CN101607992B - Antibacterial peptide separated from cow blood and code sequence and application thereof - Google Patents
Antibacterial peptide separated from cow blood and code sequence and application thereof Download PDFInfo
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Abstract
The invention relates to an antibacterial peptide with antibacterial activity separated from cow blood, a code sequence and an application thereof. The antibacterial peptide has 1 to 25 amino acid sequences in a sequence table SEQ ID NO: 1.Except for the common property of the common antibacterial peptide such as wide antibacterial spectrum, quick sterilization, high selectivity, no drug resistance generation and no teratogenic action, the antibacterial peptide also has the flowing advantages that the structure is simple; the artificial synthesis is convenient; no antigenicity exists when the antibacterial peptide is applied to mammals; the antibacterial peptide is separated from the red blood cell of the cow blood; and the red blood cell is one of animal blood components, is involved in the process of blood circulation, and has no hemolytic toxicity or low hemolysis rate. The antibacterial peptide not only can be used for preparing a medicament for treating gram positive bacteria, gram negative bacteria, and epiphyte or viral infection, but also can be applied to the fields such as milk fresh-keeping, or other food preservatives, feed mould inhibitors and the like.
Description
Technical field
The invention belongs to biological technical field, relate in particular to a kind of from cow blood isolated antibacterial peptide and encoding sequence and purposes with anti-microbial activity.
Background technology
Antibacterial peptide (antimicrobial peptides) is the polypeptide that a class of biomass cells genes encoding generation has anti-microbial activity, being body natural immunity bioactive molecule for conforming and producing with its own existence in the organic evolution process, is autarcetic important medium.The antibacterial peptide molecular weight is little, and peptide chain is generally 10～50 amino-acid residues.Find that at present antibacterial peptide is except antibiotic (gram positive organism and the gram-negative bacteria) activity with wide spectrum, also fungi (as Candida albicans etc.), virus (as influenza virus, hiv virus etc.), parasite (as nematode, flagellate etc.) and tumour etc. had the extremely strong ability of killing, the what is more important antibacterial peptide is to the almost not effect of normal eukaryotic cell, only act on the eukaryotic cell of prokaryotic cell prokaryocyte and generation pathology, non-immunogenicity can not produce anaphylaxis simultaneously.The sterilization mechanism of antibacterial peptide is different fully with microbiotic, antibacterial peptide generally is by acting on the cytolemma of target cell, destroy its integrity and produce the perforation phenomenon, cause the bacterial cytoplasm membrane permeability to increase, cause that water-soluble substances in the born of the same parents oozes out in a large number and reaches the effect of broad-spectrum antimicrobial.Therefore, pathogenic bacteria generally can not produce resistance to antibacterial peptide.
At present, be mainly to depend on microbiotic at the treatment bacteriosis, the antibiotic use removed bacterial infection as the mankind and brought into play enormous function.But because long-term abuse of antibiotics, bacterial drug resistance is more and more stronger, and the Resistant strain cases of infection are more and more, not only makes many once highly effective antibiotic medicines lose efficacy, and human life's health has been constituted serious threat.Current, virus disease is mainly depended on vaccine inoculation, but almost past medical help after the morbidity; Parasitic diseases is not treated substantially or do not prevented.The annual financial loss that causes thus is quite huge.
Antibacterial peptide has been compared following characteristics with the small molecules chemobiotic: (1) high efficiency, and (minimum inhibitory concentration MIC) is 0.25～4 μ g/L to the causal organism minimal inhibitory concentration; (2) broad spectrum all has effect to bacterium, fungi, virus, parasite, tumour cell; (3) hypotoxicity is because human and mammiferous normal cell structure and causal organism and tumour cell is different, in the antibacterial peptide concentration range in action, very little to the toxicity of normal body tissue cell; (4) stability, but through 100 ℃ handle 30min or far depart from neutrality with the pH value, than the solution-treated of heavy ion intensity after retains biological activity still.Some polypeptide can form the polymer structure or combine with the cytolemma lipid in solution, obtain the ability of opposing protease hydrolysis; (5) sterilizing ability rapidly, in experiment in vitro, most of antibacterial peptides are under the condition of effective MIC, and 5min can kill 99.7% pathogenic agent; (6) antibacterial peptide also has the enhance immunity system function, improves food conversion ratio, promotes functions such as animal production.
