CN105175525A - Hylarana guentheri antibacterial peptide and application thereof - Google Patents
Hylarana guentheri antibacterial peptide and application thereof Download PDFInfo
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- CN105175525A CN105175525A CN201510682141.0A CN201510682141A CN105175525A CN 105175525 A CN105175525 A CN 105175525A CN 201510682141 A CN201510682141 A CN 201510682141A CN 105175525 A CN105175525 A CN 105175525A
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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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/463—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from amphibians
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations 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
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/10—Peptides having 12 to 20 amino acids
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- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
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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 relates to sequences, a preparation method and application of two types of hylarana guentheri antibacterial peptides. The two types of antibacterial peptides are separated from skin secreta of hylarana guentheri, and antibacterial and hemolytic activities of the antibacterial peptides are detected; a secondary structure of the antibacterial peptides under a simulated film environment is researched. The two antibacterial peptides are obtained: the antibacterial peptide A with an amino acid sequence shown as SEQ ID NO.1; the antibacterial peptide B with an amino acid sequence shown as SEQ ID NO.2. The antibacterial peptide A provided by the invention has an inhibition effect on staphylococcus aureus, colon bacillus and bacillus subtilis; the antibacterial peptide B has a very good sterilization effect on the bacillus subtilis and the staphylococcus aureus. The two types of antibacterial peptides, provided by the invention, have the characteristics of novel structure, strong antibacterial activities and the like, and have an important value in the aspects of medicine development and application. The sequences, the preparation method and the application of two types of the hylarana guentheri antibacterial peptides have important meanings on researches of an antibacterial mechanism of the antibacterial peptides, and further improvement, and development and utilization of the antibacterial peptides.
Description
Technical field
The present invention relates to two kinds of natural antibacterial peptides and the application in pharmacy field thereof, belong to biomedical sector.
Background technology
Antibacterial peptide makes it have important theoretical investigation and drug development using value due to its broad spectrum antibiotic activity and special antimicrobial mechanism.Amphibians skin can secrete a large amount of antibacterial peptides to resist the invasion and attack of external microorganism, from investigator finds first Amphibians antibacterial peptide magainins from Africa xenopus skin secretion, had thousands of kinds of antibacterial peptides to be obtained by separation and purification or gene clone method from Amphibians skin secretion, these antibacterial peptides are generally by 10-50 Amino acid profile.Be divided into individual different family more than 100 according to the aminoacid sequence of antibacterial peptide, the antibacterial peptide of these different families is not identical on molecular size range, electric charge, hydrophobicity, structure and function.By the research of the structure and function to these antibacterial peptides, not only obtain many polypeptide with the germicidal action of broad-spectrum high efficacy, but also improve many natural antibacterial peptides.
There is significant difference in the Amphibians antibacterial peptide of different sources, can be divided into alpha-helix antibacterial peptide, beta sheet antibacterial peptide, random coil antibacterial peptide and extended pattern antibacterial peptide according to second structure characteristic on amino acid composition and sequence.Investigator is found by circular dichroism spectrum research, and many antibacterial peptides, as derived from
xenopuslaevismagainin2, derive from
rananigromaculatatemporin-1RNa, temporin-1RNb etc. spontaneously can be folded into amphipathic α-helixstructure at antibacterial peptide under analog cell membrane environment.These antibacterial peptides are combined by the phospholipid bilayer of electrostatic interaction on bacterial cell membrane, under cell-membrane environment, be folded into amphipathic α-helixstructure, thus destroy cell membrane integrity, cause dissolution of cellular content and cause necrocytosis.Along with the further investigation to antibacterial peptide structure-function relationship, the medical value of antibacterial peptide is obvious all the more, and studied person is called " peptide antibiotics ".Current exploitation anti-microbial activity is strong, and toxic side effect is little, and the simple antibacterial peptide of structure has become a urgent task.
Guenther's frog (
hylaranaguentheri) be the common Amphibians in SOUTHERN CHINA area, containing multiple antibacterial peptide in its skin secretion.There are some researches show, ranid at least needs 20-30 kind antibacterial peptide could form good antibacterial barrier, and the Guenther's frog antibacterial peptide reported at present has 9, belong to brevinin, temporin and guentherin family respectively, still have many Guenther's frog antibacterial skin peptides undiscovered.The separation and purification of Guenther's frog antibacterial skin peptide and anti-microbial activity research also need further reinforcement.
Summary of the invention
The object of the invention is to provide two kinds and prepares simple, the Guenther's frog antibacterial peptide that bacteriostatic activity is strong, and the manufacture and exploit that this antibacterial peptide can be applied to antimicrobial DP finish.
