CN117917432A - Non-hemolytic artificial polypeptide and application thereof in oral products - Google Patents
Non-hemolytic artificial polypeptide and application thereof in oral products Download PDFInfo
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- CN117917432A CN117917432A CN202310027933.9A CN202310027933A CN117917432A CN 117917432 A CN117917432 A CN 117917432A CN 202310027933 A CN202310027933 A CN 202310027933A CN 117917432 A CN117917432 A CN 117917432A
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
- C07K14/43586—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects from silkworms
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61P31/10—Antimycotics
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q11/00—Preparations for care of the teeth, of the oral cavity or of dentures; Dentifrices, e.g. toothpastes; Mouth rinses
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q17/00—Barrier preparations; Preparations brought into direct contact with the skin for affording protection against external influences, e.g. sunlight, X-rays or other harmful rays, corrosive materials, bacteria or insect stings
- A61Q17/005—Antimicrobial preparations
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Zoology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Pharmacology & Pharmacy (AREA)
- Dermatology (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Insects & Arthropods (AREA)
- Oral & Maxillofacial Surgery (AREA)
- Tropical Medicine & Parasitology (AREA)
- Toxicology (AREA)
- Birds (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
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Abstract
The invention provides a non-hemolytic artificial polypeptide and application thereof in oral products, and the sequence is shown as SEQ ID NO. 1. The artificial polypeptide without hemolysis has the advantages of high titer and weak hemolysis, can selectively inhibit pathogenic bacteria, can not cause obvious harm to the growth of probiotics, can be used for preparing antibacterial preparations, such as preparations for preventing and treating pathogenic bacteria infectious diseases, and has good clinical transformation capacity and disease prevention capacity.
Description
Technical Field
The invention belongs to the field of genetic engineering. More particularly, to a non-hemolytic artificial polypeptide and its use in oral products.
Background
The discovery and application of antibiotics lead the clinical technology for preventing and treating pathogenic bacteria infectious diseases to generate revolutionary leaps and make great contribution to the healthy development of human beings. In recent years, due to the increasing bacterial resistance to antibiotics, antibiotic resistance has become a great risk for humans. With the increasing severity of bacterial resistance, the discovery of new antimicrobial agents has been urgent.
Bacterial resistance is closely related to the biological membrane (such as cell membrane) of the bacteria, and antibacterial peptides generally achieve antibacterial effect by destroying the physical integrity of the bacterial cell membrane, so that the antibacterial peptides are used for preventing and treating pathogenic bacteria infectious diseases, and are not easy to generate bacterial resistance.
Cecropins (cecropins), which are the first animal antimicrobial peptides to be discovered, generally contain 37-39 amino acid residues, do not contain cysteine, have strong basicity in the N-terminal region, can form a nearly perfect amphipathic helix structure, and can form a hydrophobic helix in the C-terminal region, and have a hinge region formed by glycine and proline between the two, and have the characteristics of strong antibacterial ability, but have low potency and strong hemolytic property (International Journal of Antimicrobial Agents.(2009).International Journal of Antimicrobial Agents,34(6),iii.doi:10.1016/s0924-8579(09)00446-4),, which is unfavorable for mass popularization and use.
Disclosure of Invention
Aiming at the defects of the prior art, the invention aims to provide the artificial polypeptide without hemolysis and the application thereof in oral products, which are obtained by artificially modifying cecropin A, have high potency and weak hemolysis and can be widely popularized and used.
It is a first object of the present invention to provide artificial polypeptides that are free of hemolysis.
The second object of the present invention is to provide a polypeptide obtained by subjecting the N-terminus of the above polypeptide to acetylation modification.
A third object of the present invention is to provide an antibacterial peptide.
A fourth object of the present invention is to provide an application of the above polypeptide or antimicrobial peptide in preparing an antimicrobial preparation.
A fifth object of the present invention is to provide the use of the above polypeptide or antimicrobial peptide in the preparation of an oral product.
A sixth object of the present invention is to provide an antibacterial agent.
The above object of the present invention is achieved by the following technical scheme:
The non-hemolytic artificial polypeptide contains 20 amino acids, has a molecular formula of C 177H301N49O40S1, a molecular weight of 3787.70, a total average hydrophilicity of-1.145, has the advantages of high titer and weak hemolytic property, can selectively inhibit pathogenic bacteria, can not cause obvious harm to the growth of probiotics, can be used for preparing antibacterial preparations, such as preparations for preventing and treating pathogenic bacteria infectious diseases, and has good clinical transformation capacity and disease prevention capacity. Therefore, the invention provides a non-hemolytic artificial polypeptide with a sequence shown as SEQ ID NO. 1, a polypeptide obtained by carrying out acetylation modification on the N end of the polypeptide, an antibacterial peptide with more than 90% of homology with the polypeptide, application of the polypeptide or the antibacterial peptide in preparation of antibacterial preparations, and application of the polypeptide or the antibacterial peptide in preparation of oral products.
