CN107501410A - A kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide and its application - Google Patents
A kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide and its application Download PDFInfo
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- CN107501410A CN107501410A CN201710533742.4A CN201710533742A CN107501410A CN 107501410 A CN107501410 A CN 107501410A CN 201710533742 A CN201710533742 A CN 201710533742A CN 107501410 A CN107501410 A CN 107501410A
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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
- C07K14/795—Porphyrin- or corrin-ring-containing peptides
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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
Abstract
The invention discloses a kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide, its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.The molecular weight of the antibacterial peptide is 1736Da.The present invention discloses a kind of application of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide again, the application in the medicine for treating or preventing bacterium is prepared.The present invention lays a good foundation for the defence immunologic mechanism of follow-up further research Environment of Litopenaeus vannamei Low and the exploitation of antibacterials.
Description
Technical field
The present invention relates to the technical field of aquaculture, more particularly to a kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide and its
Using.
Background technology
In recent years, as expanding economy, people increasingly increase to the demand of aquatic products, market can not be met in amount of fishing
In the case of demand, culture fishery has obtained swift and violent development.Prawn is one of fastest-rising product in aquaculture, I
State is cultured prawn annual production highest country.However, compared with international shrimp culture industry, China, our province shrimp culture industry phase
It is relatively low to benefit, delayed effect of development is insufficient, Prospects of Sustainable Development allows of no optimist.To find out its cause, mainly supported with current China prawn
Grow disease take place frequently it is relevant by trade barrier etc. repeatly with prawn export caused by bio-safety.
Hemocyanin is also known as keyhole limpet hemocyanin, is a kind of multifunctional protein, is referred to as respiratory protein in the past, and it is moved positioned at segmental appendage
Cupric respiratory protein in thing and mollusk hemolymph, it is the indigo plant of the cupric found in arthropod and mollusk hemolymph
Green Polymer amount protein, is the carrier of oxygen, and be it is known can be with unique cuprein of oxygen Reversible binding.
Antibacterial peptide (Antibac-terial peptide) be called antimicrobial peptide (Antimicrobial pep-tide),
Antibiotic peptide (Antibiotics peptide), it is to be induced to produce through external condition by a variety of biological cell specific genes coding
One kind there is broad spectrum antibiotic, fungi, virus, protozoon, the polypeptide of suppression tumor killing cell isoreactivity effect.So far, state
It is inside and outside to report that kind of an antibacterial peptide is accredited, separated about more than 2000, it is artificial synthesized that template progress is made with natural antibacterial peptide
Simulating peptide reaches thousands of kinds.Four major classes can be divided into according to the difference of its structure in the antibacterial peptide of living nature naturally occurring：β-pleated sheet
Type antibacterial peptide, α screw types antibacterial peptide, extended structure type polypeptide and loop structural type polypeptides.
At present, the general character key issue that China's shrimp culture industry is badly in need of solving includes：The prevention and control of prawn infectiousness epidemic disease, product
Seed selection, nutrient research, Aquaculture Environmental Control and the upgrading of prawn process technology of kind etc..And successfully to solve these problems, explain
Bright prawn immune defence mechanism is premise and basis.In view of this, the present inventor studies and devised a kind of Environment of Litopenaeus vannamei Low blood
Thus azurin antibacterial peptide and its application, this case produce.
The content of the invention
It is an object of the invention to provide a kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide and its application, pass through vannamei boone pair
The research of shrimp hemocyanin antibacterial peptide S10 structure-activity relationships, to find new shrimp disease prevention and control, the tactful of fine-variety breeding provides think of
Road, promote health, the sustainable development of China's shrimp culture industry.
In order to solve above-mentioned purpose, the technical solution adopted by the present invention is as follows：
A kind of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide, its amino acid sequence such as sequence table SEQ ID NO:Shown in 1.
As the preferred embodiment of embodiment, the molecular weight of the antibacterial peptide is 1736Da.
A kind of application of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide, answering in the medicine for treating or preventing bacterium is prepared
With.
As the preferred embodiment of embodiment, the bacterium includes vibrio alginolyticus, vibrio parahaemolytious, Escherichia coli, thermophilic water
Aeromonas, staphylococcus aureus, Vibrio flurialis and beta streptococcus.