Antibacterial peptide all has stronger killing action to multiple Gram-positive in the food and negative bacteria, can suppress microbial growth fast, after the people, animal foods easily by body endoproteinase hydrolytic digestion and have no side effect, activity is very strong under acidic conditions, having good solubility and stability, is a kind of new Type of Preservatives that has development prospect; Some bacterial classification can also be trained or kill to antibacterial peptide during the fermentation for a certain area, or orientation is preserved bacteria group (as milk-acid bacteria) and prevented pernicious bacteria abnormal fermentation in food.Most of bioactive peptides also have good solubility, thermostability and be processing characteristics such as low-viscosity under the high density states, as soybean polypeptide, rapeseed peptides etc., can add in the food, make various functional food, and still can keep original physiologically active, also can directly make oral pharmaceutical dosage form, healthcare products, nutritious prod etc.Aspect the research of animal-feed antibacterial peptide additive, available gene engineering method is produced the environment-friendly type antibiotic peptide addition, with the negative issue that reduces or avoid Antibiotic Additive to cause.The use havoc of Antibiotic Additive the microecological balance of animal intestinal, and easily residual in animal body, had a strong impact on the quality and the human beings'health of livestock product.
Antibacterial peptide has unique antibacterial mechanisms and wide spectrum and does not produce chemical sproof superior character, it appear as that people seek the ideal antibacterials and foodstuff additive provide new direction, brought new opportunity for the mankind defeat drug-resistant microorganism, therefore antibacterial peptide also has huge application potential.
Since first antibacterial peptide cecropin (cecropin) is found in the world, be separated to more than 750 kind of antibacterial peptide from organic sphere so far, their distribution is extremely extensive, to plant, bacterium and virus etc. discovery is arranged all from Mammals, crustacean, fish, insect, Amphibians, birds.At present, domestic have more scholar to be separated to some in different terrestrial animals and the hydrocoles body to have active antibacterial peptide.And the antibacterial peptide of finding in Mammals mainly contains three classes, is respectively alexin, cathelicidins and histatinst23.Alexin is according to the position of amino acid whose quantity, halfcystine and the difference of disulfide linkage mode of connection, can be divided into α-alexin, beta-alexin and θ-alexin three classes: α-alexin is that the extremely strong small molecules antibacterial peptide of cationic that obtains is at first separated in U.S. Lehrer laboratory from the rabbit pulmonary macrophage, mainly is present in the Paneth cell of Mammals neutrophil leucocyte, scavenger cell and animal small intestine; Beta-alexin is at first found in the tracheal mucosa epithelial cell of ox, about 38～42 amino-acid residues of size, and by the beta sheet structure that three disulfide linkage are connected to form, the site of three disulfide linkage is respectively 1 and 5,2 and 4; 3 and 6, mainly be present in the epithelial cells such as mammalian skin, mucous membrane; θ-alexin is the novel alexin of a kind of structure circlewise of separating from the white corpuscle of macaque, is made up of 18 amino acid.Cathelicidins is another big class antibacterial peptide in the Mammals, is to be separated to from the white corpuscle of pig at first.This class peptide is not stored in the secretory granules of neutrophil leucocyte there to be active precursor forms, is subjected to cytositimulation and discharges by proteolysis, extensively is present among the neutrophil(e) cell of pig, sheep, horse, ox, cavy, rabbit and goat.Another family of Mammals antibacterial peptide is histatins, is isolated one group of little cationic peptide that is rich in Histidine from people's saliva, and relative molecular mass is 3000～4000.They have the activity of fungicidal and bacterium, only are found at present in human and the Old World monkey (Macaca fascicularis).