A kind of Guenther's frog antibacterial peptide, described cecropin A is by 29 Amino acid profiles, and sequence is that two halfcystines of SEQIDNO.1:FLQHIIGALSKIFLVSIDKVRCKVAGGCN, C end form a pair disulfide linkage.
A kind of Guenther's frog antibacterial peptide, described cecropin B gene is by 18 Amino acid profiles, and sequence is SEQIDNO.2:FFPLIFGALSKILPKIFL, C-terminal amidation.
Antibacterial peptide of the present invention comprises the polypeptide with antibacterial peptide described in SEQIDNO.1 or SEQIDNO.2 with 80% or more homology, and described in this polypeptide function and SEQIDNO.1 or SEQIDNO.2, antibacterial peptide is same or similar.
Another object of the present invention is to provide a kind of polypeptide fragment, comprises polypeptide or homologous polypeptide that sequence is SEQIDNO.1 or SEQIDNO.2.This polypeptide fragment and sequence are that the antibacterial peptide function of SEQIDNO.1 or SEQIDNO.2 is same or similar.
Described cecropin A has broad spectrum antibiotic activity, have high inhibition effect, and cecropin B gene is remarkably productive to gram-positive microorganism to gram-positive microorganism and Gram-negative bacteria.Compared with its minimal inhibitory concentration, the hemolytic of cecropin A and B is all lower, shows that they have important value in antibacterials development and application.The restraining effect of above-mentioned antibacterial peptide to bacterium is shown in embodiment 3, and hemolytic activity the results are shown in embodiment 4.
Antibacterial peptide of the present invention forms α-helixstructure in hydrophobic environment.Circular dichroism spectrum (CD) is utilized to measure antibacterial peptide at different concns trifluoroethanol (2,2,2-Trifluoroethanol, TFE, analog cell film hydrophobic environment) in secondary structure, result show the α-helixstructure content of cecropin A and B along with TFE concentration improve and increase.The antifungal mechanism of this constitutional features to research antibacterial peptide is significant.
The spiral colyliform map analysis of antibacterial peptide of the present invention is known, and the analogue that cecropin A or the B obtained was replaced, and lacked or modified to the hydrophobic surface of this antibacterial peptide or the corresponding amino acid of hydrophilic surface all may have same or analogous activity with former antibacterial peptide.
In view of character and the function of above-mentioned antibacterial peptide, those of ordinary skill in the art can with this antibacterial peptide for template, by changing the sequence pair Guenther's frog antibacterial peptide directional transformation of this antibacterial peptide or synthesizing its derivative to improve its anti-microbial activity, for medicament research and development and clinical treatment.
Accompanying drawing explanation
Fig. 1: Guenther's frog skin secretion SephedexG-50 gel filtration chromatography figure.
Fig. 2: the restraining effect of gel filtration chromatography discrete group swarming 1 and 2 pairs, peak intestinal bacteria (A) and streptococcus aureus (B).
Fig. 3: the RPLC figure of gel chromatography wash-out peak-to-peak 1.
Fig. 4: Guenther's frog cecropin A and the circular dichroism spectrum of B in different concns TFE solution.
Fig. 5: the spiral colyliform figure (A) of Guenther's frog cecropin A and the spiral colyliform figure (B) of cecropin B gene.
Embodiment
The present embodiment is implemented under premised on technical solution of the present invention, gives detailed embodiment and process, but protection scope of the present invention is not limited only to following embodiment.
embodiment 1
The separation and purification of antibacterial peptide of the present invention comprises SephadexG-50 gel filtration chromatography and RPLC (RP-HPLC) two steps.
Extract Guenther's frog skin secretion: adult Guenther's frog, deionized water is cleaned, and commercially available 9V dc-battery electric shock Guenther's frog ear rear gland and the flourishing partial skin of back body of gland, treat that experimental subjects skin surface produces a large amount of secretory product, with containing 0.05%(
v/V) trifluoroacetic acid deionized water rinsing and collect secretory product, the centrifugal 15min of 12000rpm, gets supernatant liquor lyophilize ,-80 DEG C of cryopreservation.
SephadexG-50 gel filtration chromatography: obtain Guenther's frog skin secretion lyophilized powder as stated above, be dissolved in deionized water, the centrifugal 15min of 12000rpm.Get supernatant liquor with after 0.22 μm of aperture micro-filtrate membrane filtration, be loaded to the SephadexG-50 gel column (1.6cm × 100cm) with deionized water balance.Use deionized water wash-out, flow velocity 0.3mL/min, detect elutriant light absorption value in 214nm wavelength place, draw elution curve, obtain two wash-out peak-to-peaks 1 and peak 2, as shown in Figure 1.Collect elution peak, lyophilize, carries out Determination of Antibacterial Activity.
