colorectal develop into tumors through genetic alterations of the protooncogene or the oncogene, a process known as the "adenoma-adenocarcinoma" process. APC gene is a colorectal cancer suppressor gene, but mutation of APC gene leading to abnormal protein function or abnormal expression thereof is a key step in initiating malignant progression of colorectal cancer "adenoma-adenocarcinoma". Among them, germline mutations in the APC gene can lead to FAP, whereas somatic mutations drive the development and malignant progression of most sporadic colorectal adenomas and colorectal cancers.
The truncated APC protein generated by the mutation of the APC gene is reported to be a nuclear plasma shuttle protein, and the nuclear-taking blocking agent, namely the Leptomycin B (LMB), can obviously inhibit the nuclear taking of the truncated APC protein after being treated. Since normal localization is an important precondition for proteins to exert their biological functions, the inventors have devised blocking their biological functions by blocking the nucleation of truncated APC proteins. However, when the inventor treats cells with LMB, the inhibitor has larger cytotoxicity and weak specificity, and is not beneficial to carrying out in vivo experiments and clinical transformation of animals. Therefore, the inventors designed a plurality of polypeptides that can specifically disrupt the process of nucleation or normal localization of truncated APC proteins, based on the amino acid positions that affect APC protein localization.
Thus, in a first aspect, the invention provides a polypeptide targeting a human APC protein, said polypeptide comprising an amino acid sequence at positions 68-74 of the human APC protein (SEQ ID NO: 7) that exactly matches the amino acid sequence of the human APC protein, said polypeptide consisting of 7-25 amino acids.
In a preferred embodiment, the polypeptide consists of 10-25 amino acids. In a more preferred embodiment, the polypeptide consists of 12-23 amino acids.
In this specification "targeting polypeptide" refers to a peptide molecule having a specific affinity for a particular biological target. The polypeptide is formed by connecting several to dozens of amino acids with different structures, properties and functions through amide bonds according to a certain sequence.
The inventor selects a plurality of polypeptide fragments containing partial amino acid sequences of human APC protein for immunofluorescence experiment, wherein the polypeptide fragments comprise the following sequences:
the amino acid sequence (SEQ ID NO: 2) of the human APC protein (SEQ ID NO: 1) at positions 67-78 (Trunepc-NEIP 1);
the amino acid sequence (SEQ ID NO: 4) of the human APC protein (SEQ ID NO: 1) at positions 164-175 (Trunepc-NEIP 2);
the amino acid sequence (SEQ ID NO: 6) of the human APC protein (SEQ ID NO: 1) at positions 68-77 (Trunepc-NEIP 3);
the amino acid sequence (SEQ ID NO: 8) of the human APC protein (SEQ ID NO: 1) at positions 70-77 (Trunepc-NEIP 4);
the amino acid sequence (SEQ ID NO: 7) of the human APC protein (SEQ ID NO: 1) at positions 68-74 (Trunepc-NEIP 5); and
the amino acid sequence at positions 58-80 (TrunePC-NEIP 6) of the human APC protein (SEQ ID NO: 1) (SEQ ID NO: 9).
The inventors found that all of the Trunepc-NEIP 1, trunepc-NEIP 3, trunepc-NEIP 4, trunepc-NEIP 5, and Trunepc-NEIP 6 resulted in truncated APC proteins not being uniformly distributed in the cytoplasm and aggregated around the nucleus, with Trunepc-NEIP 1 and Trunepc-NEIP 6 being most effective. In addition, trunk apc-NEIP1 can significantly inhibit proliferation of human colorectal cancer cells and formation of mouse intestinal adenoma in both animal models. Through many experiments, the inventors found and considered that leucine at positions 68, 69, 72, 75 and 77 of the human APC protein was the most critical. And the rest of the amino acids in the polypeptide must be completely matched with the amino acid sequence of the human APC protein in the presence of the polypeptide, because the polypeptide is a blocking polypeptide, the purpose is to block the action of the fragment of the human APC protein with the binding molecule, which is sequence dependent, and if the sequences are not matched, the blocking effect will be affected.
The inventors found that the size of the polypeptide fragment is most preferably 12 amino acids (i.e., trunk apc-NEIP 1) because shortening the amino acid sequence of trunk apc-NEIP1 from both ends reduces the effect of its nuclear blocking function, while increasing the length of trunk apc-NEIP1 does not increase its effect but increases the production cost. In addition, if the polypeptide fragment is too long, the time and difficulty of production increase, and a new secondary mechanism may be generated to interfere with the action of the core peptide fragment.
Thus, in one embodiment, the polypeptide consists of SEQ ID NO:2, and a polypeptide having the amino acid sequence shown in (a) and (b).
In a second aspect, the invention provides a fusion polypeptide comprising a polypeptide of the first aspect of the invention that targets a human APC protein, and a transmembrane peptide.
In the present specification, "transmembrane peptide" means a polypeptide having a function of transporting across a cell membrane. The binding of therapeutic polypeptides to transmembrane peptides is an effective method of increasing the passage of therapeutic polypeptides across the cell membrane.