Antibacterial peptide is to the general not damaged of Mammals normal cell, but most of anti-mattress peptides (the anti-mattress peptide of minority even under lower concentration) under high density have hemolytic action, thereby the Mammals normal cell is also had certain toxicity.Hemolytic action is relevant with hydrophobic residue content, high more then often hemolytic action is strong more for hydrophobic residue content in the peptide molecule, the existence of antibacterial peptide hemolytic activity is the important factor that hinders its application, research from now on will guarantee to eliminate its hemolytic activity on the basis of antibacterial peptide anti-microbial activity, can really promote the application of antibacterial peptide at aspects such as medicine, food.
At present, do not see the research report of the isolation identification of carrying out antibacterial peptide in the cow blood oxyphorase as yet.
Summary of the invention
The technical problem to be solved in the present invention provides a kind ofly isolatedly from cow blood has an active antibacterial peptide of anti-gram-positive bacteria, gram-negative bacteria and pathogenic fungi, measured its aminoacid sequence, and provided this antibacterial peptide separating and purifying method, and indicated its purposes.
Isolated antibacterial peptide in a kind of cow blood has following aminoacid sequence:
Asn-Glu-Phe-Thr-Pro-Val-Leu-Gln-Ala-Asp-Phe-Gln-Lys-Val-Val-Ala-Gly-Val-Ala-Asn-Ala-Leu-Ala-His-Lys, its molecular weight are 2668.03, and iso-electric point pI is 7.15.
The preparation method of described antimicrobial polypeptide is as follows:
(1) collection of blood is collected the blood of healthy cow down in the test tube that contains heparin with the processing aseptic condition, use 0.9% sterile saline Washed Red Blood Cells immediately 2～4 times, use 0.83% chloride leach solution red corpuscle again, behind centrifugal removal white corpuscle under 4 ℃, the solution that will contain the protoheme polypeptide dissolves with 0.01% acetate after freeze-drying again;
(2) haemachrome solution that will slightly carry of the purifying of antibacterial peptide passes through ion exchange column, cationic compound is in conjunction with on the resin anion(R.A), with 25mM ammonium acetate solution flush away non-cationic molecule, again with 10% acetic acid solution wash-out cationic molecule, and collect this elutriant, the elute soln of collecting is poured in the cationic exchange pillar with the speed of 20mL/h, is monitoring its absorbancy in 230nm place with the twin-beam ultraviolet-visible pectrophotometer at wavelength, collect elution peak, freeze-drying, resuspended with 0.01% acetate, 30～35% acetonitriles and 0.1% trifluoroacetic acid with gradient distribution on RPLC carry out, collect the peptide at 215nm place respectively, 0.01% acetate dissolution is used in freeze-drying.
Antibacterial peptide of the present invention also can carry out synthetic according to the correlative coding sequence, and its preparation method can be a mechanochemical method, also the encoding gene of antibacterial peptide can be cloned on the carrier, expresses the back then and obtain in host cell.Wherein expression vector can be a kind of in plasmid or the virus; host cell can be a prokaryotic cell prokaryocyte; comprise intestinal bacteria, subtilis etc., host cell can be eukaryotic cell also, comprise yeast cell, vegetable cell, insect cell and mammalian cell etc.The antibacterial peptide of preparation can be identified by mass spectrum.
Described antibacterial peptide can be used for preparation treatment gram-positive microorganism, Gram-negative bacteria, fungi or medicine for treating viral infections.
Described medicine contains the appeal antibacterial peptide, and is mixed with one or more pharmaceutically acceptable carrier and/or additives.
Described antibacterial peptide also can be used as fodder additives or foodstuff additive.
The beneficial effect that the present invention had:
(1) has a broad antifungal spectrum all has anti-microbial effect efficiently to G+, G-bacterium and fungi; (2) sterilization is quick; (3) Gao Du selectivity, prokaryotic cell prokaryocyte, tumour cell are different with normal eukaryotic cell membrane structure, and antibacterial peptide can selectively act on prokaryotic cell prokaryocyte, tumour cell, and not obvious to Normocellular effect; (4) do not produce resistance; (5) no teratogenesis.