For the present invention using hemocyanin in shrimp Litopenaeus vannamei as research object, the hemocyanin of Environment of Litopenaeus vannamei Low can produce feature
Antibacterial peptide, and by bioinformatics on-line prediction peptide fragment find hemocyanin subunit in 12 kinds of peptide fragments there is antibacterial work
Property possibility it is maximum.A kind of peptide fragment S10 is selected on basis herein, the suction under maximum absorption wavelength is drawn with circular dichroism detector
Luminosity, then calculate alpha-helix and the isostructural content of beta sheet, therefore tentative prediction S10 two level knot with CD pro softwares
Structure.Then S10 is studied for the antibacterial activity of seven kinds of aquatic pathogenic bacterias, and 3D models first finally are carried out to the peptide with Pymol softwares
Prediction, then verify its secondary structure with nuclear magnetic resonance method.Suppress to make test result indicates that the peptide all has seven kinds of pathogenic bacteria
With.It is basically identical with software prediction to obtain structure for nuclear magnetic resonance method simultaneously.The present invention exempts from for further research Environment of Litopenaeus vannamei Low
Epidemic disease defense mechanism provides the foundation.
Brief description of the drawings
Fig. 1 antibacterial peptides S10 3D models；
Fig. 2 antibacterial peptides S10 HMBC spectrums；Wherein, abscissa is composed for H, and ordinate is composed for C；
Fig. 3 antibacterial peptides S10 NOESY spectrums；Wherein, transverse and longitudinal coordinate is all H spectrums；
Fig. 4 is the possible space structures of antibacterial peptide S10 of the present invention.
Embodiment
The prediction of the hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide of embodiment 1
First with tri- AntiBP Server, CAMP, APD2 on-line prediction softwares, Environment of Litopenaeus vannamei Low blood indigo plant egg is predicted
White large and small subunit antibacterial peptide fragment, as shown in table 1, table 2, prediction altogether obtains 34 small molecule pieces may with antibacterial activity
Section, wherein 11 peptide sequences (black matrix overstriking expression) may form αhelix, and can with pathogen membrane interaction and
Bacteriostasis is played, these prediction polypeptide molecular weight magnitude ranges are 1.5~1.9kDa.In addition, prediction result is shown, it is blue in blood
The α helical domains of albumen n end, the active fragment of the conservative copper ion binding domain in the Ig-like domains of C-terminal and center section, its
Middle copper ion binding domain and Ig-like domains account for main region.
The prediction of the hemocyanin in shrimp Litopenaeus vannamei large subunit antibacterial peptide fragment of table 1
Note：1st, overstriking peptide sequence：Speculated according to its physicochemical property and be likely to form αhelix, and can be with cause of disease mycoderm
Interaction plays bacteriostasis；2、Ⅰdomain：α helical domains；Ⅱdomain：Copper ion binding domain；Ⅲdomain：Ig-like
Domain.
The hemocyanin in shrimp Litopenaeus vannamei small subunit antibacterial peptide fragment of table 2 is predicted
Note：1st, overstriking peptide sequence：Speculated according to its physicochemical property and be likely to form αhelix, and can be with cause of disease mycoderm
Interaction plays bacteriostasis；2、Ⅰdomain：α helical domains；Ⅱdomain：Copper ion binding domain；Ⅲdomain：Ig-like
Domain.
Embodiment 2 is using circular dichroism detector analysis hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide Secondary Structure Content
11 kinds (overstriking peptide fragments in Tables 1 and 2) implementing described in 1 may be formed into αhelix, and energy and cause of disease
The peptide fragment that mycoderm interacts and plays bacteriostasis carries out circular dichroism spectra scanning, analyzes its structural content.
2.1 experiment equipment
2.1.1 experiment material
Experiment antibacterial peptide by BeiJing ZhongKe Yaguang Biology Science Co., Ltd (SciLight Biotechnology,
LLC) synthesize, the acetylation of polypeptide N-terminal, C-terminal amidatioon modification, purity is ﹥ 95%.
2.1.2 laboratory apparatus
Ultraviolet specrophotometer (UV5200) producer：Shanghai Yuan Xi Instrument Ltd.
