New polypeptides and their use in the preparation of medicaments for the treatment of skin wounds or mucosal lesions

CN114773428BActive Publication Date: 2026-08-11SICHUAN GOODDOCTOR PANXI PHARMA
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2021-12-29
Publication Date
2026-08-11

AI Technical Summary

Technical Problem

慢性胃炎好发于中老年人群,发病和年龄有一定的关联但与性别没有关系,发病缓慢且病势缠绵,迁延难愈,治疗棘手

Benefits of technology

[0021] The polypeptides in this invention have small molecular weights, are easy to synthesize artificially, and have high purity, making them suitable for large-scale production. In terms of application, these polypeptides exert biological effects by binding to the epidermal growth factor receptor EGFR, and have significant therapeutic effects on skin and mucous membrane injuries caused by various reasons. The polypeptides can be used to treat various skin diseases, acute and chronic gastrointestinal diseases, tumors, and other related diseases.

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Abstract

This invention belongs to the fields of pharmaceuticals and daily chemical products, specifically relating to a group of novel polypeptides and their application in the preparation of drugs for treating / or preventing skin wounds or mucosal injuries. The novel polypeptides described in this invention can bind to the epidermal growth factor receptor (EGFR) to exert biological effects and can be used to prepare drugs or daily chemical products for treating / or preventing skin or mucosal diseases, acute and chronic gastrointestinal diseases, tumors, and related diseases.
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Description

Technical Field

[0001] This invention belongs to the fields of pharmaceuticals and daily chemicals, specifically relating to a group of novel polypeptides and their application in the preparation of drugs for treating and / or preventing skin wounds or mucosal damage. Background Technology

[0002] Epidermal growth factor receptor (EGFR) is a multifunctional glycoprotein widely distributed on the cell membranes of various human tissues. It is a homolog of the oncogene of avian erythroblastic leukemia viral (v-erb-b) and one of the four members of the HER / ErbB family, hence also known as HER1 or ErbB-1. EGFR and its ligands are part of the cell signaling system. Studies have shown that increased EGFR gene copy number or overexpression can promote the transformation of normal cells and the metastasis of malignant tumors. The EGFR signaling network plays an important role in tumor formation and development. Since the EGFR gene was first cloned in 1984, research has shown that EGFR is a promising target molecule for cancer treatment.

[0003] Skin and / or mucous membrane injury is a common pathological feature of many diseases. Skin injury refers to damage to normal skin (tissue) caused by external traumatic factors such as surgery, external force, heat, electric current, chemicals, and low temperature, as well as internal factors such as local blood supply disorders. It is often accompanied by the disruption of skin integrity and the loss of a certain amount of normal tissue, while also impairing normal skin function. It is also called a wound or trauma. Currently, protein / peptide drugs, including basic fibroblast growth factor, epidermal growth factor, platelet-derived growth factor, granulocyte-macrophage colony-stimulating factor, and growth hormone, have significant effects on wound repair, skin care, anti-wrinkle, and anti-aging. However, the long amino acid sequences of these protein / peptide drugs lead to high preparation costs and poor stability, thus limiting their application.

[0004] Chronic gastritis is a chronic inflammation of the gastric mucosa, a common and frequently occurring disease in gastroenterology. Clinically, chronic gastritis refers to chronic inflammation of the gastric mucosa (pathologically manifested as mononuclear cell and lymphocyte infiltration) and / or glandular atrophic lesions caused by various factors. Chronic gastritis is more common in middle-aged and elderly people. Its onset is related to age but not to gender. It has a slow onset and a protracted course, making it difficult to cure and challenging to treat.

[0005] Currently, there are still many challenges in the treatment of skin and mucous membrane diseases and tumors that require scientific and technological personnel to research and solve, and to discover better and more promising drugs. Summary of the Invention

[0006] Existing treatment methods cannot meet the needs of clinical treatment. In order to better treat skin and mucous membrane diseases and tumors, such as acute and chronic gastrointestinal diseases and skin or mucous membrane injury diseases, the inventors conducted extensive experimental research in the field of peptides, and found that multiple peptides bind to the epidermal growth factor receptor EGFR to exert biological effects, which can reduce the pathological development of acute and chronic gastrointestinal diseases, promote skin damage repair, and have anti-tumor and anti-fibrotic effects.