Reverse high performance liquid chromatography: deionized water dissolving above-mentioned peak 1 lyophilized powder, adopts RPLC to be separated further.Liquid chromatographic system is LC-20A, assembling Gemini5 μ C18(250mm × 10mm) reversed-phase column (Phenomenex, UK), with containing 0.05%(
v/V) the water of trifluoroacetic acid and the elution system that forms of acetonitrile solution carry out gradient elution.Gradient: 0 ~ 5min, 0 ~ 20% acetonitrile; 5 ~ 40min, 20% ~ 70% acetonitrile; Elution flow rate 1.0mL/min, determined wavelength 214nm, elution curve as shown in Figure 3.Collect all elution peaks, measure anti-microbial activity.
Collect the component with stronger anti-microbial activity, lyophilize, check order with automatic Protein Sequencer, obtain the sequence (SEQID:NO.2) of cecropin A (SEQID:NO.1) and cecropin B gene.
embodiment 2
Agar coating method detects the bacteriostatic activity of gel filtration chromatography separated portion:
Bacterial classification intestinal bacteria (EscherichiacoliATCC8099) used and streptococcus aureus (StaphylococcusaureusCMCC26003) are for preserving this room.Concrete operations are as follows: choose single colony inoculation in beef extract-peptone liquid nutrient medium, and (37 DEG C, 130rpm) are cultivated in jolting of spending the night, and be inoculated in 20mL beef extract-peptone liquid nutrient medium by 200 μ L incubated overnight bacterium liquid, jolting cultivates 4 hours.Cultured bacteria suspension dilutes 1000 times, gets 100 μ L and adds slat chain conveyor primary surface, and coating evenly.Uniformly stick at the plate culture medium of coated bacterium liquid the circular filter paper sheet that diameter is 5mm, each filter paper adds 10 μ L testing samples.Gentamicin is as positive control, and sterilized water does negative control.The flat-plate inverted adding sample is placed in 37 DEG C of constant incubators and cultivates 18 ~ 20h, experimental result as shown in Figure 2.Obvious inhibition zone is there is around the filter paper of the sample (being labeled as " 1 ") of interpolation gentamicin (being labeled as "+") and SephadexG-50 gel chromatography separation component F1, and add the filter paper surrounding bacterial normal growth of the sample (being labeled as " 2 ") of sterilized water (being labeled as "-") and SephadexG-50 gel chromatography separation component F2, show that SephadexG-50 gel chromatography component F1 has obvious restraining effect to intestinal bacteria (Fig. 2 A) and streptococcus aureus (Fig. 2 B), adopt high performance liquid chromatography to be separated further.
embodiment 3
Liquid growth is utilized to suppress method to detect the suppression vigor of polypeptide of the present invention to bacterium:
The present embodiment antibacterial peptide used is synthesized according to sequence SEQIDNO.1 and sequence SEQIDNO.2 by the biochemical company limited of Shanghai gill, and the antibacterial peptide of synthesis keeps original modification, and wherein the C of cecropin A holds halfcystine to form disulfide linkage, and the C of cecropin B gene holds amidation.Two synthetic peptide purity are all not less than 95%.Adopt 96 well plate method working samples minimal inhibitory concentration (minimalinhibitoryconcentration, MIC), concrete operations are as follows:
Bacterial classification is recovered, and inoculation 37 DEG C, inclined-plane overnight incubation, chooses single colony inoculation in common LB substratum, 37 DEG C of overnight incubation, and dilution bacterium liquid makes bacteria concentration be 10
4-10
5cFU/mL, is inoculated in 96 orifice plates by every hole 100 μ L bacterium liquid, adds 10 μ L with the polypeptide after certain proportion dilution, 96 orifice plates is placed in 37 DEG C of incubated overnight, detects the light absorption value of 630nm wavelength, the results are shown in Table one by microplate reader.
Bacterial growth concentration (OD containing antibacterial peptide
630) antibacterial peptide concentration when being greater than 90% with the ratio of bacterial growth concentration not adding antibacterial peptide is minimal inhibitory concentration (being defined as the minimum concentration of remarkable bacteria growing inhibiting).
From detected result, cecropin A and the minimal inhibitory concentration of cecropin B gene to common bacterium all reach Gamma Magnitude, have extremely strong Antibacterial Activity.The killing action of cecropin B gene to gram-positive microorganism is particularly evident.
