CN111701011A - Host defense peptide composition and application thereof in preparation of antibacterial drugs - Google Patents

Host defense peptide composition and application thereof in preparation of antibacterial drugs Download PDF

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CN111701011A
CN111701011A CN202010680824.3A CN202010680824A CN111701011A CN 111701011 A CN111701011 A CN 111701011A CN 202010680824 A CN202010680824 A CN 202010680824A CN 111701011 A CN111701011 A CN 111701011A
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王天放
倪国颖
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Zhongao Biomedical Technology Guangdong Co ltd
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    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
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    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K9/00Medicinal preparations characterised by special physical form
    • A61K9/0012Galenical forms characterised by the site of application
    • A61K9/0014Skin, i.e. galenical aspects of topical compositions
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    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61PSPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61PSPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/04Antibacterial agents

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Abstract

The invention belongs to the technical field of medicines, and relates to an application of a host defense peptide composition in preparation of antibacterial drugs, in particular to an application of host defense peptides, namely peptide 1.1 and peptide 1.9 in preparation of antibacterial drugs. The present invention provides compositions of a calein 1.1 peptide and a calein 1.9 peptide. Wherein the weight ratio of the calein 1.1 peptide to the calein 1.9 peptide is as follows: 1: 1-3. The antibacterial drug is used for resisting bacteria of skin mucosa. The bacteria include, but are not limited to, staphylococcus aureus (s. aureus), pseudomonas aeruginosa (p. aeruginosa), methicillin-resistant staphylococcus aureus (MRSA, GDM1.1263), Acinetobacter Baumannii (GDM1.609), Neisseria (Neisseria gonorrhoeae), and the like. The combination of the calein 1.1 peptide or the calein 1.9 peptide can play a synergistic effect, and has the best antibacterial effect. Can be used as antibacterial agent for first-line skin mucosa. Can be used for treating bacterial infection of skin mucosa.

