CN113735953B - Sea anemone polypeptide toxin Ap-GT as well as preparation method and application thereof - Google Patents
Sea anemone polypeptide toxin Ap-GT as well as preparation method and application thereof Download PDFInfo
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- A01N37/44—Biocides, pest repellants or attractants, or plant growth regulators containing organic compounds containing a carbon atom having three bonds to hetero atoms with at the most two bonds to halogen, e.g. carboxylic acids containing at least one carboxylic group or a thio analogue, or a derivative thereof, and a nitrogen atom attached to the same carbon skeleton by a single or double bond, this nitrogen atom not being a member of a derivative or of a thio analogue of a carboxylic group, e.g. amino-carboxylic acids
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Abstract
The invention provides an anemone polypeptide toxin Ap-GT as well as a preparation method and application thereof, the synthesized anemone polypeptide toxin Ap-GT has more obvious insecticidal action on yellow mealworms, and the half lethal dose is 14.8nM. The sea anemone polypeptide toxin Ap-GT with a specific sequence is synthesized, so that the addition amount of the sea anemone polypeptide toxin Ap-GT can be effectively controlled in application, the effect is exerted to the maximum extent, the dosage of a medicament is reduced, and the safety is improved to the maximum extent. The invention obtains the marine polypeptide with high-efficiency insecticidal effect and small toxicity to mammals, and can lay a foundation for researching and developing novel, high-efficiency and safe biological insecticides.
Description
Technical Field
The invention relates to the technical field of sea anemone, and particularly relates to sea anemone polypeptide toxin Ap-GT and a preparation method and application thereof.
Background
Sea Anemone (Sea Anemone), also known as Sea chrysanthemum, belongs to the phylum Echinacea, the class Coralliacea, the class Laurencia sextoddalis. Sea anemone is one of the most primitive metazoan groups and also one of the oldest toxic marine animals in existence, and there is molecular evidence and fossil data that the sea anemone originally originated 7.5 hundred million years ago. Sea anemones are in various varieties, more than 1100 species of the order of sea anemones are recorded in the world, and belong to about 400 genera of 50 families, while Chinese sea anemone species account for about 1/10 of the world and are widely distributed in warm and tropical sea areas. Stinging cells on the sea anemone tentacles can secrete venom predatory fish, shellfish, copepods, crustaceans and worms, and the venom is rich in various polypeptide toxin components and is an important marine medicine resource. The anemone has the effects of astringing, arresting discharge, eliminating dampness, killing parasites and the like according to records of Chinese materia medica and Chinese medicinal animal records, and is used for treating rectocele, hemorrhoids, entomosis and the like in traditional Chinese medicine. Salgado VL et al found that three anemone toxins, shI, cpI and CgII, were particularly lethal to crustaceans, moderately toxic to insects (cockroaches), and substantially non-toxic to mammals (mice). ATX-I and ATX-II are highly effective against insect sodium channels, have high binding affinity to cockroach neural membranes, and have low binding affinity to rat brain synaptosomes, so ATX-I and ATX-II preferentially target insects over mice. Certain actitoxins are capable of specifically acting on insects and have a strong insecticidal capacity with little or no toxic side effects on mammals. The sea anemone polypeptide toxin is safe and effective as a novel pesticide. CN111876457A discloses preparation of an enzymolysis polypeptide of mulched sea anemone and insecticidal application thereof, wherein the extract of the mulched sea anemone is a mixture of multiple sequence polypeptides, and the composition is not easy to control, so that the drug effect and the safety of a medicament are not easy to improve.
Disclosure of Invention
In view of this, the invention provides an anemone polypeptide toxin Ap-GT, a preparation method and an application thereof, and solves the technical problems.
The technical scheme of the invention is realized as follows: an actinia polypeptide toxin Ap-GT,
the sequence is GIDCTCNGHNGEYWFGVQSCNGNAKHDCSSILGRCCVY, has 6 cysteines, and forms 3 disulfide bonds.