In a specific embodiment, the transmembrane peptide may be SEQ ID NO:3, and a transmembrane peptide shown in 3.
The polypeptide of the present invention, including fusion polypeptide, may be synthesized artificially or synthesized with its encoding gene before biological expression.
In a third aspect, the present invention provides a pharmaceutical composition comprising: (1) The polypeptide targeting the human APC protein according to the first aspect of the present invention, or the fusion polypeptide according to the second aspect of the present invention, and (2) a pharmaceutically acceptable carrier.
In a fourth aspect, the present invention provides the use of a polypeptide targeting human APC protein according to the first aspect of the present invention, or of a fusion polypeptide according to the second aspect of the present invention, in the manufacture of a medicament for the treatment of colorectal cancer, colorectal cancer metastasis and/or familial adenomatous polyposis in which there is a mutation in the APC gene.
In one embodiment, the medicament is an injectable formulation.
In summary, the present invention provides a polypeptide targeting human APC protein, which can disrupt the nucleation or normal localization process of truncated APC protein, thereby inhibiting the tumorigenicity and proliferation capacity of colorectal cancer cells. The polypeptide has small toxic side effect and strong specificity, so the polypeptide can be used for preparing medicaments for treating the morbidity and metastasis of rectal cancer and/or familial adenomatous polyposis.
Examples
The inventor firstly selects two common CRC cell lines SW480 and DLD-1 with APC gene mutation and truncated APC generation, knocks out the endogenous mutant APC genes of the colorectal cancer cell lines SW480 and DLD-1 by a CRISPR/Cas9 method, establishes stable cell lines, and then performs a nude mouse subcutaneous tumor experiment to determine the functions of the mutant APC genes and the truncated APC proteins generated by the mutant APC genes.
Example 1 mutant APC Gene and function of truncated APC protein produced thereby
1) And (3) cells: human colon carcinoma cell lines SW480 and DLD-1 used in this experiment were purchased from American type culture Collection (American type culture collection, ATCC) using RPMI1640 medium containing 10% fetal bovine serum, on a 5% CO basis 2 Culturing in a constant temperature incubator at 37 ℃. SW480 and DLD-1 cells both have endogenous APC gene mutation (mutation at amino acid 1338 and 1427, respectively) and produce truncated APC proteins.
2) CRISPR/Cas9 method knocks out APC genes: the single-guide RNAs (sgRNAs) were designed on-line using http:// crispr. Mit. Edu, the sgRNA-1 sequence was: CCGGCTTCCATAAGAACGGA, sgRNA-2 sequence is CGTTCTTATGGAAGCCGGGA. The sgRNA sequence was cloned into the lentiCRISPR v2 plasmid (52961, purchased from Addgene) by cleavage and ligation, thus constructing a knockout vector for knocking out APC genes in cells. FIG. 1A shows the sites of action of sgRNA-1 and sgRNA-2 on the APC gene. APC knock-out vector and control empty vector were then transfected into SW480 and DLD-1 cells with Lipofectamine 2000 (Invitrogen) and cells were treated with puromycin at a final concentration of 2 μg/ml for two weeks. Then, the cells were transferred to a 96-well plate for single cell culture, and after 3 weeks, the single cell cultured cells were extracted, and the expression of APC proteins was detected by western blotting.
FIG. 1B shows the detection results by Western blotting. As can be seen from the figure, the negative control group (NC) of either SW480 cells or DLD-1 cells normally expressed the APC protein, whereas in the four gene knockout cell clones, no significant decrease in the expression of the APC protein or the APC protein was seen. Clones from which the APC gene was successfully knocked out were selected for continued expansion culture for subsequent experiments.
3) Nude mice subcutaneous tumor experiment: nude mice were purchased from Beijing vitamin Tonglihua company for 3-4 weeks of week, with no limitation on male and female, 6 per group. Expanding the cells, namely transferring the idle SW480 and DLD-1 cells and stably knocking out the monoclonal strain of APC gene, taking the cells in logarithmic phase, digesting with 0.25% pancreatin, washing twice with PBS to removeSerum-containing medium was removed. The cells obtained were counted and the cell concentration was resuspended to 4X 10 with serum-free medium 6 Individual cells/0.1 ml, then injected subcutaneously into the back of the hind limb of nude mice. Observations were made 2-3 times per week. Three weeks later or if the tumor length and diameter were found to be close to 2cm during the experiment, the mice were euthanized, then taken out of the subcutaneous tumor for photographing, and then 10% formalin fixation, paraffin embedding and slicing were performed.