Preferably, the antibacterial formulation is a formulation against bacterial infection.
Preferably, the oral product has the effect of preventing and treating oral diseases.
Further preferably, the oral disease is caused by infection with oral pathogenic bacteria.
Further preferably, the oral pathogenic bacteria is one or more of staphylococcus aureus, escherichia coli, actinobacillus actinomyces, fusobacterium nucleatum, porphyromonas gingivalis, candida albicans, streptococcus mutans, fosetylbacteria, treponema denticola, actinomyces viscosus, or praecox intermedia.
Preferably, the oral product includes, but is not limited to, an oral care solution, a mouthwash effervescent tablet, a mouthwash or toothpaste, and the like.
The non-hemolytic artificial polypeptide can selectively inhibit pathogenic bacteria, can not cause obvious harm to the growth of probiotics, can be used for preparing antibacterial preparations, such as preparations for preventing and treating pathogenic bacteria infectious diseases, and has good clinical transformation capacity and disease prevention capacity. Therefore, bacteriostats containing the above polypeptides or the above antimicrobial peptides should be within the scope of the present invention.
The invention has the following beneficial effects:
The non-hemolytic artificial polypeptide has the advantages of high titer and weak hemolysis, can selectively inhibit pathogenic bacteria, can not cause obvious harm to the growth of probiotics, can be used for preparing antibacterial preparations, such as preparations for preventing and treating pathogenic bacteria infectious diseases, and has good clinical transformation capacity and disease prevention capacity.
Drawings
FIG. 1 is a LCMS spectrum of an acetylated artificial polypeptide of example 1.
FIG. 2 is an HPLC plot of the acetylated artificial polypeptide of example 1.
Detailed Description
The invention is further illustrated in the following drawings and specific examples, which are not intended to limit the invention in any way. Unless specifically stated otherwise, the reagents, methods and apparatus employed in the present invention are those conventional in the art.
Reagents and materials used in the following examples are commercially available unless otherwise specified.
Staphylococcus aureus (No. ATCC 29213), escherichia coli (No. ATCC 15597), actinobacillus actinomyces (No. ATCC 700685), fusobacterium nucleatum (No. ATCC 10953), porphyromonas gingivalis (No. ATCC 33277), candida albicans (No. ATCC 10231), streptococcus mutans (No. ATCC 25175), sartana (No. ATCC 43037), treponema pallidum (No. ATCC 35405), actinomyces viscosus (No. ATCC 27044), praecox intermedia (No. ATCC 25611), lactobacillus salivarius (No. ATCC 11741), lactobacillus rhamnosus (No. ATCC 11981), enterococcus faecalis (No. ATCC 29212), lactococcus lactis (No. ATCC 11007): all from the American type culture Collection (AMERICAN TYPE culture collection).
EXAMPLE 1 preparation of a non-hemolytic Artificial polypeptide
Selecting N-terminal amino acids 1-15 of cecropin A (the sequence is shown as SEQ ID NO: 2: KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK), adding 3 lysines in front of the N-terminal amino acid 1, adding a leucine and an asparagine at the end of the N-terminal amino acid 15, and obtaining an amino acid sequence: KKKKWKLFKKIEKVGQNILN (shown as SEQ ID NO: 1). The target polypeptide with the sequence shown as SEQ ID NO. 1 is synthesized by a protein chemical synthesis method (dehydration condensation) by the Minkangde New drug development Limited company of Shanghai medicine, and in order to improve the stability of the target polypeptide in the following test experiment, the first lysine at the N end of the target polypeptide is subjected to acetylation modification to obtain the acetylated artificial polypeptide of the example 1.
The basic physicochemical properties of the acetylated artificial polypeptide are as follows:
The number of amino acids is 20; molecular weight 3787.70; the theoretical isoelectric point is 10.59; the molecular formula is C 177H301N49O40S1; the total number of negatively charged residues (Asp+Glu) is 1; the total number of positively charged residues (Arg+Lys) was 8; an instability index of 38.57<40.00, classified as a stable protein; fat coefficient 92.50 (good stability); the total average hydrophilicity was-1.145 (hydrophilic protein, soluble in water).
