CN107446032A - A kind of antibacterial peptide and its application - Google Patents
A kind of antibacterial peptide and its application Download PDFInfo
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- CN107446032A CN107446032A CN201710533310.3A CN201710533310A CN107446032A CN 107446032 A CN107446032 A CN 107446032A CN 201710533310 A CN201710533310 A CN 201710533310A CN 107446032 A CN107446032 A CN 107446032A
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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
- C07K14/43509—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from crustaceans
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- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
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Abstract
The invention discloses a kind of antibacterial peptide, its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.The present invention discloses a kind of application of antibacterial peptide in the medicine for treating or preventing bacterium is prepared.The bacterium is Vibrio flurialis, vibrio alginolyticus, Escherichia coli, Aeromonas hydrophila, vibrio parahaemolytious, beta streptococcus or staphylococcus aureus.The invention also discloses a kind of application of antibacterial peptide in antineoplastic.The present invention lays a good foundation for further exploitation with bacteriostatic activity, the biological products of antitumor activity.
Description
Technical field
The present invention relates to the technical field of molecular biology, more particularly to a kind of antibacterial peptide and its application.
Background technology
Environment of Litopenaeus vannamei Low (Litopenaeus vannamei), also known as be Penaeus Vannmei (Penaeus vannamei
Boone), Arthropoda, Crustachia, Decapoda, swimming suborder, Penaeidae, shore Penaeus are under the jurisdiction of on taxology, is originated in
South America Pacific coast waters.Environment of Litopenaeus vannamei Low due to the speed of growth it is fast, require food low, environment-adapting ability is strong,
The features such as suitable dense stocking, per unit area yield height, delicious meat, have become and cultivate shrimp species greatly after the world three of Chinese prawn, Penaeus monodon
One of.Although Environment of Litopenaeus vannamei Low yield increases year by year, industrialization, the highly dense of Environment of Litopenaeus vannamei Low cultivation are accompanied by,
The problem of Environment of Litopenaeus vannamei Low cultivates also continuously emerges, and breeding environment deteriorates the generation for having triggered various diseases, and Environment of Litopenaeus vannamei Low resists
Sick ability declines, and causes large-scale death, causes huge ecology and economic loss.
With marine drug progress of research, there is the very abundant antibacterial peptide of species to be sent out in the aquatile of ocean
Existing, wherein the shrimps in first gram animal and crab class are it has also been found that many antibacterial peptides.Studies have shown that adds in the breeding process of prawn
Antibacterial protein, prawn growth rate, body weight increase rate, feed coefficient, survival rate and resistance against diseases etc. can be obviously improved.
Research shows that antibacterial peptide can prevent and treat shrimp disease, and contains antibacterial peptide in Environment of Litopenaeus vannamei Low blood, therefore point
From obtaining, preventing and treating of the antibacterial peptide to shrimp disease is significant.In view of this, the present inventor studies and devised a kind of antibacterial
Thus peptide and its application, this case produce.
The content of the invention
It is an object of the invention to provide a kind of antibacterial peptide and its application, is that further exploitation has bacteriostatic activity, resists and swell
The biological products of tumor activity lay the foundation.
In order to solve above-mentioned purpose, the technical solution adopted by the present invention is as follows：
A kind of antibacterial peptide, its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.
A kind of application of antibacterial peptide, the application in the medicine for treating or preventing bacterium is prepared.
As the preferred embodiment of embodiment, the bacterium is Vibrio flurialis, vibrio alginolyticus, Escherichia coli, thermophilic aqueous vapor unit cell
Bacterium, vibrio parahaemolytious, beta streptococcus or staphylococcus aureus.
A kind of application of antibacterial peptide, the application in antineoplastic.
Because present invention employs above-mentioned technical scheme so that the invention has the advantages that：Present invention separation
Obtained antibacterial peptide is laid a good foundation for further exploitation with bacteriostatic activity, the biological products of antitumor activity.
Brief description of the drawings
Fig. 1 is below molecular weight 3000KD of the present invention prawn plasma mass spectrometry figure；
Fig. 2 ESEM result figures；Wherein, (A) vibrio parahaemolytious blank control；(B) beta streptococcus blank control；
(C) scanning electron microscope (SEM) photograph of the vibrio parahaemolytious after polypeptide VLGDHS processing；(D) beta streptococcus is after polypeptide VLGDHS processing
Scanning electron microscope (SEM) photograph.