FIG. 1C is a photograph of a tumor formed by injection of tumor cell SW480 in nude mice, and a photograph of a corresponding HE stained section, and FIG. 1D is a photograph of a tumor formed by injection of tumor cell DLD-1 in nude mice, and a photograph of a corresponding HE stained section. As can be seen from these figures, in NC groups, i.e., in nude mice injected with cells in which the APC gene was not knocked out, tumors were formed in a relatively large volume; in the case of knockdown of the APC gene, however, the volume of tumor formed is greatly reduced, and even the tumor disappears (in the DLD-1 cell-treated group in which the APC gene is knocked out). In HE stained sections NC groups exhibited a large number of proliferating cells, whereas in the knocked out SW480 cell treated group, it can be seen that cell proliferation was greatly affected.
The experimental result shows that the mutant APC gene is knocked out, and the nodulation and proliferation capacity of colorectal cancer cells in nude mice can be obviously inhibited.
EXAMPLE 2 Synthesis of polypeptide targeting human APC protein
From the results of example 1, it was found that the truncated APC protein resulted in colorectal cancer. Therefore, in order to find a method of blocking the action of truncated APC proteins, the inventors thought to influence the biological functions of the proteins by inhibiting the nucleation of APC proteins, based on the property that truncated APC proteins are nuclear plasma shuttle proteins.
For this reason, the inventors designed a number of polypeptides that could specifically disrupt the process of nucleation or normal localization of truncated APC proteins, based on the amino acid positions that affect APC protein localization.
The sequence of the polypeptide targeting the human APC protein is as follows:
trunk APC-NEIP1: amino acids 67-78 of human APC protein, the sequence is DLLERLKELNLD;
trunk APC-NEIP2: amino acids 164-175 of human APC protein, the sequence is NLTKRIDSLPLT;
trunk APC-NEIP1 Mut: leucine in trunk apc-NEIP1 was all mutated to alanine, sequence DAAERAKEANAD.
Trunk APC-NEIP3: amino acids 68-77 of human APC protein, LLERLKELNL;
trunk APC-NEIP4: amino acids 70-77 of human APC protein, ERLKELNL;
trunk APC-NEIP5: amino acids 68-74 of human APC protein, the sequence is LLERLKE;
trunk APC-NEIP6: 58 th-80 th amino acid of human APC protein, sequence EAMASSGQIDLLERLKELNLDSS
To facilitate the interaction of these polypeptides with APC proteins into cells, a transmembrane peptide sequence CRGDKGPDC was also added to the C-terminus of the above polypeptides, and the transmembrane peptide sequence itself was used as a control polypeptide (NC: negative control).
The above polypeptides are all synthesized by the company limited by the biotechnology of Chinese gold and the solubility is measured, and the synthetic purity is more than 95%. When in first use: the polypeptide powder was dissolved to a maximum concentration with DMSO and then diluted to a desired concentration with physiological saline. The medicine is prevented from repeated freezing and thawing, and is stored in a refrigerator at-80deg.C.
EXAMPLE 3 Effect of the polypeptide of the invention on truncated APC protein positioning
In this example, the effect of the polypeptide on the localization of truncated APC proteins was observed by immunofluorescence.
Taking DLD-1 cells in good logarithmic phase, plating the DLD-1 cells in a confocal glass small dish after conventional pancreatin digestion, and calculating the number of required plated cells according to the area ratio of the cell culture dish to the confocal small dish, wherein the number of the required plated cells is less than 50% of the cell density of the small dish after packaging and plating, thereby being beneficial to observing the cell morphology. After the cells had attached to the wall and recovered to normal morphology, the polypeptide was added to the conventional medium at a final concentration of 5. Mu.g/0.2 ml. After 24 hours the medium was discarded, after elution with PBS, the mixture was fixed with 4% paraformaldehyde for 15 minutes at room temperature, after removal of the fixative, 0.5% Triton X-100 was added and the membrane was broken for 10 minutes at 4 ℃. The subsequent steps of sealing, incubating primary antibody, secondary antibody, DAPI nuclear staining and eluting according to the conventional immunofluorescence, and adding proper amount of 50% glycerol to prevent fluorescence quenching. APC antibodies were purchased from abcam (ab 16794) at a dilution ratio of 1:100. after completion, the sample was observed under a confocal laser microscope and photographed.
Fig. 2 shows the experimental results. From this figure, it can be found that: the location of truncated APC protein was almost not affected by trunk APC-NEIP2 (amino acids 164-175), the distribution of truncated APC protein was very similar to that in the control group (NC), both of which were widely distributed in the cytoplasm, while trunk APC-NEIP1 (amino acids 67-78) caused aggregation of truncated APC protein around the nucleus, which could not be widely distributed in the cytoplasm, indicating that the polypeptide could effectively prevent the ejection of truncated APC protein; whereas the leucine-to-alanine mutation of Trunep-NEIP 1 Mut lost the above-described nuclear-export prevention function. Shortening the amino acids of Trunepc-NEIP 1 from both ends (sequences Trunepc-NEIP 3 to Trunepc-NEIP 5) resulted in a decrease in blocking effect over Trunepc-NEIP 1, whereas increasing the amino acid length at both ends of Trunepc-NEIP 1 (Trunepc-NEIP 6 sequence, amino acids 58-80 of the APC protein) did not increase the blocking effect. Thus, the inventors believe that trunk APC-NEIP1 has a significant impact on truncated APC protein localization and leucine therein may play an important role.
