CN113952446B - Application of bioactive peptide in inhibiting bone marrow toxicity - Google Patents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/38—Albumins
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
- A61K38/011—Hydrolysed proteins; Derivatives thereof from plants
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/06—Free radical scavengers or antioxidants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
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Abstract
The invention belongs to the technical field of medicines, and particularly relates to application of bioactive peptide in preparation of a medicament for inhibiting bone marrow toxicity. Wherein the bioactive peptide is albumin peptide or corn oligopeptide. The application is the inhibition of bone marrow toxicity caused by cisplatin, doxorubicin or daunorubicin by bioactive peptides. The bone marrow toxicity is hematopoietic function injury, and is specifically expressed by reduction of peripheral blood leukocyte number, and/or reduction of peripheral blood erythrocyte number, and/or reduction of platelet number. The invention discovers biological functions of albumin peptide and corn oligopeptide except oxidation resistance, and expands the application range of bioactive peptide; the bioactive peptide has remarkable effect of inhibiting bone marrow toxicity and has no side effect.
Description
Technical Field
The invention relates to the technical field of medicines, in particular to application of bioactive peptide in preparation of a medicament for inhibiting bone marrow toxicity.
Background
Chemotherapy is widely applied to clinical treatment of tumors as one of the main means of tumor treatment. However, due to the lack of specificity, the tumor cells are killed, normal cells are destroyed, and especially the damage to the marrow hematopoietic system with vigorous proliferation is serious, so that marrow hematopoiesis is inhibited, and peripheral blood cells are reduced; further, adverse reactions such as hypoimmunity and secondary infection can be caused, so that a plurality of tumor patients receiving chemotherapy are forced to reduce or interrupt treatment, and the treatment fails. Aiming at bone marrow toxicity caused by chemotherapy, granulocyte colony stimulating factor medicines are clinically used for promoting proliferation, differentiation and activation of hematopoietic cells at present, but the medicines are expensive, can cause adverse reactions such as bone pain, fever, leucopenia and the like, and some medicines can also stimulate the growth of certain malignant tumors. Therefore, the search for low-toxicity and high-efficiency drugs for treating cytopenia has become a hot spot in recent researches.
The albumin peptide is a peptide obtained by hydrolyzing milk protein or egg white protein, the corn oligopeptide is a peptide obtained by further enzymolysis of the obtained corn protein after deoiling and deproteinizing corn, and the albumin peptide and the corn oligopeptide have potential biological functions such as antioxidant activity, immunity regulation and the like.
Disclosure of Invention
The invention provides a novel function of bioactive peptide, and particularly relates to application of bioactive peptide in inhibiting bone marrow toxicity.
The technical scheme of the invention is as follows:
the invention provides application of bioactive peptide in preparing medicines for inhibiting bone marrow toxicity.
In a further embodiment, the bioactive peptide is an albumin peptide or a maize oligopeptide.
In a further embodiment, the use is for the inhibition of myelotoxicity caused by cisplatin, doxorubicin or daunorubicin by a bioactive peptide.
In a further embodiment, the bone marrow toxicity is a hematopoietic impairment, and is characterized by a reduction in peripheral blood leukocyte count, and/or a reduction in peripheral red blood cell count, and/or a reduction in platelet count.
Specifically, cisplatin causes impaired hematopoietic function in mice, mainly manifested by a decrease in the number of peripheral blood leukocytes and platelets, whereas albumin peptide and maize oligopeptide have an inhibitory effect on the bone marrow toxicity of cisplatin.
Doxorubicin has an inhibitory effect on bone marrow development in mice and consequently, impaired hematopoietic function, mainly manifested by a decrease in peripheral blood cell numbers, whereas albumin peptide and maize oligopeptide have an inhibitory effect on bone marrow toxicity of doxorubicin.
Daunorubicin inhibits bone marrow development in mice and thus causes impaired hematopoietic function, primarily manifested by a decrease in peripheral blood cell numbers, while albumin peptide and corn oligopeptide inhibit bone marrow toxicity of daunorubicin.
The beneficial effects of the invention are as follows:
the bioactive peptide is derived from natural products, has remarkable antioxidant activity, immune function regulation and the like, and has other advantages such as high safety, easy absorption, wide sources, low price and the like, so the bioactive peptide becomes a research hot spot in recent years. Aiming at the problems of the prior art that the bone marrow suppression toxicity of the chemotherapeutic drugs is more in clinical problems, mainly the reduction of the immune function of patients caused by the bone marrow suppression, and the interruption of the chemotherapy, the invention adopts three chemotherapeutic drugs to cause the bone marrow suppression animal model, observes the effect of albumin peptide and corn oligopeptide on the bone marrow suppression toxicity, and can provide safe and effective bioactive substances for controlling the bone marrow toxicity caused by the chemotherapeutic drugs for clinic.