The present invention has isolated antibacterial peptide first from cow blood, except that the general character with general antibacterial peptide, also have following characteristics:
(1) compare with the antimicrobial polypeptide in other sources, simple in structure, synthetic convenience that this antimicrobial polypeptide has is applied to the Mammals no antigen;
(2) antibacterial peptide of the present invention is located away from the red corpuscle of cow blood, and red corpuscle is one of animal blood composition, participate in the blood circulation process, there is not hemolytic toxicity, or the hemolysis rate value is extremely low, has the resistance of not producing, no teratogenesis, the difficult biological characteristics that produces some safe without toxic side effect such as accumulate poisoning.
Description of drawings
Fig. 1 is for carrying out the figure as a result of ion exchange chromatography to crude extract;
Fig. 2 is for carrying out the figure as a result of RP-HPLC to Fig. 1 middle-jiao yang, function of the spleen and stomach quasi-molecular ions;
Fig. 3 is to the mass spectrometric detection of antibacterial peptide of the present invention figure as a result.
Embodiment
Embodiment 1: the collection of blood and processing
After healthy cow is butchered, by aseptic method with its blood collecting in the test tube that contains heparin (15IU/ml), place ice bath, in 1h, deliver to the laboratory, use 0.9% sterile saline Washed Red Blood Cells immediately 3 times, use 0.83% chloride leach solution red corpuscle (volume ratio is 3: 1) again.After 4 ℃ of centrifugal 15min of 700 * g removed white corpuscle, the solution that will contain the protoheme polypeptide dissolved with 0.01% acetate after freeze-drying again.
Embodiment 2: the purifying of antibacterial peptide
With ion-exchange chromatography (reversible adsorption of cationic peptide, and negative ion fixed ion exchange column) haemachrome solution of slightly carrying is separated wherein antibacterial peptide.The sample of slightly carrying is passed through ion exchange column.Cationic compound is in conjunction with on the resin anion(R.A), by 25mM ammonium acetate flush away non-cationic molecule, again by 10% acetate wash-out cationic molecule.The solution of collecting is poured in the pillar with the speed of 20mL/h, is monitoring its absorbancy in 230nm place with the twin-beam ultraviolet-visible pectrophotometer at wavelength.Collect elution peak 5mL/ peak respectively), freeze-drying, resuspended with 0.01% acetate.The result has 4 peaks after separating, and E1 is the negatively charged ion peak, and E2, E3 and E4 are the positively charged ion peak, referring to Fig. 1, detects (method of embodiment 3) through anti-microbial activity, find that peak liquid E1 does not have antibiotic activity, and peak liquid E2, E3 and E4 has anti-microbial activity.
Peak liquid E2, E3 and E4 are mixed the back separate activated peptide with RPLC (RP-HPLC).With 30～35% acetonitriles of gradient distribution and 0.1% trifluoroacetic acid at Jupiter (5U C18
) carry out on the separator column, collect the peptide at 215nm place respectively, 0.01% acetate dissolution is used in freeze-drying.After the separation, have 7 peaks,, detect the anti-microbial activity of 7 peak liquid respectively referring to Fig. 2.
Embodiment 3: anti-microbial activity detects
Measure the antimicrobial acivity (strain subject is streptococcus aureus NCTC 4163, intestinal bacteria O111 and Candida albicans 3135A) of ion exchange method and reversed-phased high performace liquid chromatographic isolated peptides with dull and stereotyped diffusion process.