EXAMPLE 4 cancer-inhibiting Effect of the polypeptide of the present invention
Further, the cancer inhibiting effect of the polypeptide of the present invention was examined by a DLD-1 cell nude mouse subcutaneous tumor experiment.
Nude mice purchased from beijing velutinin corporation were used, aged 3-4 weeks, with no limitation on male and female, 6 per group. DLD-1 cells resuspended in serum-free medium (concentration 4X 10) 6 Individual cells/0.1 ml), injected subcutaneously into the back of hind limbs of nude mice. After macroscopic growth of subcutaneous tumors, the C-terminal TrunaPC-NEIP1 with the transmembrane peptide added at the tail vein of 5mg/kg body weight or the transmembrane peptide as a negative control was injected twice weekly for three weeks at a concentration of 75 μg/200 μl. The major and minor diameters of the tumor were measured prior to each injection. If the tumor length and diameter are found to be more than 2cm in the experimental process, the mice are killed after dislocation. After the mice are sacrificed, subcutaneous tumors and important viscera are removed, includingHeart, liver, lung, kidney, taking a photograph of the general tissue, then timely fixing with 10% formalin, embedding with paraffin, and slicing. HE staining of subcutaneous tumors and vital organs was observed to see if there was damage to vital organs.
FIG. 3A is a photograph of a tumor after injection of Trunepc-NEIP 1 polypeptide into nude mice with subcutaneous tumors, and FIG. 3B is a photograph of a corresponding HE-stained section. In NC groups, i.e. in nude mice injected with only transmembrane peptide, tumors of relatively large volume were formed; in the case of injection of the Trunepc-NEIP 1 polypeptide, however, the tumor volume formed was significantly reduced. In HE stained sections NC groups exhibited a large number of proliferating cells, whereas in experimental groups injected with the TrunAPC-NEIP1 polypeptide, a large effect on cell proliferation was seen.
The experimental results show that the Trunepc-NEIP 1 can obviously inhibit the subcutaneous proliferation capacity of nude mice with colorectal cancer cells, and the biological toxicity of the polypeptide is low. Therefore, the polypeptide has good clinical transformation prospect in preparing medicines for treating occurrence and metastasis of colorectal cancer and familial adenomatous polyposis.
TABLE 1 sequence listing
Sequence listing
<110> center for tumor prevention and control at university of Zhongshan
Auxiliary tumor hospital for Zhongshan university
Tumor institute of Zhongshan university
<120> polypeptide targeting human APC protein and application thereof in preparing medicament
<160> 11
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<210> 1
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Leu Ser Glu Thr Phe Asp Asn Ile Asp Asn Leu Ser Pro Lys Ala Ser
770 775 780
His Arg Ser Lys Gln Arg His Lys Gln Ser Leu Tyr Gly Asp Tyr Val
785 790 795 800
Phe Asp Thr Asn Arg His Asp Asp Asn Arg Ser Asp Asn Phe Asn Thr
805 810 815
Gly Asn Met Thr Val Leu Ser Pro Tyr Leu Asn Thr Thr Val Leu Pro
820 825 830
Ser Ser Ser Ser Ser Arg Gly Ser Leu Asp Ser Ser Arg Ser Glu Lys
835 840 845
Asp Arg Ser Leu Glu Arg Glu Arg Gly Ile Gly Leu Gly Asn Tyr His
850 855 860
