CN108752433A - The application of antimicrobial peptide CRAMP and its cyclic peptide in the drug for preparing bacteria removal biomembrane - Google Patents
The application of antimicrobial peptide CRAMP and its cyclic peptide in the drug for preparing bacteria removal biomembrane Download PDFInfo
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- CN108752433A CN108752433A CN201810701474.7A CN201810701474A CN108752433A CN 108752433 A CN108752433 A CN 108752433A CN 201810701474 A CN201810701474 A CN 201810701474A CN 108752433 A CN108752433 A CN 108752433A
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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
- C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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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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Abstract
The present invention relates to the application of antimicrobial peptide CRAMP and its cyclic peptide in the drug for preparing bacteria removal biomembrane, the amino acid sequence of antimicrobial peptide CRAMP is as shown in SEQ ID NO.1, and head and the tail are cyclized, obtain cyclic peptide CRAMP, it has been investigated that antimicrobial peptide CRAMP and its cyclic peptide have apparent scavenging effect, this research to have highly important scientific meaning and clinical medicine to be worth the ripe dispelling tactics of aeruginosa biofilm and its further investigation of mechanism pseudomonas aeruginosa biofilm.
Description
Technical field
The invention belongs to biomedicine fields, and in particular to antimicrobial peptide CRAMP and cyclic peptide and antimicrobial peptide
The application of CRAMP and cyclic peptide in the drug for preparing bacteria removal biomembrane.
Background technology
Bacterial biof iotalm (biofilm, BF) is multiple bacterial adhesions in abiotic or biological surface, secretion extracellular polymeric
(extracellular polymeric substances, EPS), and one kind that itself package is wherein formed is organized thin
Bacterium group, including polysaccharide, protein, extracellular dna and lipid etc., are an ecosystems with three-dimensional space structure.It is raw
The bacterium of object form membrane has the protection of EPS, can escape the attack of body immune system and the killing of antibacterials, drug resistance
Property enhancing, while biomembrane can also sustained release bacterium, cause infection recurrent exerbation and obstinate.It is reported that forming life
The bacterium of object film, which can show, is up to 1000 times of antibiotics resistance than flcating germ so that it is difficult that biomembrane is more easy to cause in clinic
The property controlled chronic infection seriously threatens human and animal's health.Therefore, it is a kind of to bacterial biof iotalm effect to be badly in need of searching, especially
To the bioactive substance of the effect of biofilm.
Invention content
In view of this, one of the objects of the present invention is to provide antimicrobial peptide CRAMP to prepare bacteria removal biomembrane
Drug in application；The second object of the present invention is that providing antimicrobial peptide CRAMP is preparing cystic fibrosis pneumonia
Application in drug；The third object of the present invention is that providing antimicrobial cyclic peptide CRAMP is preparing bacteria removal biomembrane
Application in drug；The fourth object of the present invention is that providing antimicrobial cyclic peptide CRAMP is preparing cystic fibrosis pneumonia
Application in drug.
For achieving the above object, the present invention provides the following technical solutions：
1. applications of the antimicrobial peptide CRAMP in the drug for preparing bacteria removal biomembrane, the antimicrobial peptide
The amino acid sequence of CRAMP is as shown in SEQ ID NO.1.
Preferably, the bacterium is pseudomonas aeruginosa.
2. applications of the antimicrobial peptide CRAMP in the drug for preparing cystic fibrosis pneumonia, the antimicrobial peptide
The amino acid sequence of CRAMP is as shown in SEQ ID NO.1.
3. applications of the antimicrobial cyclic peptide CRAMP in the drug for preparing bacterial biof iotalm bacteria removal biomembrane, described
The amino acid sequence of antimicrobial peptide CRAMP is as shown in SEQ ID NO.1.
Preferably, the bacterium is pseudomonas aeruginosa.
It is furthermore preferred that the effective dose concentration of the antimicrobial cyclic peptide CRAMP is more than 5 μM.