Circular dichroism spectrometer (Jasco J-810) producer：Japanese Jasco
Cuvette：1mm quartz colorimetric utensils
2.2 sample preparation
The most long absorption ripple of 11 samples is scanned in scanning range is 190nm-400nm using ultraviolet specrophotometer
It is long, progressively add water until absorbance is 1 into sample, record data is that circular dichroism spectra makees early-stage preparations.
2.3 sample test steps
2.3.1, open instrument
Computer is opened, fully opens nitrogen cylinder main valve, pressure-reducing valve is opened, gauge outfit is maintained at 0.1Pa.Open instrument side
Nitrogen stream gauge, be that air-flow is maintained at 3-5L/min.Instrument power source is opened, instrument starts lighting (about needing 0.5min), treats instrument
After " open " lamp is bright on device panel, double-click " Spectra Manager " icons, selects in Spectra Manager dialog boxes
" Spectrum Measurement ", instrument start self-examination, after about 2min, after self-test, occur for required mensuration
Spectrum Measurement dialog boxes, according to test request arrange parameter.
2.3.2, parameter setting
Parameters arrange parameters：
Wave-length coverage：190-250nm
Data collection point：0.5nm
Scanning Speed：100nm/min
Scanning Mode：Continuous
Narrow peak width：1nm
Data Mode are set：CD or FDCD (fluorescence CD) method of testing
Option：Selection note has related parameter
2.3.3, sample test
The sample prepared is put into 1mm quartz colorimetric utensils, is put into specimen holder, solution example frame is placed on by aperture
Side, covers cover plate, clicks on START and starts to test, when length scanning to 400nm once, open nitrogen protection, the end of scan is automatic
Generate Spectra Analysis dialog boxes.
2.3.4, spectrogram processing
File menus in the dialog box of generation are clicked on, select save as that CD spectrograms are preserved into generation .jws files.
2.3.5, shut down
Instrument host power supply is closed after exiting CD programs, then closes and removes nitrogen cylinder main valve, discharge residual nitrogen, is finally closed
Nitrogen stream gauge on instrument.
2.4 data processing
1st, using CDPro softwares, CD data descendings is exported to notepad .inp forms is saved as, is copied into
In CDPro files, CRDATA.EXE is first run, calculating is performed in operation SELLON3.EXE, as a result opens sellon3.out and look into
See.
2nd, computational methods：
α helical contents=H (r)+H (d)；
β-pleated sheet=S (r)+S (d)；
Corner=Trn；
Random=Unrd.
2.5 experimental data
CDpro software data processing of the table 3 to 11 peptides
2.6 antibacterial peptide fragments are chosen
The present invention chooses antibacterial peptide S10 therein from 11 kinds of peptide fragments of table 3 and carries out further structure activity study.From table
3 learn, antibacterial peptide S10 α helical contents are 20.6%, β-pleated sheet content is 15.1%, β-bend content is 26.1%, illustrate peptide
The content of αhelix only has 3 amino acid residues in S10 15 amino acid residues, it is impossible to forms αhelix, β-bend
Content has 4 amino acid residues, can form β-bend structure.
Embodiment 3 verifies antibacterial peptide S10 bacteriostatic activity using colony counting method
3.1 operating procedure
Experiment antibacterial peptide by BeiJing ZhongKe Yaguang Biology Science Co., Ltd (SciLight Biotechnology,
LLC) synthesize, the acetylation of polypeptide N-terminal, C-terminal amidatioon modification, purity is ﹥ 95%.
The analysis of prawn hemocyanin chemical synthesis antibacterial peptide fragment bacteriostatic activity is carried out using following methods, and idiographic flow is such as
Under：
(1) be first placed on -80 DEG C preservation seven kinds of aquatic pathogenic bacterias (vibrio alginolyticus, vibrio parahaemolytious, Escherichia coli,
Aeromonas hydrophila, staphylococcus aureus, Vibrio flurialis, beta streptococcus) activated (50 μ L strain+1mL meat in a small amount respectively
Soup fluid nutrient medium), then (or can also be until exponential phase with shaking table culture 6-12h under 37 DEG C of constant temperatures
About 24h is cultivated at 28 DEG C)；
(2) take the μ L of bacterium solution 100 after activation to add 900 μ L sterilized waters in centrifuging in tubule and be diluted respectively, be
10-1Times, 10 are diluted to successively-6—10-7Times.