Pro Ala Thr Glu Asn Pro Gly Thr Ser Ser Lys Arg Gly Leu Gln Ile
865 870 875 880
Ser Thr Thr Ala Ala Gln Ile Ala Lys Val Met Glu Glu Val Ser Ala
885 890 895
Ile His Thr Ser Gln Glu Asp Arg Ser Ser Gly Ser Thr Thr Glu Leu
900 905 910
His Cys Val Thr Asp Glu Arg Asn Ala Leu Arg Arg Ser Ser Ala Ala
915 920 925
His Thr His Ser Asn Thr Tyr Asn Phe Thr Lys Ser Glu Asn Ser Asn
930 935 940
Arg Thr Cys Ser Met Pro Tyr Ala Lys Leu Glu Tyr Lys Arg Ser Ser
945 950 955 960
Asn Asp Ser Leu Asn Ser Val Ser Ser Ser Asp Gly Tyr Gly Lys Arg
965 970 975
Gly Gln Met Lys Pro Ser Ile Glu Ser Tyr Ser Glu Asp Asp Glu Ser
980 985 990
Lys Phe Cys Ser Tyr Gly Gln Tyr Pro Ala Asp Leu Ala His Lys Ile
995 1000 1005
His Ser Ala Asn His Met Asp Asp Asn Asp Gly Glu Leu Asp Thr Pro
1010 1015 1020
Ile Asn Tyr Ser Leu Lys Tyr Ser Asp Glu Gln Leu Asn Ser Gly Arg
1025 1030 1035 1040
Gln Ser Pro Ser Gln Asn Glu Arg Trp Ala Arg Pro Lys His Ile Ile
1045 1050 1055
Glu Asp Glu Ile Lys Gln Ser Glu Gln Arg Gln Ser Arg Asn Gln Ser
1060 1065 1070
Thr Thr Tyr Pro Val Tyr Thr Glu Ser Thr Asp Asp Lys His Leu Lys
1075 1080 1085
Phe Gln Pro His Phe Gly Gln Gln Glu Cys Val Ser Pro Tyr Arg Ser
1090 1095 1100
Arg Gly Ala Asn Gly Ser Glu Thr Asn Arg Val Gly Ser Asn His Gly
1105 1110 1115 1120
Ile Asn Gln Asn Val Ser Gln Ser Leu Cys Gln Glu Asp Asp Tyr Glu
1125 1130 1135
Asp Asp Lys Pro Thr Asn Tyr Ser Glu Arg Tyr Ser Glu Glu Glu Gln
1140 1145 1150
His Glu Glu Glu Glu Arg Pro Thr Asn Tyr Ser Ile Lys Tyr Asn Glu
1155 1160 1165
Glu Lys Arg His Val Asp Gln Pro Ile Asp Tyr Ser Leu Lys Tyr Ala
1170 1175 1180
Thr Asp Ile Pro Ser Ser Gln Lys Gln Ser Phe Ser Phe Ser Lys Ser
1185 1190 1195 1200
Ser Ser Gly Gln Ser Ser Lys Thr Glu His Met Ser Ser Ser Ser Glu
1205 1210 1215
Asn Thr Ser Thr Pro Ser Ser Asn Ala Lys Arg Gln Asn Gln Leu His
1220 1225 1230
Pro Ser Ser Ala Gln Ser Arg Ser Gly Gln Pro Gln Lys Ala Ala Thr
1235 1240 1245
Cys Lys Val Ser Ser Ile Asn Gln Glu Thr Ile Gln Thr Tyr Cys Val
1250 1255 1260
Glu Asp Thr Pro Ile Cys Phe Ser Arg Cys Ser Ser Leu Ser Ser Leu
1265 1270 1275 1280
Ser Ser Ala Glu Asp Glu Ile Gly Cys Asn Gln Thr Thr Gln Glu Ala
1285 1290 1295
Asp Ser Ala Asn Thr Leu Gln Ile Ala Glu Ile Lys Glu Lys Ile Gly
1300 1305 1310
Thr Arg Ser Ala Glu Asp Pro Val Ser Glu Val Pro Ala Val Ser Gln
1315 1320 1325
His Pro Arg Thr Lys Ser Ser Arg Leu Gln Gly Ser Ser Leu Ser Ser
1330 1335 1340
Glu Ser Ala Arg His Lys Ala Val Glu Phe Ser Ser Gly Ala Lys Ser
1345 1350 1355 1360
Pro Ser Lys Ser Gly Ala Gln Thr Pro Lys Ser Pro Pro Glu His Tyr
1365 1370 1375
Val Gln Glu Thr Pro Leu Met Phe Ser Arg Cys Thr Ser Val Ser Ser
1380 1385 1390
Leu Asp Ser Phe Glu Ser Arg Ser Ile Ala Ser Ser Val Gln Ser Glu
1395 1400 1405
Pro Cys Ser Gly Met Val Ser Gly Ile Ile Ser Pro Ser Asp Leu Pro
1410 1415 1420
Asp Ser Pro Gly Gln Thr Met Pro Pro Ser Arg Ser Lys Thr Pro Pro
1425 1430 1435 1440
Pro Pro Pro Gln Thr Ala Gln Thr Lys Arg Glu Val Pro Lys Asn Lys
1445 1450 1455
Ala Pro Thr Ala Glu Lys Arg Glu Ser Gly Pro Lys Gln Ala Ala Val
1460 1465 1470
Asn Ala Ala Val Gln Arg Val Gln Val Leu Pro Asp Ala Asp Thr Leu
1475 1480 1485
Leu His Phe Ala Thr Glu Ser Thr Pro Asp Gly Phe Ser Cys Ser Ser
1490 1495 1500
Ser Leu Ser Ala Leu Ser Leu Asp Glu Pro Phe Ile Gln Lys Asp Val
1505 1510 1515 1520
Glu Leu Arg Ile Met Pro Pro Val Gln Glu Asn Asp Asn Gly Asn Glu