Embodiment
Embodiment 1
A kind of antibacterial peptide, its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.
Embodiment 2
The identification of 2.1 Environment of Litopenaeus vannamei Low degradation fragments
The Environment of Litopenaeus vannamei Low blood plasma ultrafiltration stimulated by vibrio parahaemolytious is obtained into the component below molecular weight 3000KD, carried out
Mass Spectrometric Identification, obtain mass spectrogram, such as Fig. 1.
Above-mentioned Mass Spectrometric Identification result is analyzed, Crustachia is searched and has identified 6 peptides altogether.Respectively：VLGDHS、
TVTAMDVVYALK, DSTALPD, TNPPRPA, AGPPP and PEDKPGPA.It neutralizes the relevant peptide of Environment of Litopenaeus vannamei Low：
VLGDHS, β -1 from Environment of Litopenaeus vannamei Low, 3- glucan-binding protein degradation fragment.Then website http is passed through://
Www.ncbi.nlm.nih.gov/ can inquire β -1 of Environment of Litopenaeus vannamei Low, the amino acid sequence of 3- glucan-binding proteins,
It is as shown in table 1 below：
The protein-bonded primary structure of beta-1,3-dextran of the Environment of Litopenaeus vannamei Low of table 1
β -1,3- the Portugals that the degradation fragment VLGDHS that Mass Spectrometric Identification obtains as shown in Table 1 is actually from Environment of Litopenaeus vannamei Low gather
Carbohydrate-binding protein.
2.2 bacteriostatic activity
2.2.1 experiment material
Experiment polypeptide used is its purity ＞ 95% as synthesized by BeiJing ZhongKe Yaguang Biology Science Co., Ltd.
Experimental water production pathogenic bacteria are respectively Vibrio flurialis, vibrio alginolyticus, Escherichia coli, Aeromonas hydrophila, secondary haemolysis
Vibrios, beta streptococcus and staphylococcus aureus, it is that this laboratory preserves strain.
2.2.2 main agents
Ox tryptone, beef extract, agar powder (being purchased from Huankai Microbes Tech Co., Ltd., Guangdong)；Sodium chloride, hydrogen
Sodium oxide molybdena (is purchased from Xilong Chemical Co., Ltd)；Plate count agar is (public purchased from Beijing overpass technology Limited Liability
Department).
2.2.3 solution is prepared
2.2.3.1 artificial synthetic polypeptide solution
1.0mg/mL polypeptide solution：Lyophilized powder polypeptide is taken out from -20 DEG C of refrigerators, is placed under room temperature condition and balances
1h, then add the dissolving of 1mL sterilized waters and be well mixed, -20 DEG C of packing save backup.
2.2.3.2 culture medium
The formula of broth bouillon (liquid)：Peptone 10g, beef extract 5g, NaCl 5g plus distilled water 800mL, use 5M
PH is adjusted to 7.2 by NaOH, is settled to 1000mL, 121 DEG C of autoclaving 20-30min, room temperature preservation.
The formula of broth bouillon (solid)：23.5g plate count agars are weighed, add 1000mL distilled water, heating is boiled
Boiling is to being completely dissolved, then at 121 DEG C of autoclaving 20-30min, be cooled to 46 DEG C or so it is standby.