[0007] The purpose of this invention is to provide a new group of polypeptides.

[0008] Furthermore, the novel polypeptide has any one of the amino acid sequences shown in SEQ ID NO:1 to SEQ ID NO:10 in Table 1:

[0009] Table 1. Amino acid sequences of the new peptides

[0010] PA1 VPPHLF SEQ ID NO.1 PA2 LRGFEPP SEQ ID NO.2 PA3 KWAP SEQ ID NO.3 PA4 TASTL SEQ ID NO.4 PA5 LAAVD SEQ ID NO.5 PA6 LAGLD SEQ ID NO.6 PA7 LAGNK SEQ ID NO.7 PA8 KCLKKQQGP SEQ ID NO.8 PA9 TATKPMPTVET SEQ ID NO.9 PA10 KASTKFKVE SEQ ID NO.10

[0011] Furthermore, the novel polypeptide described in this invention has the ability to bind to the EGFR receptor.

[0012] Furthermore, the method for preparing the novel polypeptide described in this invention can be carried out using methods known in the prior art. It can be chemically synthesized using a polypeptide automated synthesizer according to conventional solid-phase synthesis methods, or it can be biosynthesized by deducing the nucleotide sequence from the amino acid sequence of the short peptide and then using genetic engineering techniques.

[0013] Furthermore, the polypeptides provided by this invention can be used as components of pharmaceuticals or daily chemical products.

[0014] Furthermore, the present invention also provides compositions of the novel polypeptides, comprising a peptide containing at least one amino acid sequence shown in SEQ ID NO.1 to SEQ ID NO.10, or a pharmaceutically acceptable salt and a pharmaceutically acceptable carrier or excipient. The compositions can be present in pharmaceutical formulations and can be prepared according to conventional pharmaceutical techniques, including mixing the pharmaceutically active ingredient, the polypeptide of the present invention, with a pharmaceutical carrier, and preparing the desired dosage form according to conventional pharmaceutical techniques.

[0015] Furthermore, the present invention provides the use of the novel polypeptide in the preparation of products for the treatment and / or prevention of diseases related to the EGFR target.

[0016] Furthermore, the present invention provides the use of the novel polypeptide in the preparation of medicaments for treating and / or preventing skin wound diseases, mucosal wound diseases, and tumor-related diseases.

[0017] Furthermore, the skin wound diseases mentioned include photoaging, psoriasis, eczema, neurodermatitis, xerosis, mechanical and surgical wounds, burns, scalds, ulcers, fistulas, bedsores, and skin damage caused by radiotherapy and chemotherapy.

[0018] The mucosal lesion diseases mentioned include acute gastritis, chronic gastritis, chronic atrophic gastritis, gastroduodenal ulcers, functional gastrointestinal disorders, indigestion, precancerous lesions, digestive system tumors, gastrointestinal bleeding, gastroesophageal reflux disease, oral ulcers, stomatitis, gingivitis, periodontitis, esophagitis, esophageal ulcers, acute and chronic enteritis, ulcerative colitis, Crohn's disease, and mucosal damage caused by radiotherapy and chemotherapy.

[0019] Furthermore, the drug is a formulation prepared by adding pharmaceutically acceptable excipients or auxiliary ingredients to a peptide with at least one amino acid sequence shown in SEQ ID NO.1 to SEQ ID NO.10 as the active ingredient.

[0020] Furthermore, the preparation is an oral preparation or a topical preparation.

[0021] The polypeptides in this invention have small molecular weights, are easy to synthesize artificially, and have high purity, making them suitable for large-scale production. In terms of application, these polypeptides exert biological effects by binding to the epidermal growth factor receptor EGFR, and have significant therapeutic effects on skin and mucous membrane injuries caused by various reasons. The polypeptides can be used to treat various skin diseases, acute and chronic gastrointestinal diseases, tumors, and other related diseases.