1525 1530 1535
Thr Glu Ser Glu Gln Pro Lys Glu Ser Asn Glu Asn Gln Glu Lys Glu
1540 1545 1550
Ala Glu Lys Thr Ile Asp Ser Glu Lys Asp Leu Leu Asp Asp Ser Asp
1555 1560 1565
Asp Asp Asp Ile Glu Ile Leu Glu Glu Cys Ile Ile Ser Ala Met Pro
1570 1575 1580
Thr Lys Ser Ser Arg Lys Ala Lys Lys Pro Ala Gln Thr Ala Ser Lys
1585 1590 1595 1600
Leu Pro Pro Pro Val Ala Arg Lys Pro Ser Gln Leu Pro Val Tyr Lys
1605 1610 1615
Leu Leu Pro Ser Gln Asn Arg Leu Gln Pro Gln Lys His Val Ser Phe
1620 1625 1630
Thr Pro Gly Asp Asp Met Pro Arg Val Tyr Cys Val Glu Gly Thr Pro
1635 1640 1645
Ile Asn Phe Ser Thr Ala Thr Ser Leu Ser Asp Leu Thr Ile Glu Ser
1650 1655 1660
Pro Pro Asn Glu Leu Ala Ala Gly Glu Gly Val Arg Gly Gly Ala Gln
1665 1670 1675 1680
Ser Gly Glu Phe Glu Lys Arg Asp Thr Ile Pro Thr Glu Gly Arg Ser
1685 1690 1695
Thr Asp Glu Ala Gln Gly Gly Lys Thr Ser Ser Val Thr Ile Pro Glu
1700 1705 1710
Leu Asp Asp Asn Lys Ala Glu Glu Gly Asp Ile Leu Ala Glu Cys Ile
1715 1720 1725
Asn Ser Ala Met Pro Lys Gly Lys Ser His Lys Pro Phe Arg Val Lys
1730 1735 1740
Lys Ile Met Asp Gln Val Gln Gln Ala Ser Ala Ser Ser Ser Ala Pro
1745 1750 1755 1760
Asn Lys Asn Gln Leu Asp Gly Lys Lys Lys Lys Pro Thr Ser Pro Val
1765 1770 1775
Lys Pro Ile Pro Gln Asn Thr Glu Tyr Arg Thr Arg Val Arg Lys Asn
1780 1785 1790
Ala Asp Ser Lys Asn Asn Leu Asn Ala Glu Arg Val Phe Ser Asp Asn
1795 1800 1805
Lys Asp Ser Lys Lys Gln Asn Leu Lys Asn Asn Ser Lys Val Phe Asn
1810 1815 1820
Asp Lys Leu Pro Asn Asn Glu Asp Arg Val Arg Gly Ser Phe Ala Phe
1825 1830 1835 1840
Asp Ser Pro His His Tyr Thr Pro Ile Glu Gly Thr Pro Tyr Cys Phe
1845 1850 1855
Ser Arg Asn Asp Ser Leu Ser Ser Leu Asp Phe Asp Asp Asp Asp Val
1860 1865 1870
Asp Leu Ser Arg Glu Lys Ala Glu Leu Arg Lys Ala Lys Glu Asn Lys
1875 1880 1885
Glu Ser Glu Ala Lys Val Thr Ser His Thr Glu Leu Thr Ser Asn Gln
1890 1895 1900
Gln Ser Ala Asn Lys Thr Gln Ala Ile Ala Lys Gln Pro Ile Asn Arg
1905 1910 1915 1920
Gly Gln Pro Lys Pro Ile Leu Gln Lys Gln Ser Thr Phe Pro Gln Ser
1925 1930 1935
Ser Lys Asp Ile Pro Asp Arg Gly Ala Ala Thr Asp Glu Lys Leu Gln
1940 1945 1950
Asn Phe Ala Ile Glu Asn Thr Pro Val Cys Phe Ser His Asn Ser Ser
1955 1960 1965
Leu Ser Ser Leu Ser Asp Ile Asp Gln Glu Asn Asn Asn Lys Glu Asn
1970 1975 1980
Glu Pro Ile Lys Glu Thr Glu Pro Pro Asp Ser Gln Gly Glu Pro Ser
1985 1990 1995 2000
Lys Pro Gln Ala Ser Gly Tyr Ala Pro Lys Ser Phe His Val Glu Asp
2005 2010 2015
Thr Pro Val Cys Phe Ser Arg Asn Ser Ser Leu Ser Ser Leu Ser Ile
2020 2025 2030
Asp Ser Glu Asp Asp Leu Leu Gln Glu Cys Ile Ser Ser Ala Met Pro
2035 2040 2045
Lys Lys Lys Lys Pro Ser Arg Leu Lys Gly Asp Asn Glu Lys His Ser
2050 2055 2060
Pro Arg Asn Met Gly Gly Ile Leu Gly Glu Asp Leu Thr Leu Asp Leu
2065 2070 2075 2080
Lys Asp Ile Gln Arg Pro Asp Ser Glu His Gly Leu Ser Pro Asp Ser
2085 2090 2095
Glu Asn Phe Asp Trp Lys Ala Ile Gln Glu Gly Ala Asn Ser Ile Val
2100 2105 2110
Ser Ser Leu His Gln Ala Ala Ala Ala Ala Cys Leu Ser Arg Gln Ala
2115 2120 2125
Ser Ser Asp Ser Asp Ser Ile Leu Ser Leu Lys Ser Gly Ile Ser Leu
2130 2135 2140
Gly Ser Pro Phe His Leu Thr Pro Asp Gln Glu Glu Lys Pro Phe Thr
2145 2150 2155 2160
Ser Asn Lys Gly Pro Arg Ile Leu Lys Pro Gly Glu Lys Ser Thr Leu
2165 2170 2175
Glu Thr Lys Lys Ile Glu Ser Glu Ser Lys Gly Ile Lys Gly Gly Lys