LCMS analysis and HPLC analysis were then performed on the above acetylated artificial polypeptides, and the spectra are shown in fig. 1 and 2. As can be seen from the figure, the purity of the acetylated artificial polypeptide was 98.83% and the molecular weight was 3787.70.
Comparative example 1
1 Lysine is added before the N-terminal amino acid 1,1 leucine and 1 asparagine are added at the tail of the 37 amino acid, 3 lysines are adopted in the middle for tandem connection, and then the artificial polypeptide sequence of the comparative example 1 is obtained: KKWKLFKKIEKVGQNIKKKVVGQATQIAKLN (shown as SEQ ID NO: 3). The target polypeptide with the sequence shown as SEQ ID NO. 3 is synthesized by a protein chemical synthesis method (dehydration condensation) by the Minkangde New drug development Limited company of Shanghai medicine, and in order to improve the stability of the target polypeptide in the following test experiment, the first lysine at the N end of the target polypeptide is subjected to acetylation modification to obtain the acetylated artificial polypeptide of the comparative example 1.
The basic physicochemical properties of the acetylated artificial polypeptide are as follows:
The number of amino acids is 31; molecular weight 3595.42; the theoretical isoelectric point is 10.60; the molecular formula is C 167H289N47O40; the total number of negatively charged residues (Asp+Glu) is 1; the total number of positively charged residues (Arg+Lys) was 10; an instability index of 8.84<40.00, classified as a stable protein; fat coefficient 97.42 (good stability); the total average hydrophilicity was-0.719 (hydrophilic protein, soluble in water).
Comparative example 2
1 Leucine and 1 asparagine are added at the tail end of N-terminal amino acids 1-15 and amino acids 28-37 of cecropin A (the sequence is shown as SEQ ID NO: 2: KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK), and 2 lysines are adopted in the middle for tandem connection, so that the artificial polypeptide sequence of comparative example 2 is obtained: KWKLFKKIEKVGQNIKKVVGQATQIAKLN (shown as SEQ ID NO: 4). The target polypeptide with the sequence shown as SEQ ID NO.4 is synthesized by a protein chemical synthesis method (dehydration condensation) by the Minkangde New drug development Limited company of Shanghai medicine, and in order to improve the stability of the target polypeptide in the following test experiment, the first lysine at the N end of the target polypeptide is subjected to acetylation modification to obtain the acetylated artificial polypeptide of the comparative example 2.
The basic physicochemical properties of the acetylated artificial polypeptide are as follows:
The number of amino acids was 29; molecular weight 3339.07; the theoretical isoelectric point is 10.48; the molecular formula is C 155H265N43 O38; the total number of negatively charged residues (Asp+Glu) is 1; the total number of positively charged residues (Arg+Lys) was 8; an instability index of 8.76<40.00, classified as a stable protein; fat coefficient 104.14 (good stability); the total average hydrophilicity was-0.500 (hydrophilic protein, soluble in water).
Comparative example 3
1 Leucine and 1 asparagine are added at the tail end of N-terminal amino acids 1-15 and amino acids 28-37 of cecropin A (the sequence is shown as SEQ ID NO: 2: KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK), 3 lysines are adopted in the middle for tandem connection, and then the artificial polypeptide sequence of comparative example 3 is obtained: KWKLFKKIEKVGQNIKKKVVGQATQIAKLN (shown as SEQ ID NO: 5). The target polypeptide with the sequence shown as SEQ ID NO.5 is synthesized by a protein chemical synthesis method (dehydration condensation) by the Minkangde New drug development Limited company of Shanghai medicine, and in order to improve the stability of the target polypeptide in the following test experiment, the first lysine at the N end of the target polypeptide is subjected to acetylation modification to obtain the acetylated artificial polypeptide of the comparative example 3.
The basic physicochemical properties of the acetylated artificial polypeptide are as follows:
The number of amino acids is 30; molecular weight 3467.25; the theoretical isoelectric point is 10.54; the molecular formula is C 161H277N45O39; the total number of negatively charged residues (Asp+Glu) is 1; the total number of positively charged residues (Arg+Lys) was 9; an instability index of 8.80<40.00, classified as a stable protein; fat coefficient 100.67 (good stability); the total average hydrophilicity was-0.613 (hydrophilic protein, soluble in water).