Table one: the minimal inhibitory concentration of Guenther's frog antibacterial peptide
Note: "-" expression does not find there is restraining effect to this bacterium when antibacterial peptide concentration reaches 250 μ g/mL
embodiment 4
The present embodiment gets blood by pulling out eyeball of mouse, measures hemolytic activity.
Be separated erythrocyte after getting blood: the blood be collected and antithrombotics fully mix, the centrifugal 3min of 3000rpm, remove supernatant liquor.Lower floor's erythrocyte physiological saline is resuspended, recentrifuge, repeats above-mentioned steps, until supernatant liquor no longer takes on a red color (processing 4 ~ 5 times).Finally use phosphate buffered saline buffer (10mM, pH7.4) that precipitation is mixed with 5%(compression volume) red blood cell solution for subsequent use.
Working sample hemolytic activity: antibacterial peptide is dissolved with phosphate buffered saline buffer, be mixed with the sample solution that concentration is 500 μ g/mL, each centrifuge tube adds the red blood cell solution that 450 μ L prepare, add 50 μ L sample solutions, be placed in after 37 DEG C of thermostat containers react 30min, the centrifugal 3min of 3000rpm, gets supernatant liquor and measures light absorption value in 540nm wavelength place.Take physiological saline as blank, 1%(
v/V) TritonX-100 as positive control, hemolysis rate is according to formulae discovery below.
in formula: A
0the light absorption value of positive controls; A
1the light absorption value of sample sets
After measured, the hemolysis rate of Guenther's frog cecropin A when 125 μ g/mL is only 14%, and hemolysis rate is lower.The hemolysis rate of cecropin B gene when concentration is 15.6 μ g/mL is 11%, and hemolysis rate when concentration is 31.3 μ g/mL reaches 24%.Compared with cecropin A, the hemolysis rate of cecropin B gene is higher, but due to its activity comparatively strong, compared with its minimal inhibitory concentration, its hemolytic is relatively weak.The above results shows that cecropin A and B have the value as prodrug development and utilization.
embodiment 5
At room temperature, the constitutional features of cecropin A and the extreme ultraviolet of B in different concns trifluoroethanol (TFE) aqueous solution (5%, 10%, 20%, 30%, 50%, 100%) is measured with J-810 circular dichroism spectrometer.Sample pool optical path 1mm, sweep velocity is 500nm/min, and sweep limit is 190-260nm, and the wavelength interval of scanning is 1nm, and continuous sweep is averaged for three times, and the same solution beyond removing antibacterial peptide is as baseline deduction.
Known (Fig. 4) is measured through circular dichroism spectrum, when TFE concentration is less than 20%, the circular dichroism spectrum of cecropin A absorbs weak, only there is a negative peak (Fig. 4 A) in 194nm vicinity, cecropin B gene, at the negative peak of 194nm more obvious (Fig. 4 B), shows the cecropin A in now solution and B mainly random coil structure; When TFE concentration higher than 20% time, at 194nm wavelength there is obvious posivtive spike in place, 208nm and 222nm wavelength location all occurs negative peak, is typical α-helixstructure characteristic absorbance.Along with the raising of TFE concentration, negative peak influx and translocation, shows that, when TFE strength of solution is greater than 20%, cecropin A and B can be folded into α-helixstructure from random coil structure.Above-mentioned example shows that Guenther's frog cecropin A and B may act on cytolemma.
embodiment 6
For studying the secondary structure of Guenther's frog antibacterial peptide further, the complete sequence of cecropin A sequence (F1-R21) and cecropin B gene is depicted as alpha-helix colyliform figure, this figure folds rule according to the alpha-helix of polypeptide and draws.Grey bead is hydrophobic amino acid, and white globules is hydrophilic amino acid.
As shown in Figure 5A, in the spirane structure of cecropin A, hydrophobic amino acid and hydrophilic amino acid all occupy certain proportion, are gathered in spirane structure both sides respectively, and forming hydrophilic surface and hydrophobic surface, is amphipathic spirane structure.Due to cecropin A band+3 electric charge, it can be adsorbed onto electronegative bacterial cell membrane surface, under the hydrophobic environment of cytolemma by electrostatic interaction, this antibacterial peptide is folded into amphipathic α-helixstructure, thus forms transmembrane channel, destroys cytolemma, kill bacterium, play anti-microbial effect.The hydrophobic amino acid ratio of cecropin B gene is higher, does not form obvious hydrophobic surface and hydrophilic surface (Fig. 5 B).But this antibacterial peptide can be folded into α-helixstructure equally under analogue membrane environment, and with+2 electric charges, thus its action site is also cytolemma, identical with the mechanism of action of cecropin A.