Tried microorganism with above-mentioned 3 kinds and be coated on lower floor's nutrient agar (10mL trypticase soybean broth (for Cole-Parmer company product) that disinfectant contains nutritive substance, the hyperpure agar of 10g (Sigma A-6013), 1L distilled water, pH 7.4) on, with punch tool punching, the about 2mm in aperture, spirit lamp are after heat is carried out back cover a little, add the specimen 5 μ L that concentration is 0.8 μ g/ml with pipettor in every hole, each flat board comprises positive control and negative control.Positive control adopts general microbiotic: AEROSPORIN is at gram-negative bacteria, and nisin (nisin) is at gram positive organism, and nysfungin is at yeast.Negative control adopts 0.01% acetic acid, because use its sample dissolution.Flat board is left standstill 1h, so that test fluid diffuses in the agar.Then, add one deck nutrient agar (about 50 ℃, nutritive ingredient is with lower floor's substratum) again.Dull and stereotyped 37 ℃ of overnight incubation, second day morning, the diameter of the transparent circle of register hole periphery.
4 peak liquid that ion exchange method obtains are after anti-microbial activity detects, and only the positively charged ion peak has stronger anti-microbial activity (referring to table 1).7 peak liquid after the HPLC separation are carried out anti-microbial activity detect, find that the peak is tried microorganism for 4 pairs 3 kinds and has stronger anti-microbial activity (referring to table 2).Therefore, peak 4 contained antibacterial peptides (being antibacterial peptide of the present invention) are expected aspect treatment animal bacteria disease and the fungal disease good application prospects is being arranged.According to the general characteristic of known antibacterial peptide, peak 4 contained antibacterial peptides also have certain application potential at the application and the aspects such as feedstuff mildew and milk preservation of antibacterials.
Table 1 ion exchange method is slightly carried the anti-microbial activity unit of peptide: mm
The anti-microbial activity unit of table 2RP-HPLC purified peptide: mm
Embodiment 4: mass spectroscopy
Analyze the molecular weight size of purified peptide by ground substance assistant laser desorption ionization flight time mass spectrum.Get 0.5 μ L peak, 4 samples (50 μ L gross samples, HPLC handles) and 0.5 μ L matrix (10mg/mL α-cyanogen-4-hydroxy-cinnamic acid is with 0.1% trifluoroacetic acid and the preparation of 60% acetonitrile) and place on the stainless steel substrates, make it at room temperature dry.When positively charged ion utmost point fluorescence excitation threshold value, collect data with the homoiotherm analyser.Under interior gauged indication, because of the ionizing event of electrospray, sample (preceding sample is carried out dilution in 1: 1 with 50%MeCN) directly injects mass spectrograph (using the electrospray ionization probe) with the speed of 3 μ L/min, and injection electric is set in 5kV, sheath gas (N
2) set about 33 units, capillary temperature is at 220 ℃.Collect data by a series of scanning, produce the spectral value of observing after data are averaged.
The result the molecular weight of isolating antibacterial peptide be 2668.03, aminoacid sequence is: Asn-Glu-Phe-Thr-Pro-Val-Leu-Gln-Ala-Asp-Phe-Gln-Lys-Val-Val-Ala-Gly-Val-Ala-Asn-Ala-Leu-Ala-His-Lys.
Embodiment 5: the iso-electric point analysis
Open EditSeq in the DNAStar software, open file, click in " new " " new protien ", import aminoacid sequence, can obtain the data of iso-electric point.The iso-electric point of this isolated peptides is 7.15.
SEQUENCE?LISTING
＜110〉Henan Science and Technology College
＜120〉isolated antibacterial peptide and encoding sequence thereof and purposes in the cow blood
＜130〉progress of natural anti-mattress peptide and application prospect
<160>1
<170>PatentIn?version?3.5
<210>1
<211>25
<212>PRT
＜213〉milk cow
<400>1
Asn?Glu?Phe?Thr?Pro?Val?Leu?Gln?Ala?Asp?Phe?Gln?Lys?Val?Val?Ala
1 5 10 15
Gly?Val?Ala?Asn?Ala?Leu?Ala?His?Lys
20 25
Claims (5)
1. isolated antibacterial peptide in the cow blood is characterized in that the aminoacid sequence of described antibacterial peptide is as follows:
Asn-Glu-Phe-Thr-Pro-Val-Leu-Gln-Ala-Asp-Phe-Gln-Lys-Val-Val-Ala-Gly-Val-Ala-Asn-Ala-Leu-Ala-His-Lys，
Its molecular weight is 2668.03, and iso-electric point pI is 7.15.