2.2.4 experimental method
The fragment VLGDHS of Environment of Litopenaeus vannamei Low bacteriostatic activity checking is with reference to Qiao Jie[15]Study the prawn hemocyanin of report
Chemical synthesis antibacterial peptide bacteriostatic activity verification method is carried out, and idiographic flow is as follows：
(1) first seven kinds of pathogenic bacteria (Vibrio flurialis, vibrio alginolyticus, Escherichia coli, the thermophilic water preserved under the conditions of -80 DEG C
Aeromonas, staphylococcus aureus, vibrio parahaemolytious, beta streptococcus) be placed in 4 DEG C of dissolvings after further take out balance to room temperature,
Then (the μ L strains of 1mL meat soups fluid nutrient medium+50), the constant-temperature table culture 18h under the conditions of 30 DEG C are activated in a small amount respectively
To exponential phase；
(2) then, the bacterium solution activated is inoculated into meat soup solid slope culture medium, 30 DEG C of constant-temperature table culture 18h
Afterwards, then it is diluted to suitable concentration with lawn under the sterile washings of 3mL；
(3) take the μ L of bacterium solution 10 after dilution to be well mixed with the μ L of polypeptide sample liquid 10 of 1.0mg/mL different components, then be placed on
2h is incubated in 30 DEG C of thermostat water baths, 10 μ L mixed liquors is then taken out and applies flat board, every group is 2 parallel, 30 DEG C of inversion culture 12-
Bacterium colony is counted after 24h and is taken pictures.Negative control is sterilized water；
(4) bacteriostasis rate is calculated according to below equation：
(5) concentration of polypeptide sample liquid is halved successively in the range of 1.0-0.001mg/mL, remaining step is same (3), then
Calculate bacteriostasis rate.
2.2.5 interpretation of result
Bacteriostasis rates (%) of the polypeptide VLGDHS of table 2 to seven kinds of pathogenic bacteria
Can be obtained by table 2, polypeptide VLGDHS to vibrio parahaemolytious, beta streptococcus the two bacterium bacteriostasis rate with more
The increase of peptide VLGDHS concentration and increase, illustrate polypeptide VLGDHS have to both bacterium bacteriostasis and this bacteriostasis with it is more
Peptide VLGDHS concentration is relevant.Staphylococcus aureus, the fungistatic effect figure of vibrio alginolyticus and upper table are pressed down from polypeptide VLGDHS
Rate processed understands that it is to staphylococcus aureus and vibrio alginolyticus without bacteriostasis.It is in addition, several to remaining from polypeptide VLGDHS
The bacteriostasis rate and fungistatic effect figure of bacterium are understood, although regularity is not presented in its inhibiting rate, still can illustrate polypeptide
VLGDHS has bacteriostasis to this several bacterium.
2.3 antitumor action
2.3.1 experiment material
Instrument：THERMO types CO2gas incubator, SM600 ELIASAs, the double one side of SW-CJ-2D types vertically purify work
Make platform, DSZ2000X type inverted phase contrast microscopes etc..
Consumptive material：Culture dish, 96 orifice plates etc..
Reagent：PBS(NaCl 8g、KCl 0.2g、Na2HPO4 1.44g、KH2PO40.24g, adjust pH 7.4)；MTT, two
Methyl sulfoxide, cis-platinum, cell culture fluid, 1640 culture mediums, glutaraldehyde, ethanol etc..
2.3.2 solution is prepared
MTT：Concentration is 5mg/mL.MTT 0.1g are weighed, are dissolved in 0.22 μm of filter membrane mistake of 20mL phosphate buffer (PBS)
Filter removes the bacterium in solution, is subsequently placed in 4 DEG C and is kept in dark place, and the term of validity is two weeks, can also be configured to 5mg/mL
Be placed in it is -20 DEG C long-term preserve, multigelation is prevented during preservation, low dose packing is optimal, also with lucifuge bag or
It is that black paper bag lives lucifuge to prevent its decomposition.
2.3.3 experimental method
The method of checking Environment of Litopenaeus vannamei Low fragment VLGDHS antitumor action is mtt assay, also known as MTT colorimetric methods, its
The growth and survival of cell can be examined.MTT is the Thiazolyl blue of yellow, and it is intracellular that it can pass through cell membrane to enter.External source MTT
The amber dehydrogenase in living cells mitochondria can be present in be reduced into bluish violet crystallization first a ceremonial jade-ladle, used in libation not soluble in water and be deposited in
In cell, and dead cell is without such function.And the first a ceremonial jade-ladle, used in libation in cell can be dissolved by dimethyl sulfoxide (DMSO), therefore use
Enzyme-linked immunosorbent assay instrument is in the absorption value of OD490nm (570nm) place measure first a ceremonial jade-ladle, used in libation, in the range of certain cell number, MTT crystallizations
Growing amount and cell number positive correlation.Based on this principle, VLGDHS antitumor activity, idiographic flow are verified using mtt assay
It is as follows：
(1) cell in logarithmic phase is collected, adjusts the concentration of cell suspension, the μ L of cell suspension 100, bed board are added per hole
Cell to be measured is set to adjust density to 1000-10000 holes, (being filled positioned at the hole at edge with sterile PBS).