2. The method of claim 1, comprising the steps of:
(1) Soaking and washing 2-cl resin in DCM; adding Fmoc-Tyr (tbu) -OH, adding DCM and DIEA for reaction, and then adding methanol and DCM for blocking reaction;
(2) Washing the resin treated in the step (1) with DMF, adding piperidine to remove Fmoc, and washing the resin after reaction;
(3) Taking next amino acid Fmoc-VAL-OH and HOBT, adding DMF (dimethyl formamide) and DIC (Didic reaction), and washing the resin after reaction;
(4) Washing the resin treated in the step (3) by using DMF (dimethyl formamide), adding piperidine to remove Fmoc (methyl methacrylate), and washing the resin after reaction;
(5) Repeating the steps (3) and (4) until the peptide chain is finished;
(6) Adding cutting liquid into the resin obtained in the step (5), shaking for cutting, filtering to remove the resin to obtain a cut filtrate, finally adding glacial ethyl ether into the filtrate, centrifuging, and collecting bottom polypeptide to obtain a crude polypeptide;
(7) Separating and purifying the crude polypeptide by HPLC, and drying to obtain a linear peptide Ap-GT;
(8) And (5) carrying out oxidation folding on the linear peptide Ap-GT obtained in the step (7) to obtain an oxidized peptide Ap-GT, and separating and purifying the oxidized peptide Ap-GT by adopting preparative HPLC to obtain a pure product.
Further, step (1), the degree of substitution Sd =0.2mmol/g of the 2-cl resin.
Further, in the step (1), DCM and DIEA are added for reaction for 80-100min, and then methanol and DCM are added for closed reaction for 20-40min.
Further, in the step (2) and the step (4), the reaction time is 15-25min.
Further, step (3), adding DIC for 0.8-1.2h.
Further, step (6), the cutting fluid is prepared from 95% of trifluoroacetic acid, 1% of water, 3,4-ethylenedioxythiophene 2% and triisopropylsilane 2% by mass percent.
Further, in the step (6), the cutting time is 1.8-2.2h.
Further, step (6), the centrifugation conditions are: centrifuging at 3000 rpm for 2min.
The invention discloses application of anemone polypeptide toxin Ap-GT in preparation of a pesticide.
The Chinese names of the raw materials used in the invention are shown in the following table 1:
TABLE 1 Compound Chinese name
Compared with the prior art, the invention has the beneficial effects that:
(1) The sequence of the synthesized anemone polypeptide toxin Ap-GT is GIDCTCNGHNGEYWFGVQSCNGNAKHDCSSILGRCCVY, the anemone polypeptide toxin has a more remarkable insecticidal effect on yellow mealworms, and the half lethal dose is 14.8nM.
(2) The sea anemone polypeptide toxin Ap-GT with a specific sequence is synthesized, so that the addition amount of the sea anemone polypeptide toxin Ap-GT can be effectively controlled in application, the effect is exerted to the maximum extent, the dosage of a medicament is reduced, and the safety is improved to the maximum extent.
(3) The invention obtains the marine polypeptide with high-efficiency insecticidal effect and low toxicity to mammals, and can lay a foundation for researching and developing novel, high-efficiency and safe biological insecticides.
Drawings
FIGS. 1-A and 1-B are HPLC analysis and mass spectrometry profiles of the linear peptide Ap-GT;
FIG. 2 is a dynamic oxidative folding process of the linear peptide Ap-GT;
FIG. 3 is an HPLC analysis profile of oxidized peptide Ap-GT;
FIG. 4 shows the insecticidal effect of the polypeptide Ap-GT on yellow mealworms, note: experimental groups showed significant differences compared to negative control groups (. P < 0.01;. P < 0.001).
Detailed Description
In order to better understand the technical content of the invention, specific examples are provided below to further illustrate the invention.
The experimental methods used in the examples of the present invention are all conventional methods unless otherwise specified.
The materials, reagents and the like used in the examples of the present invention can be obtained commercially without specific description.
Examples
1. Materials and methods
1.1 Experimental materials
Chromatographic grade Trifluoroacetic acid (TFA) and chromatographic grade Acetonitrile (ACN) were purchased from shanghai alatin biochem ltd; water analytical C18 column (5 μm,4.6 mm. Times.250 mm) was purchased from Waters corporation, USA; eilide preparative C18 columns (10 μm,10 mm. Times.250 mm) were purchased from Dalianglitt analytical instruments, inc.; conventional molecular biological reagents such as a plasmid extraction kit and the like are purchased from Tiangen Biochemical technology (Beijing) Co., ltd.
1.2 Experimental instruments
CEM full-automatic microwave polypeptide synthesizer (LibertyBlue, usa); reversed phase high performance liquid chromatography (Thermo Fisher, germany); triple quadrupole liquid chromatography mass spectrometer (shimadzu, japan); desktop lyophilizers (seifei, china); an enzyme-labeling instrument (MR-96A, shenzhen Mirui); patch clamp system (Axon 900A, usa).