2180 2185 2190
Lys Val Tyr Lys Ser Leu Ile Thr Gly Lys Val Arg Ser Asn Ser Glu
2195 2200 2205
Ile Ser Gly Gln Met Lys Gln Pro Leu Gln Ala Asn Met Pro Ser Ile
2210 2215 2220
Ser Arg Gly Arg Thr Met Ile His Ile Pro Gly Val Arg Asn Ser Ser
2225 2230 2235 2240
Ser Ser Thr Ser Pro Val Ser Lys Lys Gly Pro Pro Leu Lys Thr Pro
2245 2250 2255
Ala Ser Lys Ser Pro Ser Glu Gly Gln Thr Ala Thr Thr Ser Pro Arg
2260 2265 2270
Gly Ala Lys Pro Ser Val Lys Ser Glu Leu Ser Pro Val Ala Arg Gln
2275 2280 2285
Thr Ser Gln Ile Gly Gly Ser Ser Lys Ala Pro Ser Arg Ser Gly Ser
2290 2295 2300
Arg Asp Ser Thr Pro Ser Arg Pro Ala Gln Gln Pro Leu Ser Arg Pro
2305 2310 2315 2320
Ile Gln Ser Pro Gly Arg Asn Ser Ile Ser Pro Gly Arg Asn Gly Ile
2325 2330 2335
Ser Pro Pro Asn Lys Leu Ser Gln Leu Pro Arg Thr Ser Ser Pro Ser
2340 2345 2350
Thr Ala Ser Thr Lys Ser Ser Gly Ser Gly Lys Met Ser Tyr Thr Ser
2355 2360 2365
Pro Gly Arg Gln Met Ser Gln Gln Asn Leu Thr Lys Gln Thr Gly Leu
2370 2375 2380
Ser Lys Asn Ala Ser Ser Ile Pro Arg Ser Glu Ser Ala Ser Lys Gly
2385 2390 2395 2400
Leu Asn Gln Met Asn Asn Gly Asn Gly Ala Asn Lys Lys Val Glu Leu
2405 2410 2415
Ser Arg Met Ser Ser Thr Lys Ser Ser Gly Ser Glu Ser Asp Arg Ser
2420 2425 2430
Glu Arg Pro Val Leu Val Arg Gln Ser Thr Phe Ile Lys Glu Ala Pro
2435 2440 2445
Ser Pro Thr Leu Arg Arg Lys Leu Glu Glu Ser Ala Ser Phe Glu Ser
2450 2455 2460
Leu Ser Pro Ser Ser Arg Pro Ala Ser Pro Thr Arg Ser Gln Ala Gln
2465 2470 2475 2480
Thr Pro Val Leu Ser Pro Ser Leu Pro Asp Met Ser Leu Ser Thr His
2485 2490 2495
Ser Ser Val Gln Ala Gly Gly Trp Arg Lys Leu Pro Pro Asn Leu Ser
2500 2505 2510
Pro Thr Ile Glu Tyr Asn Asp Gly Arg Pro Ala Lys Arg His Asp Ile
2515 2520 2525
Ala Arg Ser His Ser Glu Ser Pro Ser Arg Leu Pro Ile Asn Arg Ser
2530 2535 2540
Gly Thr Trp Lys Arg Glu His Ser Lys His Ser Ser Ser Leu Pro Arg
2545 2550 2555 2560
Val Ser Thr Trp Arg Arg Thr Gly Ser Ser Ser Ser Ile Leu Ser Ala
2565 2570 2575
Ser Ser Glu Ser Ser Glu Lys Ala Lys Ser Glu Asp Glu Lys His Val
2580 2585 2590
Asn Ser Ile Ser Gly Thr Lys Gln Ser Lys Glu Asn Gln Val Ser Ala
2595 2600 2605
Lys Gly Thr Trp Arg Lys Ile Lys Glu Asn Glu Phe Ser Pro Thr Asn
2610 2615 2620
Ser Thr Ser Gln Thr Val Ser Ser Gly Ala Thr Asn Gly Ala Glu Ser
2625 2630 2635 2640
Lys Thr Leu Ile Tyr Gln Met Ala Pro Ala Val Ser Lys Thr Glu Asp
2645 2650 2655
Val Trp Val Arg Ile Glu Asp Cys Pro Ile Asn Asn Pro Arg Ser Gly
2660 2665 2670
Arg Ser Pro Thr Gly Asn Thr Pro Pro Val Ile Asp Ser Val Ser Glu
2675 2680 2685
Lys Ala Asn Pro Asn Ile Lys Asp Ser Lys Asp Asn Gln Ala Lys Gln
2690 2695 2700
Asn Val Gly Asn Gly Ser Val Pro Met Arg Thr Val Gly Leu Glu Asn
2705 2710 2715 2720
Arg Leu Asn Ser Phe Ile Gln Val Asp Ala Pro Asp Gln Lys Gly Thr
2725 2730 2735
Glu Ile Lys Pro Gly Gln Asn Asn Pro Val Pro Val Ser Glu Thr Asn
2740 2745 2750
Glu Ser Ser Ile Val Glu Arg Thr Pro Phe Ser Ser Ser Ser Ser Ser
2755 2760 2765
Lys His Ser Ser Pro Ser Gly Thr Val Ala Ala Arg Val Thr Pro Phe
2770 2775 2780
Asn Tyr Asn Pro Ser Pro Arg Lys Ser Ser Ala Asp Ser Thr Ser Ala
2785 2790 2795 2800
Arg Pro Ser Gln Ile Pro Thr Pro Val Asn Asn Asn Thr Lys Lys Arg
2805 2810 2815
Asp Ser Lys Thr Asp Ser Thr Glu Ser Ser Gly Thr Gln Ser Pro Lys
2820 2825 2830
Arg His Ser Gly Ser Tyr Leu Val Thr Ser Val
2835 2840
<210> 2
<211> 12