The research of antibacterial peptide structure activity relationship is significant, plays directive function for engineer's novel antibacterial peptide molecule.The special acid of antibacterial peptide, spirane structure, positive charge and the activity of hydrophobicity to antibacterial peptide are most important.According to the structure activity relationship of antibacterial peptide, if by the aminoacid replacement of Guenther's frog antibacterial peptide correspondence position, its anti-microbial activity may be improved or reduce its hemolytic, there is important Research Significance.
The foregoing is only preferred embodiment of the present invention, all equalizations done according to the present patent application the scope of the claims change and modify, and all should belong to covering scope of the present invention.
SEQUENCELISTING
<110> University of Fuzhou
<120> Guenther's frog antibacterial peptide and application thereof
<130>2
<160>2
<170>PatentInversion3.3
<210>1
<211>29
<212>PRT
<213> cecropin A
<400>1
PheLeuGlnHisIleIleGlyAlaLeuSerLysIlePheLeuValSer
151015
IleAspLysValArgCysLysValAlaGlyGlyCysAsn
2025
<210>2
<211>18
<212>PRT
<213> cecropin B gene
<400>2
PhePheProLeuIlePheGlyAlaLeuSerLysIleLeuProLysIle
151015
PheLeu
Claims (4)
1. a Guenther's frog antibacterial peptide, is characterized in that: described cecropin A aminoacid sequence is that two halfcystines of SEQIDNO.1:FLQHIIGALSKIFLVSIDKVRCKVAGGCN, C end form a pair disulfide linkage.
2. an a kind of Guenther's frog antibacterial peptide as claimed in claim 1, is characterized in that: described sequence and SEQIDNO.1 have the polypeptide of 80% and above homology, this polypeptide function and SEQIDNO.1 same or similar.
3. an a kind of Guenther's frog antibacterial peptide as claimed in claim 1 or 2, is characterized in that: the front end of described antibacterial peptide sequence, middle-end or end comprise antibacterial peptide described in claim 2, and this polypeptide is identical or similar with antibacterial peptide function described in claim 2.
4. the application of a kind of Guenther's frog antibacterial peptide as claimed in claim 1 or 2 in antibacterials exploitation.
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| CN201510682141.0A CN105175525B (en) | 2014-04-25 | 2014-04-25 | Guenther's frog antibacterial peptide and its application |
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| CN201510682141.0A CN105175525B (en) | 2014-04-25 | 2014-04-25 | Guenther's frog antibacterial peptide and its application |
| CN201410170141.8A CN103965340B (en) | 2014-04-25 | 2014-04-25 | Guenther's frog antibacterial peptide and application thereof |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106496317A (en) * | 2016-11-08 | 2017-03-15 | 南方医科大学 | Guenther's frog secretion peptide and its gene and the application in pharmacy |
| CN109627312A (en) * | 2018-12-17 | 2019-04-16 | 江苏医药职业学院 | A kind of novel antimicrobial peptide and its application |
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111333716B (en) * | 2020-03-23 | 2021-12-21 | 集美大学 | Pseudosciaena crocea hemoglobin antibacterial peptide and application thereof |
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| CN103724416A (en) * | 2014-01-17 | 2014-04-16 | 福州大学 | hylarana guentheri antibacterial peptide as well as preparation and application thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN103724416A (en) * | 2014-01-17 | 2014-04-16 | 福州大学 | hylarana guentheri antibacterial peptide as well as preparation and application thereof |
Non-Patent Citations (2)
| Title |
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| 谢智等: "沼水蛙皮肤中抗菌肽的分离纯化与活性测定", 《福州大学学报(自然科学版)》 * |
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Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106496317A (en) * | 2016-11-08 | 2017-03-15 | 南方医科大学 | Guenther's frog secretion peptide and its gene and the application in pharmacy |
| CN106496317B (en) * | 2016-11-08 | 2019-12-20 | 南方医科大学 | Rana chensinensis secretory peptide, gene thereof and application thereof in pharmacy |
| CN109627312A (en) * | 2018-12-17 | 2019-04-16 | 江苏医药职业学院 | A kind of novel antimicrobial peptide and its application |
| CN109627312B (en) * | 2018-12-17 | 2021-11-05 | 江苏医药职业学院 | Novel 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 |
Also Published As
| Publication number | Publication date |
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| CN105175525B (en) | 2018-09-18 |
| CN103965340A (en) | 2014-08-06 |
| CN103965340B (en) | 2016-07-06 |
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