[0022] Experimental results demonstrate that the novel polypeptides described in this invention exhibit significant anti-ulcer activity against an ethanol-induced mouse gastric ulcer model; significant wound healing effects on rat skin after mechanical injury; and cell proliferation. This confirms that the novel polypeptides described in this invention can effectively promote the repair of digestive system mucosal damage, alleviate the progression of gastrointestinal diseases such as acute and chronic gastritis and peptic ulcers; and can treat various skin diseases, providing a new approach and strategy for skin diseases, acute and chronic gastrointestinal diseases, tumors, and related diseases. Attached Figure Description

[0023] Figure 1 This is the mass spectrum of the new polypeptide PA1.

[0024] Figure 2 This is the mass spectrum of the new polypeptide PA2.

[0025] Figure 3 This is the mass spectrum of the new polypeptide PA3.

[0026] Figure 4 This is the mass spectrum of the new polypeptide PA4.

[0027] Figure 5 This is the mass spectrum of the new polypeptide PA5.

[0028] Figure 6 This is the mass spectrum of the new polypeptide PA6.

[0029] Figure 7 This is the mass spectrum of the new polypeptide PA7.

[0030] Figure 8 This is the mass spectrum of the new polypeptide PA8.

[0031] Figure 9 This is the mass spectrum of the new polypeptide PA9.

[0032] Figure 10 This is the mass spectrum of the new polypeptide PA10.

[0033] Figure 11 This is a diagram illustrating the effect of the novel peptide PA2 on the proliferation of HaCaT cells.

[0034] Figure 12 This is a diagram illustrating the effect of the novel peptide PA2 on the proliferation of HMEC-1 cells.

[0035] Figure 13 This is a diagram illustrating the effect of the novel peptide PA3 on the proliferation of HMEC-1 cells.

[0036] Figure 14 This is a diagram illustrating the effect of the novel peptide PA4 on the proliferation of HMEC-1 cells.

[0037] Figure 15 This is a graph showing the effect of the new peptide PA5 on the proliferation of HMEC-1 cells.

[0038] Figure 16 This is a graph showing the effect of the new polypeptide PA10 on the proliferation of RSC96 cells. Detailed Implementation

[0039] Example 1: Screening of novel polypeptide molecules

[0040] (1) The new polypeptide comes from Sichuan Good Doctor Panxi Pharmaceutical Co., Ltd.

[0041] (2) EGFR protein target affinity screening

[0042] EGFR affinity screening: The freeze-dried peptides of this invention were dissolved in protein buffer to prepare peptide compound sample solutions. An appropriate concentration of EGFR solution was incubated with the peptide compound sample solutions at room temperature for 50 min, followed by affinity screening. The centrifugation speed was 90,000 rpm for 70 min. After centrifugation, the samples were separated into upper, middle and lower layers by volume. An appropriate volume of acetonitrile and water was added to each layer to precipitate the protein. The supernatant was then centrifuged and analyzed by mass spectrometry.

[0043] EGF peptides were used as positive control compounds.

[0044] Affinity screening conditions: One-dimensional liquid chromatography (LC) conditions: PolyLC column, mobile phase A: KH₂PO₄, NaCl, pH 7.5, mobile phase B: acetonitrile, column temperature 8℃, flow rate 1 mL / min, appropriate injection volume; Two-dimensional liquid chromatography (LC) conditions: BONUS RRHD column, mobile phase A: 0.1% formic acid aqueous solution, mobile phase B: 0.1% formic acid acetonitrile, column temperature 60℃, flow rate 0.3 mL / min, injection volume 40 μL. Gradient elution was used: 98% A (0-1 min), 98%-10% A (1-6 min), 10% A (6-7.5 min), 10%-98% A (7.5-8 min), 98% A (8-9.5 min). Mass spectrometry conditions: Agilent 6530Q-Tof, ESI ion source, voltage 3.5KV, mass-to-charge ratio scan range m / z = 200-3000, acquisition mode positive ion scan, ion source temperature 350℃, desolventization temperature 300℃, nitrogen flow rate 8L / min.