Description

Host defense peptide composition and application thereof in preparation of antibacterial drugs
The technical field is as follows:
the invention belongs to the technical field of medicines, and relates to an application of a host defense peptide composition in preparation of antibacterial drugs, in particular to an application of host defense peptides, namely peptide compositions of Caerin1.1 (F1) and peptide compositions of Caerin1.9 (F3) in preparation of antibacterial drugs.
Background art:
skin and Soft Tissue Infections (SSTI) are caused by pathogenic invasion of the Skin and underlying Soft Tissue, with manifestations and severity varying from one cause to another. The estimated incidence of SSTI is 24.6 per 1000 years, with approximately 70% to 75% of all cases being treated in the outpatient setting. Staphylococcus aureus is a major cause of simple and complex infections of the skin and soft tissues. In addition, drug-resistant bacteria, primarily methicillin-resistant Staphylococcus aureus (community-acquired and healthcare-related methicillin-resistant Staphylococcus aureus), are associated with a significant increase in SSTI morbidity, mortality, hospitalization time, and expense. SSTIs are typically managed in communities, including self-administration of topical antibiotics, oral or systemic administration of antibiotics in outpatients or hospitals, depending on the severity of the symptoms. Currently, for mild impetigo and folliculitis, topical application of antibiotic ointments, such as mupirocin ointment, etc., is recommended.
Naturally derived host defense peptides are one of the first successful forms of defense of eukaryotes against bacteria, protozoa, fungi and viruses. More than 200 host defense peptides were isolated and identified from skin secretions of Australian frogs and toads. Many of these peptides, including the calein 1 peptide, have anti-tumor, antimicrobial and/or neuropeptide type activity. The cancer cell line of Caerin1.1(1GLLSVLGSV10AKHVLPHVLP20HVVPVIAEHL-NH2) has anticancer effect on various human cancer cell lines (including leukemia, lung cancer, colon cancer, CNS, melanoma, ovarian cancer, renal cancer, prostate cancer and breast cancer). The Caerin1.1 can also inhibit Bacillus cereus, Escherichia coli, Cryptococcus lactis, Listeria avirulenta, Cryptococcus, Pasteurella multocida, Staphylococcus aureus, Staphylococcus epidermidis, and Streptococcus. The calein 1.9 peptide (1GLFGVLGSI10AKHVLPHVVP20VIAEKL-NH2) has antibacterial activity against a wide range of gram-positive and gram-negative microbial strains.
The invention content is as follows:
the invention provides application of a calein 1.1 peptide or a calein 1.9 peptide in preparation of an antibacterial drug.
Further, the present invention provides compositions of a calein 1.1 peptide and a calein 1.9 peptide. Wherein the weight ratio of the calein 1.1 peptide to the calein 1.9 peptide is as follows: 1: 1-3, preferably 1: 1.
the invention also provides application of the composition in preparing antibacterial drugs.
The antibacterial drug is used for resisting bacteria of skin mucosa.
The bacteria include, but are not limited to, staphylococcus aureus (s. aureus), pseudomonas aeruginosa (p. aeruginosa), methicillin-resistant staphylococcus aureus (MRSA, GDM1.1263), Acinetobacter Baumannii (GDM1.609), Neisseria (Neisseria gonorrhoeae), and the like.
When the concentration of the calerin 1.1 peptide and the calerin 1.9 peptide is between 1/64MIC and 2 XMIC respectively, and the chessboard method is used for detection, and the bacteriostasis of acinetobacter baumannii and MRSA is measured, the superimposed bacteriostasis rate FICI is 0.5< FICI < 1.
The Caerinn 1.1 or 1.9 polypeptide or the composition thereof has an inhibitory effect on various drug-resistant bacteria, particularly drug-resistant staphylococcus aureus in vitro and in vivo.
Caerin1.9 does not induce the production of drug-resistant bacteria, whereas antibiotics can induce the production of drug-resistant bacteria. Caerinn 1.1 and 1.9 in vitro bacteriostasis have additive effects.
The Caerin1.1 and 1.9 peptides can be mixed with pharmaceutically acceptable carriers to prepare clinically acceptable external preparations, such as ointment, external gel, liniment, cream and the like, by a pharmaceutically conventional method.
The Caerinn 1.1 and 1.9 ointment can inhibit the drug-resistant staphylococcus aureus infection of the skin of mice.
The combination of the calein 1.1 peptide and the calein 1.9 peptide can play a synergistic effect, and has the best antibacterial effect. Can be used as antibacterial agent for first-line skin mucosa. Treating bacterial infection of skin mucosa.
Description of the drawings:
FIG. 1 shows the dynamic bacteriostatic action of calein 1.9 on tiwai1 of different bacteria:
FIG. 2 shows the bacteriostatic effect of the calerin polypeptide gel of in vivo bacteriostatic test 1 in experiment 5:
FIG. 3 is a test chart of in vivo test 2 of experiment 6:
FIG. 4 is an analysis result of the test result of FIG. 3.
FIG. 5 shows that the calein 1.1/1.9 gel inhibited skin infection in mice (A: Balb/C mice results; B: C57BL/6 mice results)
The specific implementation mode is as follows:
the PBS buffer used in the following examples can be prepared according to a conventional method.
Example 1: calerin 1.9MIC assay
The method comprises diluting with broth, measuring the operation specification according to the method of American Clinical Laboratory Standards Institute (CLSI), placing filter paper containing bacteria in a triangular flask containing 25ml liquid MH culture medium, culturing at 37 deg.C for 12-18h, and adjusting the concentration of the cultured bacteria to 2-5 × 10 with MH culture medium under OD600 condition5CFU/ml. In the experiment of 96-well cell culture plate, 100ul of bacterial suspension is added, and then 100ul of polypeptide solutions with different concentrations are sequentially added, wherein the final concentrations (mu g/ml) of the polypeptide solutions (the solvent is PBS buffer solution) are respectively as follows: 120. 60, 30, 15, 7.5, 3.75, 1.875. The PBS buffer solution with the same volume is used as a growth control group, each group is provided with three parallel holes, the three groups are cultured in a biochemical incubator at 37 ℃ for 24 hours, and a microplate reader is used for measuring the growth condition of bacteria (OD600 nm). The minimum Inhibitory concentration mic (minimum Inhibitory concentrations) is defined as the peptide concentration in the well where bacterial growth is completely inhibited.
Table 1: minimum inhibitory concentration MIC (μ g/ml) of Calerin 1.9 against Standard strains and clinically isolated multidrug resistant strains
Figure BDA0002585769860000031
The results show that: calerin 1.9 vs. standard strains: staphylococcus aureus (S.aureus), Pseudomonas aeruginosa (P.aeruginosa), methicillin-resistant Staphylococcus aureus (MRSA, GDM1.1263), Acinetobacter Baumannii (GDM1.609) and clinically isolated multidrug-resistant Staphylococcus aureus (MRSA pt1-3), Pseudomonas aeruginosa and Acinetobacter Baumannii (60 cag/ml), 7.5cag/ml,15cag/ml,7.5cag/ml (MRSA pt1-3), 60cag/ml and 15 cag/ml.
Example 2: calerin 1.9 against Staphylococcus aureus (GDM 1.4)41) Growth inhibition curves of Pseudomonas aeruginosa (GDM1.443), methicillin-resistant Staphylococcus aureus (MRSA, GDM1.1263) and Acinetobacter baumannii (GDM1.609) Experimental method that MH culture medium is used for adjusting the concentration of bacterial suspension to 2.0 × 105CFU/m L. Adding 100uL of bacterial suspension into an experimental well of a 96-well cell culture plate, adding equal-volume polypeptide solution (a PBS buffer solution is used as a solvent) with final concentration of MIC value and 1/4-time MIC value respectively, taking the PBS buffer solution added into the well as a bacterial growth control group, arranging three parallel groups in each group, culturing in a biochemical incubator at 37 ℃, measuring the OD600nm value of the 96-well plate by using a microplate reader, and recording for 24h in total.
Influence of the cairin 1.9 polypeptide on the growth curves of standard strains of staphylococcus aureus (s. aureus, GDM1.441), pseudomonas aeruginosa (p. aeruginosa, GDM1.443), methicillin-resistant staphylococcus aureus (MRSA, GDM1.1263) Acinetobacter Baumannii (GDM 1.609)).
The Caerin1.9 polypeptide was co-cultured with the bacteria at the Minimal Inhibitory Concentration (MIC) for 24 hours, respectively, and the bacterial growth was completely inhibited throughout. When the growth of the bacteria was determined by co-culturing the bacteria with the MIC value of 1/4, it was found that the bacteria began to grow after 4 hours in the PBS (phosphate buffered saline) control group and after 6 hours in the Caerinn 1.9 polypeptide, indicating that the Caerinn 1.9 polypeptide antimicrobial peptide could better retard the growth of the bacteria. After 48 hours of culture, the Minimal Inhibitory Concentration (MIC) of the Caerin1.9 polypeptide can still inhibit the growth of staphylococcus aureus (S.aureus, GDM1.441) and methicillin-resistant staphylococcus aureus (MRSA, GDM1.1263) Acinetobacter Baumannii (GDM1.609), but can not inhibit the growth of pseudomonas aeruginosa (P.aeruginosa, GDM 1.443). (FIG. 1)
Example 3: CAERIN1.9 INDUCTION-FREE DRUG RESISTANCE
Log of pseudomonas aeruginosa (GDM1.443) and methicillin-resistant staphylococcus aureus (MRSA, GDM1.1263) were collected and the suspension concentration was adjusted to 2.0 × 105CFU/ml in MH medium. Bacteria were kept in 96-well plates containing cererin 1.9 or piperacillin sodium (tasocin sodium) at MIC 1, control MH medium, equal volume of PBS. The medium was changed every 3 days and cultivation was continued for 3 months. After 3 months and 30 passages of culture, the MICs of calein 1.9 or Tazocin against MRSA and Pseudomonas aeruginosa were tested and resistance induction was compared and analyzed. The MICs of Caerin1.9 for Pseudomonas aeruginosa and MRSA were unchanged and no drug resistant strains were induced. The MIC of the antibiotic tazoxan resulted in a 16-fold increase in MRSA, while the MIC increased 8-fold.
TABLE 2
Figure BDA0002585769860000041
Example 4: combined antibacterial action of Caerin1.1 and Caerin1.9