(3) by the μ L of bacterium solution 10 after dilution and 1.0mg/mL, 0.5mg/mL, 0.25mg/mL, 0.125mg/mL different component
The μ L of polypeptide sample liquid 10 mix, be put in the incubation that 2h is carried out among 30 DEG C of thermostat water bath, draw 10 μ L mixed liquor afterwards
Flat board is applied to, every group of setting 2 is parallel, is inverted under 37 DEG C of condition of culture, and bacterium colony is counted after cultivating 12-24h
(negative control is used as using sterilized water).
(4) bacteriostasis rate (%)=(negative control clump count-experimental group clump count)/negative control clump count × 100 are calculated.
3.2 interpretation of result
Bacteriostasis rates (%) of the peptide S10 of table 4 to seven kinds of pathogenic bacteria
As shown in Table 4, peptide S10 is respectively provided with inhibitory action to seven kinds of pathogenic bacteria, wherein to vibrio parahaemolytious, B-mode hammer
Bacterium, Vibrio flurialis, Escherichia coli, Aeromonas hydrophila have stronger inhibitory action, to staphylococcus aureus and vibrio alginolyticus
Inhibitory action it is relatively weak.
Embodiment 4 is using nuclear magnetic resonance method research antibacterial peptide S10 secondary structures
4.1 antibacterial peptide S10 3D model predictions
Pass through websitehttp://swissmodel.expasy.orgAmino acid sequence progress three-dimensional structure to peptide S10 is pre-
Survey, select the higher tomograph of similarity, download .pdb files, opened in PyMol softwares and checked and edited, obtained
3D illustratons of model to peptide S10 are as shown in Figure 1.Rightmost side fractional prediction peptide S10 may contain corner structure in figure, pars intermedia in figure
It may be parallel to divide prediction.Further structure prediction needs to be verified by nuclear magnetic resonance method.
4.2 nuclear magnetic resonance methods prediction antibacterial peptide S10 secondary structure
4.2.1
Sample is sent to Zhong Ke new lives company, the C spectrums, H spectrums, HMBC spectrums for obtaining antibacterial peptide S10 (represent the long-range of C and H
Relation), NOESY spectrum (the long-range relation for representing H and H).
4.2.2
Its chemical structural formula is drawn with Chemoffice softwares according to peptide S10 amino acid sequence, and applied
Chemical structural formula is belonged to C and composed, in H spectrums by MestReNova softwares automatically, so as to draw the position at the peak corresponding to each C, H
Put.
4.2.3
Antibacterial peptide S10 C spectrums, H spectrums, HMBC spectrums and NOESY spectrums is opened in MestReNova softwares, using H compose as
The abscissa of HMBC spectrums, ordinate of the C spectrums as HMBC spectrums, transverse and longitudinal coordinate of the H spectrums as NOESY spectrums, import chemical formula and carry out
Ownership, H and long-range C possibility dependency relation is analyzed in HMBC spectrums, H passes related to long-range H possibility are analyzed in NOESY spectrums
System.
4.3 nuclear magnetic resonance methods predict the interpretation of result of antibacterial peptide S10 secondary structures
4.3.1 antibacterial peptide S10 chemical formula
Antibacterial peptide S10 peptide section sequence：FWVSLKGGKTSIERK, translating into characters No. three is：
Phe-Trp-Val-Ser-Leu-Lys-Gly-Gly-Lys-Thr-Ser-Ile-Glu-Arg-Lys。
4.3.2 antibacterial peptide S10 NMR spectra
HMBC spectrums and NOESY spectrums in antibacterial peptide S10 secondary structure parsing Main Analysis NMR spectra.
The atlas analysis and data processed result of nuclear magnetic resonance method are as shown in Figure 2 and Figure 3.
