CN116731153B - Pig beta-interferon antibacterial peptide IFN7 and application thereof - Google Patents
Pig beta-interferon antibacterial peptide IFN7 and application thereof Download PDFInfo
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Classifications
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/34—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals
- A23L3/3454—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals in the form of liquids or solids
- A23L3/3463—Organic compounds; Microorganisms; Enzymes
- A23L3/3526—Organic compounds containing nitrogen
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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
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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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
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- 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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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Polymers & Plastics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
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- General Chemical & Material Sciences (AREA)
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- Veterinary Medicine (AREA)
- Oncology (AREA)
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- Communicable Diseases (AREA)
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Abstract
The invention discloses a pig beta-interferon antibiotic peptide IFN7, the amino acid sequence of which is YYLSILQYLK, and the molecular weight of the antibiotic peptide IFN7 is 1303.56Da. Experiments prove that the antibacterial peptide IFN7 provided by the invention can have a strong inhibition effect on escherichia coli and streptococcus B, can be used for preparing medicines and feed additives for treating or preventing diseases caused by escherichia coli and streptococcus B, and can also be used for preparing food preservatives.
Description
Technical Field
The invention relates to the technical field of biology, in particular to a pig beta-interferon antibacterial peptide IFN7 and application thereof.
Background
Coli is one of the important causes of death of nursing pigs and weaned pigs worldwide, is pathogenic bacteria of various pig diseases, can cause yellow diarrhea, white diarrhea and edema disease of piglets, and can cause septicemia, nerve symptoms and the like. Generally, during the epidemic period, due to the lack of passive protection, newborn piglet diarrhea caused by escherichia coli often occurs in 0-4 day old piglets. Streptococcus suis is an acute, high-heat zoonotic infectious disease caused by different groups of streptococcus. After infection of humans, this disease is mainly manifested by sepsis, meningitis, arthritis, and suppurative lymphadenitis. The epidemic characteristics of pigs after infection are that piglets mainly take the type of septicemia and meningitis, middle and big pigs mainly take the type of arthritis, and the pigs can be ill all the year round, spread rapidly and have high death rate.
The treatment of pig colibacillosis and streptococcosis is mainly carried out by antibiotics, but in recent years, the drug resistance to pig colibacillosis and streptococcosis is serious, the clinically isolated strain has stronger multi-resistance, and the original antibiotic medicine can not achieve the effect of killing pathogenic bacteria. The search for chemical drug alternatives is therefore also a major hotspot in current research. Antibacterial peptides (AMPs) refer to basic polypeptide substances with antibacterial activity, which are generated by induction in animals, and most of the active polypeptides have the characteristics of strong alkalinity, thermal stability, broad-spectrum antibacterial property and the like. Therefore, the antibacterial peptide is considered as a potential substitute of antibiotics, and has good application prospect in the fields of biological medicines, feed additives, food preservatives and the like.
Interferons are a class of glycoproteins, which have a high degree of species specificity and are responsible for protecting host cells from viral and bacterial infections. It has been found that interferon is susceptible to other factors during the bacteriostatic process, resulting in low bacteriostatic activity.
Therefore, the interferon antibacterial peptide which can effectively inhibit the infection of escherichia coli and streptococcus and has good stability is provided, and has important research significance.
Disclosure of Invention
The invention aims to overcome the defects of the prior art, provides a pig beta-interferon antibacterial peptide IFN7 and application thereof, and solves the problems in the prior art.
One of the technical schemes adopted for solving the technical problems is as follows: provides the pig beta-interferon antibiotic peptide IFN7. The amino acid sequence is YYLSILQYLK, such as SEQ ID NO:1.