The combined bacterial growth inhibition of both calirin 1.1 and calirin 1.9 on MRSA and Acinetobacter baumannii was tested by the checkerboard method, the bacterial suspension was 2.0 × 108CFU/ml, and the final concentration of antimicrobial peptides, calein 1.1 and calein 1.9, was diluted from 2-fold of MIC to 1/64 MIC. The overall effect was evaluated using a fractional inhibitory concentration FIC index (fractional inhibitory concentration index). The Minimum Inhibitory Concentration (MIC) values for calerin 1.1 and 1.9 when used alone are indicated by MICA and MICB, respectively. The respective concentrations of the good assembly points are indicated by a and B, respectively. The FIC index formula is: FIC index is FICA + FICB is A/MICA + B/MICB. When the FIC index is 0.5 or less, it means that the synergistic antibacterial action between A and B is exhibited, and 0.5<FIC index ≦ 1 means that there is an additive antibacterial effect between A and B. Combined use of calerin 1.9 and FIC 0.5<FIC index is less than or equal to 1, and the FIC index and the Acinetobacter baumannii have accumulated antibacterial action, so that after the FIC index and the Acinetobacter baumannii are used in combination, the antibacterial effect is obviously improved, and the antibacterial concentration of the MRSA and the Acinetobacter baumannii is obviously reduced (tables 3 and 4).
TABLE 3 results of the combination of Caerin1.1 and Caerin1.9 for gold resistance (MRSA) drug susceptibility testing
Figure BDA0002585769860000051
TABLE 4 results of drug susceptibility test of combination of Caerin1.1 and Caerin1.9 against A. baumannii
Figure BDA0002585769860000052
Example 5: in vivo bacteriostasis test 1
Preparation of a Calerin 1.1 and Calerin 1.9 polypeptide gel:
blank gel matrix: 46g Poloxamer
Figure BDA0002585769860000053
127 and 10g
Figure BDA0002585769860000054
68 (from BASF, Germany) in 200ml distilled water, storing in a refrigerator at 4 deg.C for 48 hr to dissolve completely, stirring, filtering with 0.22 μm microporous membrane, adding F1 or a 1.1/1.9 polypeptide dissolved in PBS buffer solution into blank gel matrix, and storing in a refrigerator at 4 deg.C for 48 hr to dissolve completely.
The in vivo bacteriostasis test method comprises the following steps:
for mouse skin wound, 10. mu.l of 8 × 105And infection of drug-resistant staphylococcus aureus in each ml, and taking pus on the 2 nd day. Then 5. mu.l pus + 5. mu.l different concentrations 25mg/ml, 12.5mg/ml,6.25mg/ml,3.125mg/ml calerin 1.1+ calerin 1.9 gel (F1+ F3 gel) and blank gel; after incubation for 30 minutes at room temperature, the plate cultures were counted. The result shows that the F1+ F3 gel can inhibit the growth of mouse drug-resistant staphylococcus aureus at 3mg/ml, the growth is obviously inhibited at 6.25mg/ml, the concentration of the gel is positively correlated, and the bacteriostasis efficiency of the gel is increased along with the increase of the gel concentration. (FIG. 2)
Example 6: in vivo experiment 2:
6-8 weeks female Balb/C trunk left and right sides each cut 1CM diameter skin, left (rat tail up) gold resistant (MARS,8 × 10)5V/ml) 12.5. mu.l + F1/F312.5. mu.l (500. mu.g/ml) mixed in vitro for 10 minutes to infect the wound, sealed translucent film, right (rat tail up) gold resistant (MARS,8 × 10)5Per ml) 12.5. mu.l + physiological saline 12.5. mu.l were mixed in vitro, and after 10 minutes the wound was infected and sealed with a translucent film. After 24 hours, a cotton swab is used for taking wound bacterial liquid, the wound bacterial liquid is put into 10ml of normal saline for elution, the wound bacterial liquid is diluted by 1:10 times, and a 30-microliter plate is used for counting the bacterial load. (FIG. 3)
Bacterial content on the left and right sides of the mouse. The result shows that the drug-resistant staphylococcus aureus treated by the calerin polypeptide gel has inhibition on the growth of the skin wound of the mouse, and the P is less than 0.05 by matching T test. (FIG. 4)
And (4) conclusion of results: the experimental results show that the drug-resistant staphylococcus aureus treated by the calerin polypeptide for 10 minutes has the capability of inhibiting the infection of the skin wound of the mouse.
Test 7: in vivo experiment 3:
female Balb/C mice (A) or C57BL/6 mice with 6-8 weeks are repeatedly pasted on the left and right sides of the back for 10 times respectively by using an elastic bandage (1 × 2 cm), so as to cause left and right skin lesions, and each wound is smeared with 10 mul of drug-resistant staphylococcus aureus (5 × 10)6cfu/ml). The wound was dressed with 25mg/ml of calerin 1.1 and 1.9 gels (F1+ F3 gel), control gel (P3) or untreated after 4 hours, and a second dressing after 16 hours, 2 times daily for 5 times total. And taking the skin lesion on the 3 rd day, homogenizing part of the skin lesion, and counting bacteria on a plate. The results show that the application of the calein polypeptide gel can inhibit the growth of drug-resistant staphylococcus aureus on the damaged skin of the mice in Balb/C and C57BL/6 mice, while the blank gel does not inhibit the growth of bacteria. (FIG. 5)
The advantages of the invention are as follows: can be used for treating slight bacterial infection of first-line skin mucosa, and preventing generation of drug-resistant bacteria.