Following information can be drawn from Fig. 2 HMBC spectrograms：
1st, the C and H on polypeptide side chain on the 1st, 2,3,5,6,9,10,12,13,14, No. 15 Amino acid side chain may have
Contact；
2nd, the C and H on polypeptide side chain on the 1st, 2,3,4,5,6,10,11,12,13, No. 14 Amino acid side chain may have
Relation；
3rd, the C of the benzene and H on 1,2,10, No. 15 Amino acid side chain may be related on the 1st, No. 2 Amino acid side chain；
4th, the C of the benzene and H on polypeptide side chain may have relation on the 1st, No. 2 Amino acid side chain；
5th, the C and H on polypeptide side chain on the 7th, 8, No. 15 Amino acid side chain may be related；
6th, the C and the 63rd on the 55th, No. 74 amino acid, the H on No. 84 amino acid may have relation；
7th, the H on C and No. 71 amino acid on No. 56 amino acid may have relation；
8th, C and the 68th, the H on No. 77 amino acid on the 57th, 59,62, No. 64 amino acid may have relation；
9th, the H on C and No. 68 amino acid on No. 61 amino acid may have relation；
10th, the H on C and No. 57 amino acid on No. 76 amino acid may have relation；
11st, the H on C and No. 58 amino acid on No. 78 amino acid may have relation；
12nd, the C and the 45th on No. 93 amino acid, the H on No. 46 amino acid may have relation；
13rd, the H on C and No. 35 amino acid on No. 97 amino acid may have relation；
14th, the H on C and No. 15 amino acid on the 119th, 122, No. 124 amino acid may have relation；
15th, the C and the 24th on No. 120 amino acid, the H on No. 25 amino acid may have relation；
16th ,-the C=O on the polypeptide backbone and H on polypeptide side chain may have relation.
Following information can be drawn from Fig. 3 NOESY spectrograms：
1st, the H on H and No. 15 amino acid on No. 116 amino acid may have relation；
2nd, the H and the 31st on No. 110 amino acid, the H on No. 32 amino acid may have relation；
3rd, the H on H and No. 27 amino acid on the 108th, No. 111 amino acid may have relation；
4th, the H on H and No. 36 amino acid on No. 97 amino acid may have relation；
5th, the H and the 45th on No. 91 amino acid, the H on No. 46 amino acid may have relation；
6th, the H on H and No. 110 amino acid on No. 76 amino acid may have relation；
7th, the H and the 69th on the 62nd, No. 64 amino acid, the H on 71, No. 72 amino acid may have relation；
8th, the H and the 36th on the 61st, No. 103 amino acid, the H on No. 62 amino acid may have relation；
9th, the H on the 34th, 40, No. 83 amino acid is relevant with the H possibility on the 48th, 50,52,93,89, No. 99 amino acid
System.
4.3.3 discuss
4.3.3.1 α spirals, β-pleated sheet, the feature of β-bend structure：
α spirals：The hydrogen bond of regular array make it that helical structure is stable, and the mode of hydrogen bond arrangement is：Each amino acid is residual
N-H of base and its amino side form hydrogen bond between being separated by the C=O of three amino acid residues.
β-pleated sheet：The flat-folded of peptide bond is serrated, and has well-regulated hydrogen bond between the N-H and C=O of adjacent peptide chains main chain,
Among beta sheet, all peptide bonds are relevant with the formation of interchain hydrogen bond, are vertically to close between the major axis and hydrogen bond of beta sheet
System.
β-bend：The characteristics of corner I is：The amide nitrogen and the 1st amino acid residue ketonic oxygen formation hydrogen bond of 4th residue；
The characteristics of corner II is：3rd residue is usually glycine.
4.3.3.2
It can be drawn from peptide S10 HMBC spectrograms：In the 6th to the 9th amino acid of S10 peptide section sequences, No. 74 H with
Between No. 63 C and between No. 61 H and No. 68 C, relation point, and the 8th of S10 peptide section sequences between No. 56 H and No. 71 C be present
Individual amino acid is glycine, meets β-bend feature foundation, can be inferred that the 6th to the 9th amino acid of S10 peptide section sequences
Between form β-bend.Other points represent relation long-range between this each C and H, affect the space structure of S10 peptide fragments.Example
Such as, the C on 1,2,3,5,6,9,10,12,13,14, No. 15 Amino acid side chain is relevant with the H on polypeptide side chain, illustrates phase be present
Interreaction force, cause the both ends of peptide chain close to each other, it is possible to which it is not one straight straight on space structure to release peptide chain
Line, but radian be present.