Test example 1 haemolysis of acetylated artificial polypeptides
The acetylated artificial polypeptide obtained in example 1 was evaluated for haemolysis by reference to the guidelines for pharmaceutical irritation, allergy and haemolysis study.
Firstly, 20mL of rabbit heart blood is taken and placed in an Erlenmeyer flask (the Erlenmeyer flask is filled with glass beads), the Erlenmeyer flask is shaken for 10min, fibrinogen is removed, the defibrinated blood is formed, 10 times of 0.9wt% sodium chloride solution is added, the mixture is shaken uniformly, centrifugation is carried out for 10min at 1500r/min, the supernatant is removed, the precipitated red blood cells are washed by 0.9wt% sodium chloride solution until the supernatant does not appear red after centrifugation, and the obtained red blood cells are diluted into a 2% red blood cell suspension by 0.9wt% sodium chloride solution according to the volume. 2.5mL of a 0.9wt% sodium chloride solution was used as a negative control group, 2.5mL of purified water was used as a positive control group, 2.5mL of a sodium chloride solution having a sample concentration of 0.5wt% (sodium chloride concentration of 0.9 wt%) was prepared as a sample group ① from the acetylated artificial polypeptide obtained in example 1, 2.5mL of a sodium chloride solution having a sample concentration of 0.5wt% (sodium chloride concentration of 0.9 wt%) was prepared as a sample group ② from the acetylated artificial polypeptide obtained in comparative example 1, 2.5mL of a sodium chloride solution having a sample concentration of 0.5wt% (sodium chloride concentration of 0.9 wt%) was prepared as a sample group ③, 2.5mL of a sodium chloride solution having a sample concentration of 0.5wt% (sodium chloride concentration of 0.9 wt%) was prepared as a sample group ④ from the acetylated artificial polypeptide obtained in comparative example 3, and 2.5mL of a sodium chloride solution having a sample concentration of 0.5wt% (sodium chloride concentration of 0.9 wt%) was prepared as a sample group ⑤ from the original cecropin A. After 2.5mL of rabbit erythrocyte suspension is added respectively, the mixture is shaken and mixed uniformly, the mixture is placed in a water bath with the temperature of 37+/-0.5 ℃ for 3 hours, the mixture is taken out after the heat preservation is finished, and the mixture is centrifuged for 10 minutes at 3000r/min, and the supernatant is sucked into a cuvette.
The experiment was repeated three times and the results averaged. Taking the negative control group as a blank, respectively measuring the absorbance (A positive) of the positive control group, the absorbance (A negative) of the negative control group and the absorbance (A sample) of the sample group at 542nm by adopting a colorimetric method, and calculating according to the formula of 'hemolysis rate= (A sample-A negative)/(A positive-A negative) ×100%': the hemolysis rate of sample group ① was 0.95%, significantly lower than 6.22% of sample group ②, 8.11% of sample group ③, 1.14% of sample group ④, and 3.01% of sample group ⑤, and it can be seen that the acetylated artificial polypeptide of example 1 of the present invention has lower hemolysis.
Test example 2 cytotoxicity of acetylated artificial polypeptides
The test example detects cytotoxicity of the acetylated artificial polypeptide by an MTT colorimetric method, and specifically comprises the following steps:
(1) Human oral epithelial cells HOEC (from Shenzhen Haodihua Biotechnology Co., ltd.) were digested with 1mL of 0.25wt% trypsin for 2min, centrifuged at 800rpm for 5min, resuspended in MEM complete medium, and then flask-expanded at 37℃under 5% volume fraction CO 2 and saturated humidity for 24h.
(2) The cells in the flask were found to grow to 90% of the area of the bottom of the flask, and the cells were collected, then inoculated into 96-well plates at 10 4 cells/well, and further cultured until 70% of the area of the bottom of the plate was covered.
(3) After removal of the medium, 30mL of MEM complete medium containing the acetylated artificial polypeptide of example 1 at a final concentration of 0.5wt% was added, respectively, as sample set ①; 30mL of MEM complete medium containing the acetylated artificial polypeptide of comparative example 3 at a final concentration of 0.5wt% was added, respectively, as sample group ②; 30mL of MEM complete medium containing cecropin A at a final concentration of 0.5wt% was added as sample group ③, respectively; a blank (30 mL of MEM complete medium containing 10wt% of fetal bovine serum without the test sample), a negative (30 mL of 0.9wt% sodium chloride solution) and a positive (30 mL of dimethyl sulfoxide solution with a volume fraction of 5%) were simultaneously established, and the culture was continued under the same culture conditions of (1) for 24 hours.