[0045] Affinity screening yielded a series of peptides with affinity for EGFR, expressed as the Cb / Ct ratio. The Cb / Ct ratio refers to the ratio of the amount (mass spectrometry signal intensity) of the lower-layer compound to the amount (mass spectrometry signal intensity) of the upper-layer compound during ultracentrifugation affinity screening. A higher Cb / Ct ratio indicates stronger affinity. The results are shown in Table 2.

[0046] Table 2. Screening results of new peptides with affinity for EGFR

[0047] Positive - - 4~5 PA1 VPPHLF SEQ ID NO.1 708.80 1.5~3 PA2 LRGFEPP SEQ ID NO.2 815.20 1.5~3 PA3 KWAP SEQ ID NO.3 500.3 1.5~3 PA4 TASTL SEQ ID NO.4 491.2 1.5~3 PA5 LAAVD SEQ ID NO.5 487.2 1.5~3 PA6 LAGLD SEQ ID NO.6 487.1 1.5~3 PA7 LAGNK SEQ ID NO.7 501.8 1.5~3 PA8 KCLKKQQGP SEQ ID NO.8 1029.3 1.5~3 PA9 TATKPMPTVET SEQ ID NO.9 1175.2 1.5~4 PA10 KASTKFKVE SEQ ID NO.10 1037.21 1.5~3

[0048] Example 2: Chemical Synthesis Method of Novel Peptides

[0049] Using a fully automated peptide synthesizer and conventional solid-phase synthesis method, new peptides were chemically synthesized through processes including resin swelling, deprotection, washing, amino acid dissolution, amino acid activation, and condensation. Ten peptides were obtained, and their structures were confirmed by mass spectrometry analysis. Figures 1-10 This is the mass spectrum of the new polypeptide.

[0050] Example 3: Effect of novel peptide PA2 on Hacat cell proliferation

[0051] The concentration of immortalized human keratinocytes (HaCaT cells) was adjusted to 1.0 × 10⁻⁶. 5 ~5.0×10 5Cells were passaged at 37°C and 5% CO2 for 24–36 hours for biological activity assay. Cells were digested with 0.25% trypsin for 5 min, and digestion was terminated by adding at least one volume of 1640 whole blood medium. The cell suspension was collected, centrifuged at 1000 RPM for 3 min, the supernatant was discarded, and the cells were resuspended in 2 mL of 1640 whole blood medium. 20 μL of the cell suspension was stained with AOPI, and the cell concentration was determined using a cell counter. A 5 × 10⁻⁶ cell concentration was prepared using 10% serum-concentrated 1640 medium. 4 HaCaT cells were seeded at 100 μL per well in 96-well cell culture plates (5000 cells / well) and cultured overnight at 37°C with 5% CO2. After 24 h, the original culture medium was discarded, and 100 μL of different concentrations of polypeptide compound solutions (PA2) prepared with 1% serum-concentrated 1640 medium were added to achieve final concentrations of 0.05, 0.2, and 0.8 μg / mL, respectively. An EGF control group was set up, containing 100 μL of recombinant human epidermal growth factor (EGF) solution prepared with 1% serum-concentrated 1640 medium, with a final concentration of 100 ng / mL. A model control group was set up, containing an equal volume of 1% serum-concentrated 1640 medium. Cells were cultured at 37°C with 5% CO2 for 72 h, and the proliferation of the HaCaT cell line was detected using a CCK8 assay kit. Results are shown below. Figure 11 .