It can be drawn from peptide S10 NOESY spectrograms：Exist between H and H on 5th amino acid and the 6th amino acid and close
It is application point, relation and function point is present between the H and H on the 8th amino acid and the 9th amino acid, therefore further demonstrate β
Corner there may be；Relation and function point be present between the H on H and the 10th to 15 amino acid on 1st to 5 amino acid, enter
The peptide chain that one step demonstrates S10 peptide fragments is not straight line on space structure.As a result it is as shown in Figure 4.
In a word, the present invention uses circular dichroism detector to determine peptide S10 α helical contents to be for 20.6%, β-pleated sheet content
15.1%th, β-bend content is 26.1%, illustrates that the content of αhelix in peptide S10 15 amino acid residues only has 3 ammonia
Base acid residue can not form αhelix, and β-bend content has 4 amino acid residues, can form β-bend structure；Bacteriostatic experiment
Checking antibacterial peptide S10 is respectively provided with inhibitory action to seven kinds of pathogenic bacteria, wherein to vibrio parahaemolytious, beta streptococcus, Vibrio flurialis, big
Enterobacteria, Aeromonas hydrophila have stronger inhibitory action, to staphylococcus aureus and the inhibitory action phase of vibrio alginolyticus
To weaker；By 3D models and magnetic nuclear resonance method, predicted polypeptide S10 may contain β-bend structure, and both ends may be parallel, class
Like U-shaped；By predicting that the stronger bacteriostatic activities of release S10 may be relevant with forming the space structure of β-bend, can subsequently pass through
The β-bend structure replaced or destroyed in peptide S10, is tested to the antibacterial activity of new synthetic peptide, so as to further verify this
One conclusion.
It is described above, only present pre-ferred embodiments, therefore the scope that the present invention is implemented can not be limited according to this, 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. hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide, it is characterised in that：Its amino acid sequence such as sequence table SEQ ID NO:1 It is shown.
- A kind of 2. hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide as claimed in claim 1, it is characterised in that：Point of the antibacterial peptide Son amount is 1736Da.
- A kind of 3. application of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide as claimed in claim 1, it is characterised in that：Controlled in preparation Application in the medicine for the treatment of or pre- bacteriological protection.
- A kind of 4. application of hemocyanin in shrimp Litopenaeus vannamei antibacterial peptide as claimed in claim 1, it is characterised in that：The bacterium Including vibrio alginolyticus, vibrio parahaemolytious, Escherichia coli, Aeromonas hydrophila, staphylococcus aureus, Vibrio flurialis and B-mode chain Coccus.
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| CN108396030A (en) * | 2018-05-10 | 2018-08-14 | 中山大学 | Litopenaeus vannamei antibacterial peptide gene Lv-BigPEN and its recombinant protein and application |
| CN108396030B (en) * | 2018-05-10 | 2021-08-06 | 中山大学 | Lifobinopenaeus antibacterial peptide gene Lv-BigPEN and recombinant protein and application thereof |
| CN108840925A (en) * | 2018-07-25 | 2018-11-20 | 汕头大学 | It is a kind of from the anti-WSSV peptide LvHcL48 of hemocyanin in shrimp Litopenaeus vannamei and its application |
| CN108840925B (en) * | 2018-07-25 | 2021-09-10 | 汕头大学 | anti-WSSV peptide LvHcL48 derived from litopenaeus vannamei hemocyanin and application thereof |
| CN113087771A (en) * | 2021-04-25 | 2021-07-09 | 集美大学 | Nanmeibai-DNA-conjugated antibacterial peptide VPDB40 and application thereof |
| CN113209126A (en) * | 2021-05-31 | 2021-08-06 | 中山大学 | Prawn immunopotentiator based on RNA interference technology and preparation method and application thereof |
| CN114380893A (en) * | 2021-12-30 | 2022-04-22 | 集美大学 | Pickled Litopenaeus vannamei antibacterial peptide EC-V10 and application thereof |
| CN114380893B (en) * | 2021-12-30 | 2023-10-27 | 集美大学 | Pickled litopenaeus vannamei antibacterial peptide EC-V10 and application thereof |
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