The pig beta-interferon is used as a target to find the feasible theoretical basis of the antibacterial peptide in the sequence. Therefore, the pig beta-interferon is taken as a protein template, and chymotrypsin and trypsin are adopted to carry out simulated enzymolysis respectively, so as to obtain a polypeptide fragment sequence. Then, an APD3 online server is utilized to screen a pig beta-interferon protein sequence according to the charge property and the hydrophobicity of the antibacterial peptide, then a Swiss-model server is utilized to predict the structure of the pig beta-interferon antibacterial peptide, and an antibacterial peptide sequence YYLSILQYLK with strong antibacterial effect on escherichia coli and streptococcus b is found and named as IFN7.
The molecular weight of the antibacterial peptide IFN7 is 1303.56Da, the charge is +1, and the total hydrophobicity ratio is 40%.
The antibacterial peptide IFN7 can destroy bacteria from the following actions: in one aspect, the antimicrobial peptide IFN7 destroys bacterial cell membranes, alters bacterial cell membrane permeability, and inhibits cell membrane production, resulting in bacterial death; on the other hand, the antibacterial peptide IFN7 is combined with bacterial genome DNA to inhibit the synthesis of bacterial DNA, thereby leading to bacterial death.
The second technical scheme adopted by the invention for solving the technical problems is as follows: provides an application of a pig beta-interferon antibacterial peptide IFN7 in preparing an antibacterial medicament for inhibiting and/or killing one or more of escherichia coli and streptococcus B.
The third technical scheme adopted by the invention for solving the technical problems is as follows: an antibacterial drug is provided, the active ingredients of which comprise a pig beta-interferon antibacterial peptide IFN7, the amino acid sequence of the antibacterial peptide IFN7 is SEQ ID NO:1.
in a preferred embodiment of the present invention, the active ingredient of the antibacterial agent is a porcine β -interferon antibacterial peptide IFN7, and the amino acid sequence of the antibacterial peptide IFN7 is SEQ ID NO:1.
in a preferred embodiment of the present invention, the antimicrobial agent is used to inhibit and/or kill one or more of E.coli and Streptococcus B.
The fourth technical scheme adopted for solving the technical problems is as follows: the effective components of the feed additive comprise pig beta-interferon antibiotic peptide IFN7, and the amino acid sequence of the antibiotic peptide IFN7 is SEQ ID NO:1.
in a preferred embodiment of the present invention, the effective component of the feed additive is a porcine β -interferon antibiotic peptide IFN7, and the amino acid sequence of the antibiotic peptide IFN7 is SEQ ID NO:1.
in a preferred embodiment of the invention, the feed additive is used to inhibit and/or kill one or more of E.coli and S.B.
The fifth technical scheme adopted by the invention for solving the technical problems is as follows: providing a food preservative, wherein the effective component of the food preservative is pig beta-interferon antibacterial peptide IFN7, and the amino acid sequence of the antibacterial peptide IFN7 is SEQ ID NO:1.
in a preferred embodiment of the present invention, the food preservative is used to inhibit and/or kill one or more of E.coli and Streptococcus B.
The antimicrobial peptides of the invention can be synthesized using methods known to those skilled in the art, such as solid phase synthesis, and purified using methods known to those skilled in the art, such as high performance liquid chromatography.
The implementation of the invention has the following beneficial effects:
the invention takes pig beta-interferon as a research object, and discovers polypeptide IFN7 with a brand new amino acid sequence through screening. The antibacterial activity of IFN7 on Escherichia coli and Streptococcus B was studied. Experimental results show that the peptide has strong inhibition effect on escherichia coli and streptococcus B, and the antibacterial mechanism is that the bacterial cell membrane structure is firstly destroyed, the permeability of the cell membrane is changed, intracellular substances leak, and then the intracellular substances are combined with bacterial genome DNA to inhibit the synthesis of bacterial DNA, so that bacterial death is caused. The antibacterial peptide IFN7 can be used for preparing antibacterial drugs, feed additives and food preservatives.
Drawings
FIG. 1 is a schematic diagram of the structure of a predictive model of the antibacterial peptide IFN7 of the present invention.