[0052] Example 4: Effect of the novel peptide on HMEC-1 cell proliferation

[0053] Human microvascular endothelial cells (HMEC-1 cells) were cultured in 10% serum at 37°C and 5% CO2, with the medium changed every 1–2 days to maintain a cell concentration of 4 × 10⁻⁶ cells / day. 6 Cells were passaged at a density of 10 cells / mL. Cells were collected and reconstituted into 5 × 10⁶ cells / mL culture medium. 4 Cells / mL; 100 μL (5000 cells / well) were seeded into 96-well cell culture plates and cultured at 37°C and 5% CO2 until cell adhesion. Peptide drugs (PA2, PA3, PA4, and PA5) were prepared into test concentrations (0.05 μg / mL, 0.2 μg / mL, 0.8 μg / mL) using 0% serum medium as the experimental groups. Positive control (300 ng / mL) was prepared using the same method and added as the positive control. An equal volume of 0% serum-free drug-free medium was added to the control group. Cells were added in 5 replicates and incubated at 37°C and 5% CO2 for 48 hours. Cell proliferation was detected using CCK-8 assay: after removing the old medium, serum-free medium containing 10% CCK-8 was added to each well. After incubation for 2 hours, absorbance was measured at 450 nm using a microplate reader. Results are shown below. Figures 12-15 .

[0054] Effect of the new polypeptide PA10 on the proliferation of RSC96 cells in Example 5

[0055] Adjust the concentration of glial cells (RSC96 cells) to 1.0×10 5 ~5.0×10 5 / mL for subculture, and culture for 24 - 36 hours at 37°C under 5% CO2 conditions for biological activity detection. Digest and collect the cells with trypsin, and prepare a concentration of 5×10 4 / mL with serum-free medium and inoculate into a 96-well cell culture plate, 100 μL per well, that is, 5000 cells / well, and culture overnight at 37°C under 5% CO2 conditions.

[0056] Prepare the polypeptide drug (PA10) with 0% serum medium into the test concentrations (0.2 μg / ml, 0.4 μg / ml, 0.8 μg / ml) as the experimental group, add an equal amount of 0% serum drug-free medium to the control group, add in 4 replicates, and incubate at 37°C under 5% CO2 conditions for 48 hours.

[0057] Use CCK-8 to detect the cell proliferation: Remove the old medium, add serum-free medium containing 10% CCK-8 to each well, incubate in the incubator for 2 h, and then measure the absorbance at 450 nm with an enzyme-labeled instrument. The results are shown in Figure 16 .

[0058] Anti-ulcer effect of the new polypeptide on the ethanol-induced mouse gastric ulcer model in Example 6

[0059] Experimental animals: SPF-grade C57BL / 6 mice, Chengdu Yakang Biotechnology Co., Ltd., animal license number: SCXK (Chuan) 2020 - 034

[0060] Experimental drugs: The positive drug group is teprenone, and the samples are the new polypeptides PA1 - PA10.

[0061] Experimental Methods: After acclimatization, all animals were fasted for 24 hours with free access to water one day before the experiment. Before modeling, mice were randomly divided into three groups: a control group (n=5), a model group (n=10), and each of the drug-treated groups (n=10). Except for the control and model groups, which were administered purified water by gavage, the drug-treated groups were administered different test samples by gavage at a dose of 0.2 mg / kg. The teprenone group was administered 160 mg / kg by gavage. One hour after administration, all mice were orally administered 0.9 ml / kg of anhydrous ethanol to induce the model. One hour later, the animals were euthanized by cervical dislocation, the cardia and pylorus were ligated, and the entire stomach was removed. 1 mL of 1% formaldehyde solution was injected into the stomach, the cardia was ligated, and the stomach was immediately immersed in 1% formaldehyde solution. After soaking for 30 minutes, the stomach tissue was removed, cut along the greater curvature, and the stomach contents were rinsed clean with physiological saline. The stomach was then laid flat to observe and measure the damage to the gastric mucosa, and the ulcer index and ulcer inhibition rate were calculated. The results are shown in Table 3.

[0062] Ulcer Index Calculation Method: For linear lesions longer than 1 mm, measure their length and score 1 point per millimeter; if their width is greater than 1 mm, double the score based on the width in millimeters; if the length is less than 1 mm, score 0.5 points. Add the scores together to obtain the ulcer index of the animal.

[0063] Ulcer inhibition rate = (Ulcer index of model group - Ulcer index of treatment group) / Ulcer index of model group × 100%;

[0064] Relative ulcer inhibition rate = (ulcer inhibition rate of test compound) / (ulcer inhibition rate of teprenone).