1.3 Experimental methods
1.3.1 Synthesis and oxidative folding of the anemone Potentilotoxin Ap-GT
(1) 3g of 2-cl resin, sd =0.2mmol/g, were weighed into a reactor and soaked for 5min with DCM (20 ml), washed 2 times with DMF (20), once with DCM for the third time, 0.8mmol of Fmoc-Tyr (tbu) -OH, 12ml of DCM,2ml of DIEA were added. After the reaction for 90min, 4ml of analytical methanol and 10ml of DCM are added, and the reaction is sealed for 30min.
(2) Washing 4 times with DMF, adding piperidine (20% piperidine +80% DMF), removing Fmoc,20min. Washing the resin with DMF for 5 times, adding a small amount of resin (10-20 particles) into a detection tube, adding ninhydrin (5 g/100ml analytical ethanol) 2 drops, pyridine 2 drops, heating at 100 deg.C for 2min, and developing.
(3) Weighing the next amino acid Fmoc-VAL-OH (1.8 mmol) and HOBT (1.8 mmol), adding into a reactor, pouring 10ml of DMF, adding 2ml of DIC for reaction for 1 hour, washing with DMF for 4 times, taking a small amount of resin, and detecting to obtain the product.
(4) Washing 4 times with DMF, adding piperidine (20% piperidine +80% DMF), removing Fmoc,20min. Washing the resin with DMF for 5 times, adding a small amount of resin (10-20 particles) into a detection tube, adding ninhydrin (5 g/100ml analytical ethanol) 2 drops, pyridine 2 drops, heating at 100 deg.C for 2min, and developing.
(5) Repeating the steps (3) and (4) until the peptide chain is finished.
(6) The resin was placed in a 50ml centrifuge tube with methanol suction, and cutting fluid was added (95% TFa +1% 2 O +2% EDT +2% TIS) 40ml, cut for 2h with shaking, and finally flatten the cut solution (filtered off resin)Dividing into 4 new 50ml centrifuge tubes, adding 40ml of glacial ethyl ether, shaking, centrifuging at 3000 rpm for 2min, leaving polypeptide at the bottom, and pouring off the upper layer of diethyl ether. Obtaining crude polypeptide.
(7) Separating and purifying the polypeptide by HPLC to obtain pure polypeptide, and freeze-drying into powder by a vacuum freeze dryer.
(8) Weighing the linear peptide sample obtained in the step (7), using a small amount of water to assist dissolution, and adding 0.1MNH according to the proportion of 1:2 4 HCO 3 Stirring, sampling at 24, 48 and 72h, observing the dynamic oxidative folding process by HPLC, purifying to obtain a pure product, and then carrying out identification confirmation by mass spectrum.
1.3.2 insect injection method
The insect injection method is carried out by selecting yellow mealworms with the weight of about 180mg, and the specific steps refer to the literature 'chemical synthesis of conotoxin ImI and the research on the insecticidal activity thereof'. Briefly described as follows: the polypeptide Ap-GT was dissolved in 0.7wt% NaCl solution to 5nM, 10nM, 15nM, 20nM and 25nM, and 5. Mu.l of the polypeptide Ap-GT was injected into the abdomen of Tenebrio molitor. Tenebrio molitor was injected as a negative control with 5. Mu.l of 0.7wt% NaCl solution as a blank control without any treatment.
1.3.3 data processing
Data were counted and processed using software GraphPad Prism6, and data between control and experimental groups were analyzed using t-test, indicating significant differences (p < 0.05) and very significant differences (p < 0.01).
2 results
2.1 Synthesis and oxidative folding of Polypeptides
The linear peptide Ap-GT was synthesized by polypeptide solid phase synthesis (SPPS), purified by HPLC, and identified by mass spectrometry as 4112.57Da (see fig. 1-B). The synthesized linear peptide Ap-GT was subjected to one-step oxidative folding by air oxidation, and the dynamic oxidative folding process was observed by HPLC after sampling at 24, 48, and 72h (see fig. 2). The theoretical molecular weight of the linear peptide Ap-GT is 4112.57Da, the molecular weight of the oxidized peptide Ap-GT is 4106.62, the difference between the two is about 6Da, which proves that 3 disulfide bonds are formed correctly.
2.2 isolation and purification of oxidized peptides
The oxidized peptide Ap-GT was separated and purified by preparative HPLC, and analyzed by analytical HPLC after purification, and the result is shown in fig. 3, where the elution time of the oxidized peptide Ap-GT was 17.477min, and the purity thereof was more than 95% by peak area calculation.