FIG. 2 is a graph showing a control of the Minimum Inhibitory Concentration (MIC) measurement of the antibacterial peptide IFN7 of the present invention against Escherichia coli. Wherein,
a: antibacterial peptide concentration 0 μg/mL;
b: the concentration of the antibacterial peptide is 250 mug/mL;
c: the concentration of the antibacterial peptide is 125 mug/mL;
d: the concentration of the antibacterial peptide is 62.5 mug/mL;
e: the concentration of the antibacterial peptide is 31.25 mug/mL;
f: the concentration of the antibacterial peptide is 15.6 mug/mL.
FIG. 3 is a graph showing a control of the Minimum Inhibitory Concentration (MIC) assay of the antibacterial peptide IFN7 of the present invention against Streptococcus B. Wherein,
a: antibacterial peptide concentration 0 μg/mL;
b: the concentration of the antibacterial peptide is 250 mug/mL;
c: the concentration of the antibacterial peptide is 125 mug/mL;
d: the concentration of the antibacterial peptide is 62.5 mug/mL;
e: the concentration of the antibacterial peptide is 31.25 mug/mL;
f: the concentration of the antibacterial peptide is 15.6 mug/mL.
FIG. 4 is a graph showing the Time-kill curve (Time kill) of the antibacterial peptide IFN7 of the present invention against E.coli. Diluted to 10 in 0.01M pH 7.2 phosphate buffer 4-5 CFU/mL. The concentration of the antibacterial peptide is 31.25 mug/mL.
FIG. 5 is a graph showing the Time-kill curve (Time kill) of the antibacterial peptide IFN7 of the present invention against Streptococcus B. Diluted to 10 in 0.01M pH 7.2 phosphate buffer 4-5 CFU/mL. The concentration of the antibacterial peptide is 31.25 mug/mL.
FIG. 6 is a transmission electron microscope image of the antibacterial peptide IFN7 of the invention and E.coli, wherein A is E.coli blank; b is the escherichia coli group treated by the antibacterial peptide IFN7.
FIG. 7 is an electrophoresis diagram of the binding of IFN7, an antibacterial peptide of the invention, to E.coli DNA, wherein, band 5: blank control; lanes 1-4: the IFN7 to DNA mass ratios were 25/4, 25/2, 25/1, 50/1, respectively.
FIG. 8 is a fluorescence spectrum of the antibacterial peptide IFN7 of the present invention competitively binding to E.coli DNA. The concentration of the antibacterial peptide is 15.6 mug/mL, 31.3 mug/mL and 62.5 mug/mL.
FIG. 9 is a graph showing the measurement of leakage of reducing sugar in E.coli cell membranes by IFN7, an antibacterial peptide of the present invention. The concentration of the antibacterial peptide was 31.25. Mu.g/mL, 62.5. Mu.g/mL.
FIG. 10 is a graph showing the measurement of nucleic acid leakage from the cell membrane of E.coli by IFN7, an antibacterial peptide of the present invention. The concentration of the antimicrobial peptide was 31.25. Mu.g/mL, 62.5. Mu.g/mL, 125. Mu.g/mL.
FIG. 11 is a graph showing the measurement of protein leakage in E.coli cell membrane by IFN7, an antibacterial peptide of the present invention. The concentration of the antimicrobial peptide was 31.25. Mu.g/mL, 62.5. Mu.g/mL, 125. Mu.g/mL.
Detailed Description
For a better understanding of the present invention, reference will now be made in detail to the following examples and accompanying drawings, which are included to provide a further understanding of the invention, and it is to be understood by those skilled in the art that the following examples are not intended to limit the scope of the invention.
The experimental methods used in the following examples are conventional methods unless otherwise specified.
Materials, reagents and the like used in the examples described below are commercially available unless otherwise specified.