Detailed Description
The following detailed description of the present invention is provided to facilitate understanding of the technical solution of the present invention, but is not intended to limit the scope of the present invention.
The albumin peptide (production lot number 20181072502) and the maize oligopeptide (production lot number 20180801027) used in the examples were purchased from Shandong Biotechnology Inc.
Embodiment one: investigation of inhibition of cisplatin (DDP) toxic side effects by Albumin peptide and corn oligopeptide
1. Experimental animal
SPF class C57BL/6 male mice of 6-8 weeks old were purchased from Henan province laboratory animal center (production license: SCXK (Yu) 2017-0001) and fed in Henan province hepatopathy pharmacology important laboratory animal houses. After 5 days of adaptive feeding and observation, healthy and active mice were selected for the experiment.
2. Experimental method
2.1 grouping and administration
24 SPF-class C57BL/6 mice with the weight of 18-20 g are randomly divided into 4 groups, A: control group, B: DDP group, C: ddp+albumin peptide group, D: DDP+Y maize oligopeptide group. B. C, D groups were intraperitoneally injected with DDP at a dose of 4mg/kg daily for 5 consecutive days, and group A was intraperitoneally injected with an equal amount of physiological saline. After 1 hour, the C, D groups were then gavaged with 600mg/kg (0.2 mL/10 g) of albumin peptide and corn oligopeptide, A, B groups were gavaged with equal amounts of physiological saline, respectively. Once every other day for 5 consecutive days for 3 times. The general status of each group of mice was observed daily.
2.2 mouse peripheral blood cell count
Whole blood was counted for Red Blood Cells (RBC), white Blood Cells (WBC), platelets (PLT) using a penta 80 fully automatic hemocytometer (HORIBA, japan).
3. Results
As shown in table 1, the number of White Blood Cells (WBCs) in peripheral blood was significantly reduced in DDP mice compared to normal control (p < 0.01). The mice given albumin peptide by gavage had a significantly increased number of White Blood Cells (WBCs) in peripheral blood (p-value less than 0.01) compared to the DDP group.
The number of Platelets (PLT) in peripheral blood was significantly reduced in DDP mice compared to normal control (p < 0.01). The number of Platelets (PLT) in peripheral blood was significantly increased (p < 0.05) in the DDP + albumin peptide mice compared to the DDP group, and more significantly (p < 0.01) in the peripheral blood of the DDP + maize oligopeptide peptide mice.
There was no significant difference in the number of Red Blood Cells (RBCs) in the peripheral blood of each group of mice.
TABLE 1 cisplatin blood cell count results
P <0.01 compared to normal control group; compared with DNR group, #p <0.05, #p < 0.01.
The above results demonstrate that DDP causes impaired hematopoietic function in mice, mainly manifested by a decrease in peripheral blood leukocyte and platelet count, while albumin peptide and corn oligopeptide have an inhibitory effect on DDP bone marrow toxicity.
Embodiment two: investigation of the inhibition of Adriamycin (DOX) induced toxicity by Albumin peptide and maize oligopeptide
1. Experimental animal
SPF class C57BL/6 male mice of 6-8 weeks old were purchased from Henan province laboratory animal center (production license: SCXK (Yu) 2017-0001) and fed in Henan province hepatopathy pharmacology important laboratory animal houses. After 5 days of adaptive feeding and observation, healthy and active mice were selected for the experiment.
2. Experimental method
2.1 grouping and administration
24 SPF-class C57BL/6 mice with the weight of 18-20 g are randomly divided into 4 groups, A: control group, B: DOX group, C: DOX + albumin peptide group, D: DOX+maize oligopeptide group. B. Group C, D DOX was injected intraperitoneally at a dose of 17mg/kg, and group A was injected intraperitoneally with an equivalent amount of physiological saline. After 1 hour, the C, D groups were then gavaged with 600mg/kg (0.2 mL/10 g) of albumin peptide and corn oligopeptide, A, B groups were gavaged with equal amounts of physiological saline, respectively. Once every other day for 5 consecutive days for 3 times. The general status of each group of mice was observed daily.