2. the preparation method of the described antimicrobial polypeptide of claim 1 is characterized in that, this method may further comprise the steps:
(1) collection of blood and processing: aseptic condition is collected the blood of healthy cow down in the test tube that contains heparin, use 0.9% sterile saline Washed Red Blood Cells immediately 2～4 times, use 0.83% chloride leach solution red corpuscle again, behind centrifugal removal white corpuscle under 4 ℃, the solution that will contain the protoheme polypeptide dissolves with 0.01% acetate after freeze-drying again;
(2) purifying of antibacterial peptide: will go up the step and pass through ion exchange column with the solution that contains the protoheme polypeptide that 0.01% acetic acid solution dissolves gained, cationic compound is combined on the resin anion(R.A), with 25mM ammonium acetate solution flush away non-cationic molecule, again with acetic acid solution wash-out cationic molecule, and collect this elutriant, the elute soln of collecting is slowly fed in the cationic exchange pillar, is monitoring its absorbancy in 230nm place with the twin-beam ultraviolet-visible pectrophotometer at wavelength, collect the positively charged ion elution peak, freeze-drying, it is resuspended with 0.01% acetate to mix the back, 30～35% acetonitriles with gradient distribution on RPLC separate with 0.1% trifluoroacetic acid, collect the pairing solution in peak of the 4th appearance, freeze-drying is dissolved with 0.01% acetate.
3. the purposes of antibacterial peptide according to claim 1 is characterized in that, the application of described antibacterial peptide in the medicine of preparation treatment streptococcus aureus, intestinal bacteria, candida albicans infection.
4. according to the application of the described antibacterial peptide of claim 3, it is characterized in that described medicine comprises the antibacterial peptide in the claim 1, and be mixed with one or more pharmaceutically acceptable carrier and/or additives.
5. the purposes of an antibacterial peptide as claimed in claim 1 is characterized in that, the application of described antibacterial peptide in preparation fodder additives or foodstuff additive.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107298706A (en) * | 2017-07-31 | 2017-10-27 | 河南科技学院 | A kind of holstein cow spleen derived antimicrobial peptide and preparation method and application |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102524558B (en) * | 2010-12-27 | 2013-07-31 | 内蒙古伊利实业集团股份有限公司 | Feed additive for treating dairy cattle recessive mastitis |
| CN107652359B (en) * | 2017-10-19 | 2018-11-27 | 浙江大学 | Antibacterial peptide KR-32 and application thereof |
| CN108264539B (en) * | 2017-12-28 | 2020-12-25 | 河南科技学院 | Antibacterial peptide RL-18 and application thereof |
| CN109060688A (en) * | 2018-08-27 | 2018-12-21 | 南京采薇且歌信息科技有限公司 | A kind of high-precision nano-sensor and its application |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1216768A (en) * | 1998-10-29 | 1999-05-19 | 吉林大学 | Biologic antibiotic peptide, and method for preparing same |
| CN1360833A (en) * | 2000-12-29 | 2002-07-31 | 中国农业大学 | Prepn for earthworm antibacterial peptide |
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2009
- 2009-07-27 CN CN2009100655479A patent/CN101607992B/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1216768A (en) * | 1998-10-29 | 1999-05-19 | 吉林大学 | Biologic antibiotic peptide, and method for preparing same |
| CN1360833A (en) * | 2000-12-29 | 2002-07-31 | 中国农业大学 | Prepn for earthworm antibacterial peptide |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107298706A (en) * | 2017-07-31 | 2017-10-27 | 河南科技学院 | A kind of holstein cow spleen derived antimicrobial peptide and preparation method and application |
| CN107298706B (en) * | 2017-07-31 | 2020-05-08 | 河南科技学院 | Spleen-derived antibacterial peptide of Holstein cow, and preparation method and application thereof |
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