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 2
Asp Leu Leu Glu Arg Leu Lys Glu Leu Asn Leu Asp
1 5 10
<210> 3
<211> 9
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 3
Cys Arg Gly Asp Lys Gly Pro Asp Cys
1 5
<210> 4
<211> 12
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 4
Asn Leu Thr Lys Arg Ile Asp Ser Leu Pro Leu Thr
1 5 10
<210> 5
<211> 12
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 5
Asp Ala Ala Glu Arg Ala Lys Glu Ala Asn Ala Asp
1 5 10
<210> 6
<211> 10
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 6
Leu Leu Glu Arg Leu Lys Glu Leu Asn Leu
1 5 10
<210> 7
<211> 7
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 7
Leu Leu Glu Arg Leu Lys Glu
1 5
<210> 8
<211> 8
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 8
Glu Arg Leu Lys Glu Leu Asn Leu
1 5
<210> 9
<211> 23
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 9
Glu Ala Met Ala Ser Ser Gly Gln Ile Asp Leu Leu Glu Arg Leu Lys
1 5 10 15
Glu Leu Asn Leu Asp Ser Ser
20
<210> 11
<211> 20
<212> DNA/RNA
<213> Artificial sequence (Artificial Sequence)
<400> 11
ccggcttcca taagaacgga 20
<210> 11
<211> 20
<212> DNA/RNA
<213> Artificial sequence (Artificial Sequence)
<400> 11
cgttcttatg gaagccggga 20
Claims (6)
1. Use of a polypeptide or fusion polypeptide targeting human APC protein consisting of the amino acid sequence of SEQ ID NO:2, and the fusion polypeptide is formed by the polypeptide targeting the human APC protein and a transmembrane peptide, wherein the APC gene mutation exists in the colorectal cancer.
2. The use according to claim 1, wherein the colorectal cancer is colorectal cancer metastasis.
3. The use according to claim 1, wherein the colorectal cancer is familial adenomatous polyposis.
4. The use of claim 1, wherein the transmembrane peptide is SEQ ID NO:3, and a transmembrane peptide shown in 3.
5. The use of any one of claims 1-4, wherein the medicament further comprises a pharmaceutically acceptable carrier.
6. The use according to any one of claims 1-4, wherein the medicament is an injectable formulation.
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Citations (3)
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WO1998005347A1 (en) * | 1996-07-22 | 1998-02-12 | The Trustees Of Columbia University In The City Of New York | Compounds that inhibit interaction between signal-transducing proteins and the glgf (pdz/dhr) domain and uses thereof |
EP1929043A2 (en) * | 2005-08-24 | 2008-06-11 | Genizon Biosciences, Inc. | Genemap of the human genes associated with crohn's disease |
CN110596385A (en) * | 2012-11-30 | 2019-12-20 | 迪森德克斯公司 | Methods for assessing the presence or risk of a colon tumor |
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WO1998005347A1 (en) * | 1996-07-22 | 1998-02-12 | The Trustees Of Columbia University In The City Of New York | Compounds that inhibit interaction between signal-transducing proteins and the glgf (pdz/dhr) domain and uses thereof |
CN1230120A (en) * | 1996-07-22 | 1999-09-29 | 纽约市哥伦比亚大学信托人 | Compounds that inhibit interaction between signal-transducing proteins and GLGF(PDZ/DHR) domain and uses thereof |
EP1929043A2 (en) * | 2005-08-24 | 2008-06-11 | Genizon Biosciences, Inc. | Genemap of the human genes associated with crohn's disease |
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