(2) 5%CO2,37 DEG C of incubations, to cell attachment, add concentration gradient (concentration is respectively 500,250,125,
62.5, unit μ g/mL) Environment of Litopenaeus vannamei Low degradation fragment VLGDHS, per the μ L of hole 100.
(3) 5%CO2,37 DEG C are incubated 24-72 hours, are observed under inverted microscope.
(4) 20 μ L MTT solution (5mg/mL, i.e. 0.5%MTT) are added per hole, continue to cultivate 4h.If the degradation fragment
It can be reacted with MTT, then discard nutrient solution after can first centrifuging again, carefully rinse 2-3 after with PBS, then added and contain
There is MTT nutrient solution.
(5) stop culture, carefully suck the cell culture fluid in hole.
(6) 150 μ L dimethyl sulfoxide (DMSO)s are added per hole, are then placed in shaking table low-speed oscillation 10min, crystal is fully molten
Solution.The light absorption value in each hole is measured at enzyme-linked immunosorbent assay instrument OD490nm (570nm) place.
(7) while zeroing hole i.e. blank group (culture medium, MTT, dimethyl sulfoxide (DMSO)), control wells (cell and VLGDHS be set
Cis-platinum, nutrient solution, MTT, the dimethyl sulfoxide (DMSO) of same concentrations)
2.3.4 interpretation of result
The polypeptide VLGDHS of table 3 is to Human normal hepatocyte and the inhibiting rate of Bel7402
Note：LO2 in form is Human normal hepatocyte, and HepG2 is then Bel7402.
Table 3 be when peptide concentration VLGDHS is respectively 62.5 μ g/mL, 125 μ g/mL, 250 μ g/mL, 500 μ g/mL to people just
Normal liver cell and the inhibiting rate of Bel7402.Concentration is that 500 μ g/mL cisplatin medicine is control group in table, its to people just
The inhibiting rate of normal liver cell and Bel7402 are all higher than 1, and the polypeptide VLGDHS solution that concentration is 500 μ g/mL to people just
The inhibiting rate of normal liver cell only has 0.085, and this shows that polypeptide VLGDHS does not have inhibitory action, side reflection to Human normal hepatocyte
It to Human normal hepatocyte does not have toxic action；Concentration is 500 μ g/mL polypeptide VLGDHS solution to Bel7402's
Inhibiting rate is 0.28, illustrates that it has faint inhibitory action to Bel7402.
The antimicrobial mechanism of 2.4 scanning electron microscopic observation Environment of Litopenaeus vannamei Low fragments
2.4.1 experiment material
Instrument：JSM-6360LA analysis scanning electronic microscopes, the Ultrasonic Cell Disruptors of BILON92- II, desk-top 100 degree of MOMA
Baking oven, H1650-W high speed centrifugal machine for minim.
Equipment：Culture dish, cover glass, tweezers, sterilized round-bottomed flask, liquid-transfering gun etc..
Reagent：0.2M PBS, 2.5% glutaraldehyde, gradient elution alcohol (30%, 50%, 70%, 85%, 95%,
100%), sterilized water, absolute ethyl alcohol, LB culture mediums.
2.4.2 solution is prepared
(1) 0.2M PBS solutions (pH 7.4) are prepared：2.6 grams of sodium dihydrogen phosphate, 29 grams of double distilled waters of disodium hydrogen phosphate add
To 500 milliliters.
The preparation of (2) 2.5% glutaraldehydes：By 25% glutaraldehyde：Sterilized water：0.2M PBS solution=1：4：5 prepare.
(3) gradient elution alcohol：Prepare 30%, 50%, 70%, 85%, 95%, 100% alcohol, sterilized water dilution.
(4) LB culture mediums：Tryptone 10g/L, yeast extract 5g/L, sodium chloride 10g/L, add deionized water
950mL, shakes container to solute and dissolves, and pH is adjusted to 7.0 with NaOH solution, then is settled to 1L, in 121 DEG C of autoclaving 20-
30min, room temperature preservation.