[0065] A relative ulcer inhibition rate >1.20 is indicated as "++++";

[0066] The relative ulcer inhibition rate was 0.9-1.20, denoted as "+++";

[0067] The relative ulcer inhibition rate is 0.6-0.9, indicated by "++";

[0068] The relative ulcer inhibition rate was 0.3-0.6, indicated by "+";

[0069] 0 < relative ulcer inhibition rate < 0.3, indicated by " / " (extremely low activity).

[0070] Table 3. Antiulcer activity of the new peptides in an ethanol-induced mouse gastric ulcer model.

[0071]

[0072]

[0073] As shown in Table 3, the novel polypeptides described in this invention have significant anti-ulcer activity against ethanol-induced mouse ulcer models, and are mostly superior to positive control drugs.

[0074] Example 7: Pharmacodynamic study of the effect of the novel polypeptide on the healing of acute mechanical skin injury in rats.

[0075] SPF-grade SD rats (Beijing Vital River Laboratory Animal Technology Co., Ltd.), weighing 180–230g, were housed in clean, sterilized cages. Water, feed, and bedding were provided daily at regular intervals, and the temperature was maintained at 22℃ with a humidity of 55%–65%. The rats were kept in these cages for one week to allow them to acclimatize. The animals were then randomly assigned to two groups: a model control group (physiological saline) and a Jin Yintai control group (40 IU / cm³). 2 Shenzhen Huashengyuan Gene Engineering Development Co., Ltd.), and the tested peptide treatment group (8, 40 μg / cm). 2 Six rats were placed in each group. After successful anesthesia with intraperitoneal injection of 3% sodium pentobarbital, the hair 1 cm from the edge of the wound was trimmed. The wound area was first disinfected with povidone-iodine, and then locally disinfected with 75% alcohol. A 1.5 cm × 1.5 cm (diameter 1.5 cm) circular full-thickness skin wound was created 4 cm down the back from the midline of the ear, close to the neck, with the spine as the midline, extending to the muscle layer. The surrounding skin was fixed with rubber bands to form an animal model of acute mechanical injury. After modeling, the rats were housed individually with the wounds exposed. During dressing changes, the wound was first cleaned with povidone-iodine, then rinsed with sterile saline and dried. For the other groups, 40 μL of the corresponding drug solution was applied topically to the wound once a day. On days 3, 7, and 14 of drug administration, images of the wounds of each group of rats were taken. The wound area was calculated using image analysis software (Image J), ​​and the wound healing rate was calculated according to the formula. The results are shown in Table 4.

[0076] Table 4. Wound healing rate of rats in each group during the mechanical injury wound healing process.

[0077] Model control group 5.98±2.45 23.80±3.91 72.00±5.85 Jin Yintai control group 18.05±7.18 56.98±9.88* 85.32±3.12* <![CDATA[PA1 administration group (40 μg / cm 2 )]]> 22.25±5.17 58.12±6.71* 87.34±2.58* <![CDATA[PA2 administration group (40 μg / cm 2 )]]> 22.14±4.92 59.71±7.76* 92.92±2.15** <![CDATA[PA3 administration group (8 μg / cm 2 )]]> 20.95±4.17 59.84±8.36* 88.30±5.57* <![CDATA[PA4 administration group (8 μg / cm 2 )]]> 19.98±3.68 57.97±7.79* 86.45±6.45* <![CDATA[PA5 administration group (40 μg / cm 2 )]]> 22.82±9.39 59.58±9.66* 88.27±7.81* <![CDATA[PA6 administration group (40 μg / cm 2 )]]> 23.08±2.45 57.24±4.81* 89.52±4.39* <![CDATA[PA7 administration group (40 μg / cm 2 )]]> 21.45±3.25 59.22±7.17* 94.33±2.30** <![CDATA[PA8 administration group (40 μg / cm 2 )]]> 22.31±5.67 62.08±7.43* 89.37±8.66* <![CDATA[PA9 administration group (8 μg / cm 2 )]]> 23.01±4.05 63.39±2.73* 92.94±2.96** <![CDATA[PA10 administration group (40 μg / cm 2 )]]> 22.27±5.47 55.78±9.62* 92.23±3.87**

[0078] Compared with the model group, *: p < 0.05; **: p < 0.01;

[0079] As shown in Table 4, the novel polypeptide described in this invention can significantly promote the healing of skin lesions in rats, showing a significant difference compared to the model group, and its effect is superior to that of the positive control, Jin Yin peptide.