Example 1: screening of porcine beta-interferon antibacterial peptides
The required protein sequence of the pig beta-interferon is obtained at a National Center for Biotechnology Information website, chymotrypsin and trypsin are simulated and digested and enzymolyzed on the beta-interferon by utilizing online software Expasy, the calculation of the hydrophobicity and charge number is carried out by combining online software APD3, so that the antibacterial efficacy of the peptide is evaluated, and the peptide sequence of the beta-interferon is screened. Then, the structure of the pig beta-interferon antibiotic peptide IFN7 is predicted by a Swiss-model server, and is edited and modified by using Pymol software to obtain the secondary structure of the antibiotic peptide IFN7, as shown in figure 1.
Example 2: determination of Minimum Inhibitory Concentration (MIC) of the antibacterial peptide IFN7
Culturing Escherichia coli and Streptococcus B at 37deg.C for 12h to logarithmic phase, respectively, and diluting to 10 in 0.01M pH 7.2 phosphate buffer 4-5 CFU/mL. The antibacterial peptide IFN7 was dissolved in phosphate buffer, mixed with bacteria in equal volume at 37℃and cultured 2 h. The Minimum Inhibitory Concentration (MIC) refers to the minimum concentration of antimicrobial peptide that inhibits bacterial growth after overnight incubation at 37 ℃. As shown in FIGS. 2 and 3, IFN7 has a Minimum Inhibitory Concentration (MIC) of 31.25 μg/mL for E.coli and Streptococcus B.
Example 3: determination of Time-Kill Curve (Time-Kill Curve) of the antibacterial peptide IFN7
The time-sterilization curve of the antimicrobial peptide IFN7 was determined using plate colony counting. Culturing Escherichia coli and Streptococcus B preserved at-20deg.C at 37deg.C for 12h to logarithmic phase, and diluting to 10 in 0.01M pH 7.2 phosphate buffer 4 -5 CFU/mL. The antibacterial peptide IFN7 is dissolved in phosphate buffer, diluted to 62.5 mug/mL and 125 mug/mL, respectively mixed with bacteria liquid in equal volume, and incubated at constant temperature of 37 ℃. At different points in time (i.e0.5, 1, 1.5, 2, 2.5 and 3 h) 20. Mu.L of the bacterial suspension was spread evenly on a nutrient broth plate and colonies were counted after incubation at 37℃for 24 h. As shown in fig. 4 and 5, the antibacterial peptide IFN7 has an obvious killing effect on escherichia coli and streptococcus b for about 4 hours, and the bacteria do not grow and reproduce any more as the action time increases.
Example 4: transmission electron microscope observation of antibiotic peptide IFN7 on colibacillus
500 mu L of a logarithmic growth phase E.coli bacterial liquid was added to an equal volume of the antibacterial peptide IFN7 (final concentration 62.5. Mu.g/mL) and incubated at 37℃for 2 h. After the completion of the culture, the cells were centrifuged at 2700 and g for 2 min, and the cell pellet was collected and washed 3 times with PBS. 12h was fixed using 2.5% glutaraldehyde. Dehydrated with ethanol (30% -100%), treated with acetone for 20 min, and the samples were 24-h at 70 ℃ to prepare 70-90 nm flakes, which were observed after staining with lead citrate and uranium acetate. As shown in FIG. 6, the cell membrane of the Escherichia coli in the blank group is complete, the limit is clear, the boundary of the cell membrane of the bacteria of the antibacterial peptide IFN7 group is fuzzy, the cytoplasmic density is reduced, and the condition of membrane wall separation appears, so that the antibacterial peptide IFN7 has a certain destructive effect on the cell membrane of the Escherichia coli, thereby affecting the normal growth of bacteria.