2.4.3 experimental method
(1) the slide processing before testing：Cover glass is converted into 1 × 1cm blockage, then with 2%HCL soaked overnights,
Rinsed several times with absolute ethyl alcohol within second day, then 30min (300W, 3s ultrasound 3s pauses) is handled with ultrasonication, then cleaning
Cover glass take out, be placed on grid iron net or small beaker (so that when taking-up with tweezers will not sticky end), be subsequently placed in 65 DEG C
It is dried for standby in baking oven.
(2) bacterial treatment and fixation：Strain (beta streptococcus, vibrio parahaemolytious) is taken, 50 μ L are inoculated with after thawing in 4mLLB
In culture medium, 37 DEG C of shaking table culture 12h, the bacterium solution shaken takes 300 μ L shaking table culture 4h in 4mL LB culture mediums.Then take out
1mL spreads cultivation to the bacterium solution of logarithmic phase, 8000rpm room temperatures centrifugation 1min, takes out 850 μ L culture mediums, adds 150 μ L polypeptide solutions
(being VLGDHS) after-blow is even, (blank group adds equivalent LB culture mediums), 37 DEG C of incubation half an hour.8000rpm room temperatures centrifuge again
1min, abandons supernatant, adds 2.5% glutaraldehyde solution, blow it is even after, it is fixed overnight in 4 DEG C.
(3) Gradient elution using ethanol：8000rpm centrifuges 1min after fixation, removes supernatant, is cleaned with 0.2M PBS solutions
4th, five times, 10000rpm centrifuges 1min again after washing every time, is taken off by 30%, 50%, 70%, 85%, 95% order gradient
Water, 15min, 10000rpm centrifugation 1min are stood after adding every time, it is, quiet after addition every time finally ethanol wash with 100% twice
Put 15min, 10000rpm centrifugations 1min.Finally, the absolute ethyl alcohol resuspension with 300~400 μ L is stand-by.
(4) a big and clean culture dish is chosen, double faced adhesive tape is sticked on culture dish and carries out mark, uses tweezers
Careful gripping cover glass, clinging the small angle of double faced adhesive tape (can play fixation, not glue too much, be otherwise bad to take piece), and general one
Individual three cover glasses of preparation of samples are standby, and then the μ L of resuspended bacterium solution 6~8 obtained by aspiration step (3), are added dropwise in dried glass
Piece surface, is then sealed with preservative film, is put into 65 DEG C of oven drying 24h (every group is done three Duplicate Samples).
(5) electron-microscope scanning is observed.
2.4.4 interpretation of result
It in voltage is 10kV that Fig. 2, which is, and multiplication factor is respectively the SEM result under 5000 times and 12000 times
Figure.The normal cell form of vibrio parahaemolytious is can be seen that by Fig. 2 (A), its cell is in shaft-like, and some is in slight curvature arcuation；By
For Fig. 2 (B) it can be seen that the normal cell form of beta streptococcus, its cell is in oval, single, paired or chaining arrangement.
(C), (D) two figure is respectively the scanning result figure of vibrio parahaemolytious and beta streptococcus under polypeptide VLGDHS processing, with compareing
Group is compared, and cell becomes coarse, rupture.
From the point of view of polypeptide VLGDHS primary structure, valine and leucine are thin in composition polypeptide VLGDHS amino acid
Water-based amino acid, and aspartic acid, histidine and serine are then hydrophilic amino acid, it can thus be appreciated that the polypeptide is amphipathic
Peptide.The polypeptide positively charged is understood from the powered situation of these amino acid again, and charge number is 1.Therefore, polypeptide VLGDHS can be with
Electrostatic adsorption occurs for the negative electrical charge on the phospholipid molecule on bacterial cell membrane, is closely adhered on plasma membrane, is then dredged
Water end (W.E.) is inserted into cell membrane, and then whole molecular drag is entered in bacterial cell, causes cellular content to be lost in, bacterium is dead
Die.
When causing it to act on vibrio parahaemolytious and beta streptococcus just because of the structures of polypeptide VLGDHS in itself, this two
The cell of kind bacterium becomes coarse, rupture.