2.2 mouse peripheral blood cell count
On day 5 of the experiment, the eyeballs of each group of mice were bled, EDTA was added to the whole blood, and the whole blood was counted for Red Blood Cells (RBC), white Blood Cells (WBC), and Platelets (PLT) using a penta 80 full automatic hemocytometer (HORIBA, japan).
3. Results
As shown in table 2, the number of White Blood Cells (WBCs) in peripheral blood was significantly reduced in the DOX group mice compared to the normal control group (p < 0.01). Compared with the DOX group, the number of White Blood Cells (WBC) in peripheral blood of mice of the DOX+albumin peptide group and the DOX+corn oligopeptide group is obviously increased (p < 0.01).
The number of Red Blood Cells (RBCs) in peripheral blood was significantly reduced in the DOX group of mice compared to the normal control group (p < 0.01). The number of Red Blood Cells (RBC) in peripheral blood was significantly increased in both the DOX + albumin peptide group and the DOX + maize oligopeptide group mice (p < 0.01) compared to the DOX group.
The number of Platelets (PLT) in peripheral blood was significantly reduced in the DOX group of mice compared to the normal control group (p < 0.01). The number of Platelets (PLT) in peripheral blood was significantly increased (p < 0.01) in both groups of mice given albumin peptide and maize oligopeptide by gavage compared to the DOX group.
TABLE 2 Adriamycin blood cell count results
P <0.01 compared to normal control group; in comparison with the DOX group, #p <0.05, #p < 0.01.
The above results demonstrate that DOX has an inhibitory effect on bone marrow development in mice and thus causes impaired hematopoietic function, mainly manifested by a decrease in peripheral blood cell count, while albumin peptide and maize oligopeptide have an inhibitory effect on bone marrow toxicity of DOX.
Embodiment III: inhibition study of toxicity caused by Daunorubicin (DNR) by Albumin peptide and corn oligopeptide
1. Experimental animal
SPF class C57BL/6 male mice of 6-8 weeks old were purchased from Henan province laboratory animal center (production license: SCXK (Yu) 2017-0001) and fed in Henan province hepatopathy pharmacology important laboratory animal houses. After 5 days of adaptive feeding and observation, healthy and active mice were selected for the experiment.
2. Experimental method
2.1 grouping and administration
24 SPF-class C57BL/6 mice with the weight of 18-22 g are randomly divided into 4 groups, A: control group, B: daunorubicin (DNR) group, C: dnr+albumin peptide group, D: dnr+maize oligopeptide group. B. Group C, D DNR was injected intraperitoneally at a dose of 1mg/kg, and group A was injected intraperitoneally with an equivalent amount of physiological saline. After 1 hour, the C, D groups were then gavaged with 600mg/kg (0.2 mL/10 g) of albumin peptide and corn oligopeptide, A, B groups were gavaged with equal amounts of physiological saline, respectively. Once every other day for 5 consecutive days for 3 times. The general status of each group of mice was observed daily.
2.2 mouse peripheral blood cell count
On the 5 th day of the experiment, eyeballs of each group of mice are taken to obtain blood, EDTA is added to the blood for anticoagulation to obtain whole blood. The whole blood obtained was counted for Red Blood Cells (RBC), white Blood Cells (WBC) and Platelets (PLT) using a penta 80 fully automatic hemocytometer (HORIBA, japan).
3. Results
As shown in table 3, the number of White Blood Cells (WBCs) in the peripheral blood was significantly reduced in DNR group mice compared to the normal control group (p < 0.01). Compared with the DNR group, the number of White Blood Cells (WBC) in the peripheral blood of the mice of the DNR+maize oligopeptide group is obviously increased, and the number of White Blood Cells (WBC) in the peripheral blood of the mice of the DNR+albumin peptide group is more increased.
The number of Red Blood Cells (RBCs) in the peripheral blood of mice in the DNR group was significantly reduced (p < 0.01) compared to the normal control group. Compared with the DNR group, the DNR+albumin peptide group and the number of Red Blood Cells (RBC) in the peripheral blood of the mice are obviously increased, but the DNR+corn oligopeptide group and the DNR group have no obvious difference in the number of Red Blood Cells (RBC) in the peripheral blood of the mice.
The number of Platelets (PLT) in peripheral blood was significantly reduced in DNR mice compared to normal control (p < 0.01). The number of Platelets (PLT) in peripheral blood was significantly increased (p < 0.05) in both groups of mice given albumin peptide and maize oligopeptide by gavage compared to DNR group.