Example 5: interaction of the antibacterial peptide IFN7 with bacterial DNA
The interaction of the antibacterial peptide IFN7 with the genomic DNA of E.coli was studied using a DNA gel blocking method. E.coli was cultured in 50mL of Nutrient Broth (NB) at 37℃for 12 hours, bacterial genomic DNA was extracted with a bacterial genomic DNA extraction kit, the concentration of the extracted DNA was measured using an ultra-micro spectrophotometer, and the ratio of Optical Densities (OD) at 260 nm and 280 nm was measured 260 /OD 280 1.9) judging the purity of the extracted DNA. Next, 10. Mu.L of DNA (198 ng/. Mu.L) was mixed with the antibacterial peptides IFN7 in a mass ratio of 25/4, 25/2, 25/1, 50/1 at 25℃for 90 minutes, and the mixture was subjected to electrophoresis on a 0.8% agarose gel. The DNA gel changes were observed under uv irradiation using a GelDocXR gel imaging system (Bio-Rad, usa), as shown in fig. 7. As the concentration of the antibacterial peptide IFN7 increases, the brightness of the DNA band is obviously reduced, which indicates that the antibacterial peptide IFN7 participates in the large intestineDegradation of bacillus DNA and its binding proteins.
Example 6: fluorescent spectroscopic experiment of the antibacterial peptide IFN7 competitive binding to DNA
By measuring the change of the fluorescence spectrum of the action of the DNA-EB complex system and the competitor (the antibacterial peptide IFN 7), whether the antibacterial peptide IFN7 is combined with DNA by the intercalation mode like EB or not is judged. First, the prepared bacterial cell DNA was diluted to 50. Mu.g/mL with 1 XTE buffer. Then, 5. Mu.L of DNA solution and 10. Mu.L of 100. Mu.g/mL Ethidium Bromide (EB) solution were added to each well of the 96-well plate, and the mixture was incubated at 37℃for 10 minutes in the absence of light. Next, 50. Mu.L of the antibiotic peptide IFN7 was added at different concentrations to give final antibiotic peptide IFN7 concentrations of 15.6. Mu.g/mL, 31.25. Mu.g/mL, 62.5. Mu.g/mL, respectively, and 50. Mu.L of 0.01M PBS (pH 7.2) was used as a control. After mixing, placing the mixture in a biochemical incubator at 37 ℃ for incubation for 30 min in a dark place, and after incubation, measuring the fluorescence spectrum of the sample in the range of excitation wavelength 535 nm and emission wavelength 570 nm-710 nm by using a multifunctional enzyme-labeled instrument. As is clear from FIG. 8, the fluorescence intensity of the EB-DNA complex decreased with increasing concentration of the antibacterial peptide IFN7, indicating that the antibacterial peptide IFN7 replaces EB previously bound to DNA base pairs with intercalation, resulting in a decrease in the fluorescence intensity of the whole system.
Example 7: effect of the antibacterial peptide IFN7 on leakage of intracellular components of bacteria
Coli was inoculated into 20mL of Nutrient Broth (NB) at 37 ℃ and grown to log phase for 12 h. The centrifuged cells were washed three times with 0.1M PBS and then adjusted to a concentration of 10 4-5 CFU/mL. The antibacterial peptide IFN7 is dissolved in 0.1M PBS to make the concentration of the antibacterial peptide IFN7 be 31.25 mug/mL and 62.5 mug/mL, a blank control group is replaced by 0.1M PBS, the antibacterial peptide IFN7 is mixed with bacteria for incubation and culture at the equal volume of 37 ℃, 100 mu L of bacteria liquid is respectively taken out after 0, 30, 60 and 90 min of culture, supernatant is obtained by centrifugation, absorbance at 540 and nm is measured by a multifunctional enzyme-labeled instrument by a DNS colorimetry method, and the absorbance is compared with a glucose standard curve. As can be seen from fig. 9, the content of reducing sugar in the escherichia coli bacterial liquid of the blank group is low, the amount of reducing sugar exudation in the bacterial liquid of the antimicrobial peptide IFN7 treatment group is obviously increased, and the amount of reducing sugar exudation is also increased along with the increase of the concentration of the antimicrobial peptide IFN7.