The present invention mainly studies Environment of Litopenaeus vannamei Low fragment VLGDHS immunocompetence in terms of three.First, pressed down
Bacterium activity confirmatory experiment, detect its seven kinds are caused a disease it is (Vibrio flurialis, vibrio alginolyticus, Escherichia coli, Aeromonas hydrophila, golden yellow
Color staphylococcus, vibrio parahaemolytious, beta streptococcus) whether there is bacteriostasis.Found by bacteriostatic experiment, Environment of Litopenaeus vannamei Low piece
Section to staphylococcus aureus and vibrio alginolyticus without effect, to Vibrio flurialis, Escherichia coli Aeromonas hydrophila, vibrio parahaemolytious
All there is bacteriostasis with beta streptococcus.Secondly, using MTT colorimetric determinations, whether it has antitumor action, experiment knot
Fruit shows that it is not acted on Human normal hepatocyte, illustrates that it does not have toxic action to human normal cell line；But it is thin to human liver cancer
Born of the same parents system but has faint effect.Finally, using scanning electron microscopic observation its to vibrio parahaemolytious and the immunologic mechanism of beta streptococcus,
Test result indicates that by polypeptide VLGDHS processing, the cell of vibrio parahaemolytious and beta streptococcus is compared with control group,
Become coarse, start to rupture, thus phenomenon consults related data, and it is probably to Gram-negative bacteria and gram sun to find it
Property bacterium cell membrane produce electrostatic adsorption, then destroy bacterium cell.
In summary, result of the invention is to furtheing elucidate the immune factor such as β -1,3- glucan-binding proteins in prawn
Effect played in immunologic mechanism is significant.Meanwhile provided more to seek the preventions of shrimp disease
Theoretical foundation, be advantageous to the sustainable development of China's shrimp culture industry.
It is described above, only present pre-ferred embodiments, therefore the scope that the present invention is implemented can not be limited successively, i.e., according to
The equivalent changes and modifications that the scope of the claims of the present invention and description are made, all should still it belong in the range of the present invention covers.
Claims (4)
- A kind of 1. antibacterial peptide, it is characterised in that：Its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.
- A kind of 2. application of antibacterial peptide as claimed in claim 1, it is characterised in that：Preparing the medicine for the treatment of or prevention bacterium In application.
- A kind of 3. application of antibacterial peptide as claimed in claim 2, it is characterised in that：The bacterium is Vibrio flurialis, molten alginic acid arc Bacterium, Escherichia coli, Aeromonas hydrophila, vibrio parahaemolytious, beta streptococcus or staphylococcus aureus.
- A kind of 4. application of antibacterial peptide as claimed in claim 2, it is characterised in that：Application in antineoplastic.
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Cited By (7)
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| CN108047321A (en) * | 2017-12-13 | 2018-05-18 | 集美大学 | A kind of litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide and its application |
| CN110218245A (en) * | 2019-05-30 | 2019-09-10 | 青岛红樱桃生物技术有限公司 | A kind of cecropin A TMP7 with bacteriostatic activity and its in the application being used to prepare in antibacterial agent |
| CN111333700A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea whey acidic protein antibacterial peptide and application thereof |
| CN111333716A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea hemoglobin antibacterial peptide and application thereof |
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN117986327A (en) * | 2024-04-03 | 2024-05-07 | 中国农业科学院农业基因组研究所 | Antibacterial peptide RS12 and application thereof |
| CN117986327B (en) * | 2024-04-03 | 2024-06-07 | 中国农业科学院农业基因组研究所 | Antibacterial peptide RS12 and application thereof |
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| CN108047321A (en) * | 2017-12-13 | 2018-05-18 | 集美大学 | A kind of litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide and its application |
| CN110218245A (en) * | 2019-05-30 | 2019-09-10 | 青岛红樱桃生物技术有限公司 | A kind of cecropin A TMP7 with bacteriostatic activity and its in the application being used to prepare in antibacterial agent |
| CN111333700A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea whey acidic protein antibacterial peptide and application thereof |
| CN111333716A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea hemoglobin antibacterial peptide and application thereof |
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN112898386B (en) * | 2021-03-02 | 2022-06-28 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN117986327A (en) * | 2024-04-03 | 2024-05-07 | 中国农业科学院农业基因组研究所 | Antibacterial peptide RS12 and application thereof |
| CN117986327B (en) * | 2024-04-03 | 2024-06-07 | 中国农业科学院农业基因组研究所 | Antibacterial peptide RS12 and application thereof |
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