TABLE 3 daunorubicin blood cell count results
| Grouping | WBC number (10≡3/mm) 3 ) | RBC number (10≡6/mm) 3 ) | PLT number (10≡3/mm) 3 ) |
| Normal control group | 7.20±1.04 | 9.65±0.89 | 1715.0±262.7 |
| DNR group | 2.13±0.72** | 5.78±0.92** | 955.0±164.6** |
| DNR+Albumin peptide group | 6.02±0.76# | 8.01±1.36## | 1325.2±224.7# |
| DNR+maize oligopeptides | 4.88±2.48# | 7.73±1.01 | 1227.2±274.8# |
P <0.01 compared to normal control group; compared with DNR group, #p <0.05, #p < 0.01.
The above results demonstrate that DNR has an inhibitory effect on bone marrow of mice and thus causes impaired hematopoietic function, which is mainly manifested by a decrease in peripheral blood cell count, while albumin peptide and maize oligopeptide have an inhibitory effect on bone marrow toxicity of DNR.
The above-described embodiments are merely preferred embodiments of the present invention and are not intended to limit the scope of the present invention, so that all equivalent changes or modifications of the structure, characteristics and principles described in the claims should be included in the scope of the present invention.
Claims (4)
1. The application of bioactive peptide in preparing bone marrow toxicity inhibiting medicine is characterized in that the bioactive peptide is corn oligopeptide.
2. The use of a bioactive peptide according to claim 1 for the preparation of a medicament for inhibiting bone marrow toxicity, wherein said use is the inhibition of bone marrow toxicity caused by cisplatin, doxorubicin or daunorubicin by the bioactive peptide.
3. The use of a bioactive peptide according to claim 1 for the manufacture of a medicament for inhibiting bone marrow toxicity, wherein said bone marrow toxicity is hematopoietic impairment.
4. The use of a bioactive peptide according to claim 3 for the manufacture of a medicament for inhibiting bone marrow toxicity, wherein said hematopoietic impairment is a reduction in peripheral blood leukocyte count, and/or a reduction in peripheral blood red cell count, and/or a reduction in platelet count.
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Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1994028013A1 (en) * | 1993-05-20 | 1994-12-08 | Research Corporation Technologies, Inc. | Peptides for suppression of myeloid progenitor cell proliferation and treatment of septic shock |
| CN1694719A (en) * | 2001-08-30 | 2005-11-09 | 蔡13医疗研究团体有限公司 | Casein derived peptides and uses thereof in therapy |
| CN101124261A (en) * | 2004-03-01 | 2008-02-13 | 派普特拉医药有限公司 | Casein derived peptides and therapeutic uses thereof |
| CN101270152A (en) * | 2008-05-13 | 2008-09-24 | 福州大学 | Peptide medicament series for accelerating medulla hematopoiesis cell proliferation |
| CN101270151A (en) * | 2008-05-13 | 2008-09-24 | 福州大学 | Peptide medicaments for accelerating medulla hematopoiesis cell proliferation |
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Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1994028013A1 (en) * | 1993-05-20 | 1994-12-08 | Research Corporation Technologies, Inc. | Peptides for suppression of myeloid progenitor cell proliferation and treatment of septic shock |
| CN1694719A (en) * | 2001-08-30 | 2005-11-09 | 蔡13医疗研究团体有限公司 | Casein derived peptides and uses thereof in therapy |
| CN101124261A (en) * | 2004-03-01 | 2008-02-13 | 派普特拉医药有限公司 | Casein derived peptides and therapeutic uses thereof |
| CN101270152A (en) * | 2008-05-13 | 2008-09-24 | 福州大学 | Peptide medicament series for accelerating medulla hematopoiesis cell proliferation |
| CN101270151A (en) * | 2008-05-13 | 2008-09-24 | 福州大学 | Peptide medicaments for accelerating medulla hematopoiesis cell proliferation |
Non-Patent Citations (4)
| Title |
|---|
| New bioactive peptide reduces the toxicity of chemotherapy drugs and increases drug sensitivity;Xian Li等;ONCOLOGY REPORTS;第38卷(第1期);第129-140页 * |
| 四种生物活性肽基于抗氧化作用的药理活性研究;游普云;万方学位论文;全文 * |
| 四种生物活性肽对顺铂所致小鼠肾毒性和骨髓抑制毒性的影响;赵莹等;郑州大学学报(医学版);第58卷(第3期);第341-345页 * |
| 源于驴血清白蛋白的肽HP-6对造血***的体内外作用研究;李昊等;中国中药杂志;第36卷(第16期);摘要 * |
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