Coli was inoculated into 20mL Nutrient Broth (NB) and grown to log phase for 12 h. The centrifuged cells were washed three times with 0.1M PBS and then adjusted to a concentration of 10 4-5 CFU/mL. The antibacterial peptide IFN7 is dissolved in 0.1M PBS to make the concentration of the antibacterial peptide IFN7 be 31.25 mug/mL, 62.5 mug/mL and 125 mug/mL, a blank control group is replaced by 0.1M PBS, the antibacterial peptide IFN7 is mixed with bacteria in equal volume, and absorbance at different time points at 260 nm and 280 nm is measured by a multifunctional enzyme-labeling instrument, so that the exudation amount of nucleic acid and protein of the bacteria is calculated. As can be seen from fig. 10 and 11, the content of nucleic acid and protein in the blank escherichia coli bacterial solution is low, but the exudation amount of nucleic acid and protein in the antimicrobial peptide IFN7 treated bacterial solution is obviously increased, and the penetration amount of nucleic acid and protein in the bacterial solution is increased along with the increase of the concentration of the antimicrobial peptide IFN7, and after 60 min, the penetration amount of nucleic acid and protein in the antimicrobial peptide IFN7 treated bacterial solution is basically unchanged.
In conclusion, the invention provides a brand new antimicrobial peptide IFN7, which has the minimum inhibitory concentration MIC of 31.25 mug/mL for escherichia coli and streptococcus B, and can inhibit the growth of the escherichia coli and the streptococcus B. The antibacterial peptide IFN7 firstly penetrates through the cell membrane of bacteria to reduce the cytoplasmic density and separate the membrane wall, and then is combined with bacterial genome DNA to inhibit the synthesis of the bacterial DNA, thereby leading to bacterial death. Therefore, the antibacterial peptide IFN7 can be used for preparing antibacterial drugs, feed additives or food preservatives.
While specific embodiments of the invention have been described above, it will be appreciated by those skilled in the art that the specific embodiments described are illustrative only and not intended to limit the scope of the invention, and that equivalent modifications and variations of the invention in light of the spirit of the invention will be covered by the claims of the present invention.
Claims (9)
1. A pig beta-interferon antibiotic peptide IFN7, the amino acid sequence of which is shown in SEQ ID NO:1.
2. The use of the porcine β -interferon antimicrobial peptide IFN7 of claim 1 for the manufacture of an antimicrobial medicament, wherein: the antibacterial drug is used for inhibiting and/or killing one or more of escherichia coli and streptococcus B.
3. An antibacterial agent characterized in that: the active ingredients of the anti-bacterial peptide comprise pig beta-interferon anti-bacterial peptide IFN7, and the amino acid sequence of the anti-bacterial peptide IFN7 is SEQ ID NO:1.
4. an antimicrobial agent as claimed in claim 3 wherein: the active ingredient of the polypeptide is pig beta-interferon antibiotic peptide IFN7, and the amino acid sequence of the antibiotic peptide IFN7 is SEQ ID NO:1.
5. a feed additive, characterized in that: the active ingredients of the anti-bacterial peptide comprise pig beta-interferon anti-bacterial peptide IFN7, and the amino acid sequence of the anti-bacterial peptide IFN7 is SEQ ID NO:1.
6. the feed additive of claim 5, wherein: the active ingredient of the polypeptide is pig beta-interferon antibiotic peptide IFN7, and the amino acid sequence of the antibiotic peptide IFN7 is SEQ ID NO:1.
7. the feed additive according to any one of claims 5 or 6, wherein: the feed additive is used for inhibiting and/or killing one or more of escherichia coli and streptococcus B.
8. A food preservative characterized by: the active ingredient of the polypeptide is pig beta-interferon antibiotic peptide IFN7, and the amino acid sequence of the antibiotic peptide IFN7 is SEQ ID NO:1.
9. a food preservative as claimed in claim 8, wherein: the food preservative is used for inhibiting and/or killing one or more of escherichia coli and streptococcus B.
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| CN110357971A (en) * | 2019-08-21 | 2019-10-22 | 中国科学院微生物研究所 | It is a kind of for promptly preventing the pig Interferon Alfacon-1 of African swine fever |
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