2.3 insect injection method
The experimental results are shown in fig. 4, the mortality rates of the flour weevils of the blank control group and the negative control group are both 0, which indicates that the injection method is feasible for evaluating the insecticidal effect of the polypeptide Ap-GT. The mortality rate of the tenebrio molitor increases along with the increase of the dosage of the polypeptide Ap-GT, and has a significant difference compared with a control group. The mortality rate of the high-dose 25nM polypeptide Ap-GT to insects reaches 90.0%, and the half lethal dose calculated by software is 14.8nM. The dosage of the polypeptide Ap-GT is only below 0.3 percent of the small molecular polypeptide mixture of the mulched sea anemone under the same mortality rate, and the dosage of the pesticide can be obviously reduced.
The above description is only for the purpose of illustrating the preferred embodiments of the present invention and is not to be construed as limiting the present invention, and any modifications, equivalents, improvements and the like made within the spirit and principle of the present invention should be included in the scope of the present invention.
Sequence listing
<110> Hainan college of medicine
<120> actinocongestin Ap-GT as well as preparation method and application thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 38
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Gly Ile Asp Cys Thr Cys Asn Gly His Asn Gly Glu Tyr Trp Phe Gly
1 5 10 15
Val Gln Ser Cys Asn Gly Asn Ala Lys His Asp Cys Ser Ser Ile Leu
20 25 30
Gly Arg Cys Cys Val Tyr
35
Claims (10)
1. An aplidine toxin Ap-GT is characterized in that,
the sequence is GIDCTCNGHNGEYWFGVQSCNGNAKHDCSSILGRCCVY, which has 6 cysteines, forming 3 disulfide bonds.
2. The method of producing actinia polypeptide toxin Ap-GT of claim 1, comprising the steps of:
(1) Soaking and washing 2-cl resin in DCM; adding Fmoc-Tyr (tbu) -OH, adding DCM and DIEA for reaction, and then adding methanol and DCM for blocking reaction;
(2) Washing the resin treated in the step (1) by using DMF (dimethyl formamide), adding piperidine to remove Fmoc (methyl methacrylate), and washing the resin after reaction;
(3) Taking next amino acid Fmoc-VAL-OH and HOBT, adding DMF (dimethyl formamide) and DIC (Didic reaction), and washing the resin after reaction;
(4) Washing the resin treated in the step (3) with DMF, adding piperidine to remove Fmoc, and washing the resin after reaction;
(5) Repeating the steps (3) and (4) until the peptide chain is finished;
(6) Adding cutting liquid into the resin obtained in the step (5), shaking for cutting, filtering to remove the resin to obtain a cut filtrate, finally adding glacial ethyl ether into the filtrate, centrifuging, and collecting bottom polypeptide to obtain a crude polypeptide;
(7) Separating and purifying the crude polypeptide by HPLC, and drying to obtain a linear peptide Ap-GT;
(8) And (5) carrying out oxidation folding on the linear peptide Ap-GT obtained in the step (7) to obtain an oxidized peptide Ap-GT, and separating and purifying the oxidized peptide Ap-GT by adopting preparative HPLC to obtain a pure product.
3. The method of producing an anemonia polypeptide toxin Ap-GT according to claim 2, wherein in step (1), the degree of substitution Sd =0.2mmol/g for the 2-cl resin.
4. The method for preparing actinia polypeptide toxin Ap-GT according to claim 2, wherein in the step (1), DCM and DIEA are added for reaction for 80-100min, and methanol and DCM are added for blocking reaction for 20-40min.
5. The method for producing the aplidine toxin Ap-GT according to claim 2, wherein the reaction time in step (2) and step (4) is 15 to 25min.
6. The method of claim 2 or 5, wherein DIC is added in step (3) for 0.8-1.2h.
7. The method of claim 2, wherein in step (6), the cutting fluid is prepared from (by mass%) trifluoroacetic acid 95%, water 1%, 3,4-ethylenedioxythiophene 2%, and triisopropylsilane 2%.
8. The method of producing the aivlosin Ap-GT according to claim 2 or 7, wherein the cleavage time in step (6) is 1.8-2.2h.
9. The method of producing the aplidine toxin Ap-GT according to claim 2, wherein in step (6), the centrifugation conditions are: centrifuging at 3000 rpm for 2min.
10. Use of the actinia polypeptide toxin Ap-GT according to claim 1 in the preparation of a pesticide.
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| CN101130775A (en) * | 2007-06-27 | 2008-02-27 | 中山大学 | Novel signal conotoxin sequence and preparing method and application thereof |
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| CN101205251A (en) * | 2007-11-29 | 2008-06-25 | 中山大学 | Chinese south China sea signal taro snail nerve toxin gene Lt3.2 and uses thereof |
| CN101285063A (en) * | 2008-03-26 | 2008-10-15 | 中山大学 | Novel conus P-superfamily toxin, sequence and uses thereof |
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