[0080] The results in summary indicate that the novel polypeptides PA1 to PA10 described in this invention can effectively promote the repair of mucosal damage in the digestive system, reduce the progression of gastrointestinal diseases such as acute and chronic gastritis and peptic ulcers, promote skin wound healing, and treat various skin diseases, providing a new approach and strategy for skin diseases, acute and chronic gastrointestinal diseases, tumors, and other related diseases. sequence list <110> Sichuan Good Doctor Panxi Pharmaceutical Co., Ltd. <120> Novel peptides and their application in the preparation of drugs for treating skin wounds or mucosal injuries <130> 2021.12.27 <141> 2021-12-27 <150> 2021100149285 <151> 2021-01-06 <150> 202110014929X <151> 2021-01-06 <150> 2021100298896 <151> 2021-01-11 <160> 10 <170> SIPOSequenceListing 1.0 <210> 1 <211> 6 <212> PRT <213> Artificial synthesis <400> 1 Val Pro Pro His Leu Phe 1 5 <210> 2 <211> 7 <212> PRT <213> Artificial synthesis <400> 2 Leu Arg Gly Phe Glu Pro Pro 1 5 <210> 3 <211> 4 <212> PRT <213> Artificial synthesis <400> 3 Lys Trp Ala Pro 1 <210> 4 <211> 5 <212> PRT <213> Artificial synthesis <400> 4 Thr Ala Ser Thr Leu 1 5 <210> 5 <211> 5 <212> PRT <213> Artificial synthesis <400> 5 Leu Ala Ala Val Asp 1 5 <210> 6 <211> 5 <212> PRT <213> Artificial synthesis <400> 6 Leu Ala Gly Leu Asp 1 5 <210> 7 <211> 5 <212> PRT <213> Artificial synthesis <400> 7 Leu Ala Gly Asn Lys 1 5 <210> 8 <211> 9 <212> PRT <213> Artificial synthesis <400> 8 Lys Cys Leu Lys Lys Gln Gln Gly Pro 1 5 <210> 9 <211> 11 <212> PRT <213> Artificial synthesis <400> 9 Thr Ala Thr Lys Pro Met Pro Thr Val Glu Thr 1 5 10 <210> 10 <211> 9 <212> PRT <213> Artificial synthesis <400> 10 Lys Ala Ser Thr Lys Phe Lys Val Glu 1 5

Claims

1. A novel polypeptide, characterized in that, The amino acid sequence of the new polypeptide is shown below: SEQ ID NO.1: VPPHLF.

2. The novel polypeptide according to claim 1, characterized in that, The novel polypeptide described herein has the ability to bind to the EGFR receptor.

3. The novel polypeptide according to claim 1, characterized in that, The novel polypeptide is prepared by chemical synthesis or by genetic engineering.

4. The novel polypeptide according to claim 1, characterized in that, The novel polypeptide is used as a component of common pharmaceuticals or daily chemical products.

5. The novel polypeptide according to claim 4, characterized in that, The daily chemical products mentioned are cosmetics.

6. A composition of novel polypeptides, characterized in that, A peptide containing the amino acid sequence of SEQ ID NO.1, or a pharmaceutically acceptable salt and a pharmaceutically acceptable carrier or excipient.

7. The use of the novel polypeptide according to any one of claims 1 to 6 in the preparation of medicaments for treating and / or preventing mechanical skin damage diseases and gastric ulcers.

8. The application according to claim 7, characterized in that, The drug is a formulation prepared by adding pharmaceutically acceptable excipients to a peptide with the amino acid sequence of SEQ ID NO.1 as the active ingredient.

9. The application according to claim 8, characterized in that, The preparation is an oral preparation or a topical preparation.

Citation Information

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