Claims (10)

1. A host defense peptide composition, characterized by consisting of a calein 1.1 peptide and a calein 1.9 peptide.
2. The composition of claim 1, wherein the weight ratio of the calein 1.1 peptide to the calein 1.9 peptide is: 1: 1-1: 3.
3. the composition of claim 1 or 2, wherein the weight ratio of the calein 1.1 peptide to the calein 1.9 peptide is: 1: 1.
4. the composition of any of claims 1-3, wherein the concentration of the calein 1.1 peptide and the calein 1.9 peptide are each between 1/64MIC and 2 x MIC diluted in two.
5. Use of the host defense peptide composition of any of claims 1 to 4 for the preparation of an antibacterial agent.
6. The use of claim 5, wherein said antibacterial agent is an antibacterial agent.
7. The use according to claim 6, wherein the bacteria are: staphylococcus aureus, Pseudomonas aeruginosa, methicillin-resistant Staphylococcus aureus, Acinetobacter baumannii or Neisseria.
8. The use according to claim 5 or 6, wherein the antibacterial agent is an antibacterial agent against bacteria of the skin mucosa.
9. The composition of any one of claims 1 to 4, wherein said composition is formulated in a clinically acceptable dosage form with a pharmaceutically acceptable carrier.
10. The composition of claim 9, wherein the dosage form is an ointment, topical gel, liniment, cream.
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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113827702A (en) * 2021-11-08 2021-12-24 北京戴域生物技术有限公司 A pharmaceutical composition or cosmetic product for skin repair
CN115969960A (en) * 2022-12-02 2023-04-18 中奥生物医药技术(广东)有限公司 Application of Caerin1.1/1.9 peptide in preparation of drugs for inhibiting/treating bacterial biofilm growth

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20100316643A1 (en) * 2009-02-05 2010-12-16 The Regents Of The University Of California Targeted antimicrobial moieties
CN111303265A (en) * 2020-03-24 2020-06-19 中奥生物医药技术(广州)有限公司 One kind contains131I-labeled Caerin1.1 polypeptide and application thereof

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20100316643A1 (en) * 2009-02-05 2010-12-16 The Regents Of The University Of California Targeted antimicrobial moieties
CN111303265A (en) * 2020-03-24 2020-06-19 中奥生物医药技术(广州)有限公司 One kind contains131I-labeled Caerin1.1 polypeptide and application thereof

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
BOWEI MA 等: "Topical application of temperature-sensitive caerin 1.1 and 1.9 gel inhibits TC-1 tumor growth in mice", 《AM J TRANSL RES.》 *
DOUGLAS C. WOODHAMS 等: "Population trends associated with skin peptide defenses against chytridiomycosis in Australian frogs", 《POPULATION ECOLOGY》 *
SIMON T. STEJNBORNER 等: "New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria", 《J. PEPTIDE RES. 》 *
XUAN PAN 等: "Synthesized natural peptides from amphibian skin secretions increase the efficacy of a therapeutic vaccine by recruiting more T cells to the tumour site", 《BMC COMPLEMENTARY AND ALTERNATIVE MEDICINE》 *

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113827702A (en) * 2021-11-08 2021-12-24 北京戴域生物技术有限公司 A pharmaceutical composition or cosmetic product for skin repair
CN113827702B (en) * 2021-11-08 2022-07-15 时垠(上海)生物科技有限公司 A pharmaceutical composition or cosmetic product for skin repair
CN115969960A (en) * 2022-12-02 2023-04-18 中奥生物医药技术(广东)有限公司 Application of Caerin1.1/1.9 peptide in preparation of drugs for inhibiting/treating bacterial biofilm growth

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