(4) Mu.L of 5mg/mL MTT solution was added to each well, the culture was continued for 4 hours, the liquid in the well was discarded, 150. Mu.L of DMSO was added, and after shaking for 10 minutes, absorbance was measured at 570nm and 630nm using an ELISA reader.
Calculated according to the formula "relative proliferation rate (RGR) =sample group absorbance/blank group absorbance×100%": the relative proliferation rate of sample group ① is 98.19+ -7.05%, which is significantly higher than that of sample group ② (85.14 + -1.04%), sample group ③ (81.44 + -3.95%), and positive control group (12.31+ -0.15%), and is comparable to that of negative control group (99.52+ -3.71%), and it is seen that the non-hemolytic artificial polypeptide of the present invention has lower cytotoxicity.
Test example 3 an acetylated artificial polypeptide has a significant inhibitory effect on pathogenic bacteria
This test example tested the inhibitory effect of the acetylated artificial polypeptide of example 1 (sample set ①, action concentration 0.5 wt%) and cecropin a (sample set ②, action concentration 0.5 wt%) against 11 oral pathogens. The experimental method refers to a method for checking the antibacterial effect (suspension quantification method) of 7.3 antibacterial daily chemical products under the item QBT 2738-2012-evaluation method of the antibacterial effect of daily chemical products, and establishes a negative control group (sodium chloride solution, final concentration of 0.09 wt%) and a positive control group (cetylpyridinium chloride, final concentration of 0.1 wt%) for 2min. The measurement results are shown in Table 1.
TABLE 1
Compared with cecropin A, the acetylated artificial polypeptide has more remarkable inhibition effect on pathogenic bacteria.
Test example 4 no significant inhibition of oral probiotics by acetylated artificial polypeptides
This test example tested the inhibitory effect of the acetylated artificial polypeptide of example 1 (sample set ①, action concentration 0.5 wt%) and cecropin a (sample set ②, action concentration 0.5 wt%) on 4 oral probiotics. The experimental method refers to a method for checking the antibacterial effect (suspension quantification method) of 7.3 antibacterial daily chemical products under the item QBT 2738-2012-evaluation method of the antibacterial effect of daily chemical products, and establishes a negative control group (sodium chloride solution, final concentration of 0.09 wt%) and a positive control group (cetylpyridinium chloride, final concentration of 0.1 wt%) for 2min. The measurement results are shown in Table 2.
TABLE 2
It can be seen that the acetylated artificial polypeptide of the present invention has no obvious inhibition effect on oral probiotics.
In conclusion, the non-hemolytic artificial polypeptide has the advantages of high titer and weak hemolysis, can selectively inhibit pathogenic bacteria, does not cause obvious harm to the growth of probiotics, can be used for preparing antibacterial preparations, such as preparations for preventing and treating pathogenic bacteria infectious diseases, and has good clinical transformation capacity and disease prevention capacity.
The above examples are preferred embodiments of the present invention, but the embodiments of the present invention are not limited to the above examples, and any other changes, modifications, substitutions, combinations, and simplifications that do not depart from the spirit and principle of the present invention should be made in the equivalent manner, and the embodiments are included in the protection scope of the present invention.
Claims (10)
1. The artificial polypeptide without hemolysis is characterized in that the sequence is shown as SEQ ID NO. 1.
2. A polypeptide obtained by acetylating the N-terminus of the polypeptide of claim 1.
3. An antibacterial peptide having a homology of 90% or more with the polypeptide of claim 1.
4. Use of the polypeptide of any one of claims 1-2 or the antimicrobial peptide of claim 3 in the preparation of an antimicrobial formulation.
5. The use according to claim 4, wherein the antibacterial agent is an agent against bacterial infection.
6. Use of the polypeptide of any one of claims 1-2 or the antimicrobial peptide of claim 3 in the preparation of an oral product.
7. The use according to claim 6, wherein the oral product has efficacy in preventing and treating oral diseases.
8. The use according to claim 7, wherein the oral disease is caused by infection with oral pathogenic bacteria.
9. The use according to claim 8, wherein the oral pathogenic bacteria is one or more of staphylococcus aureus, escherichia coli, actinobacillus actinomyces, fusobacterium nucleatum, porphyromonas gingivalis, candida albicans, streptococcus mutans, fosetyl, treponema denticola, actinomyces viscosus, or praecox intermedia.
10. An antibacterial agent comprising the polypeptide of any one of claims 1 to 2 or the antibacterial peptide of claim 3.
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