4. applications of the antimicrobial cyclic peptide CRAMP in the drug for preparing cystic fibrosis pneumonia, the antimicrobial ring
The amino acid sequence of Peptide C RAMP is as shown in SEQ ID NO.1.
Advantageous effect of the invention is：The present invention has synthesized antimicrobial peptide CRAMP and cyclic peptide, is found for the first time to verdigris vacation
Monad biofilm has apparent scavenging effect and inhibits to be formed, and is substantially better than control LL-37.Due in clinical medicine
The very high cystic fibrosis of lethality (Cystic fibrosis, CF) pneumonia, basic reason are exactly the life of pseudomonas aeruginosa maturation
Object film is difficult to clean off, so the research is treated to cystic fibrosis pneumonia and the dispelling tactics and machine of aeruginosa biofilm
The further investigation of system has highly important scientific meaning and clinical medicine value.
Description of the drawings
In order to keep the purpose of the present invention, technical solution and advantageous effect clearer, the present invention provides following attached drawing and carries out
Explanation：
Fig. 1 is CRAMP and LL-37 viable counts and biofilm biomass result (A：LL-37；B：CRAMP；Broken line：Biomembrane viable bacteria
Number；Block diagram：Biofilm biomass).
Fig. 2 is scavenging effect (broken lines of the cyclic peptide CRAMP to the wild type strain PAO1 biomembranes of pseudomonas aeruginosa：It is raw
Object film viable count；Block diagram：Biofilm biomass).
Fig. 3 is the active influences (antibacterial circle diameter, x ± SD, N=6) of different protease E.coli anti-on CRAMP
(Neutral protease：Neutral proteinase, Pepsase：Pepsin, Trypsase：Trypsase).
Specific implementation mode
Below in conjunction with attached drawing, the preferred embodiment of the present invention is described in detail.
Pseudomonas aeruginosa (Pseudomonas aeruginosa, P.a) is a kind of common conditioned pathogen, is capsule
The main pathogenic bacteria of lungs' chronic infections such as fibrosis (Cystic fibrosis, CF), and cause hypoimmunity body slow
The common causative of property repeated infection.The bacterium infects easy recurrent exerbation to a variety of common antibiotics drug resistances, it is difficult to remove, study carefully it
Reason mainly easily forms BF, and can cause widely to infect in animals and plants, is current known most species, has apparent
One of bacterium of ecological significance.Therefore the embodiment of the present invention is studied by taking pseudomonas aeruginosa as an example to the biologically active objects of BF
Matter.
Embodiment 1, the research of CRAMP antibacterium biomembranes
According to another report, LL-37 has the function of significantly inhibiting P.aeruginosa biofilm formations in vitro, while
Observe that LL-37 also has certain effect to the ripe P.aeruginosa biomembranes formed, but inhibition is limited, institute
To be badly in need of a kind of there is more effectively bioactive substance to bacterial biof iotalm.CRAMP(Cathelicidin Related
Antimicrobial Peptide) it is the testis for being present in vertebrate mouse, spleen, stomach, the bioactivity of the organs such as small intestine
Polypeptide.It is the Cathelicidin of one of mammal AMPs (Antimicrobial peptides) main two family members
In one kind, based on alpha-helix, amino acid sequence is structure：GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ(SEQ
ID NO.1).But the effect about CRAMP to bacterial biof iotalm at present especially yet there are no report to the effect of biofilm
Road.
Therefore biomembrane Inhibition test is carried out to P.aeruginosa with present invention selection CRAMP and LL-37, passes through crystallization
Purple decoration method and count plate observe viable count and biofilm biomass in biomembrane, and the results are shown in Figure 1.The results show that
CRAMP has apparent scavenging effect to biofilm, and is substantially better than control LL-37.
It is as follows that CRAMP methods are synthesized in the present embodiment：
Specific synthetic method is as follows：
Synthesis material：Resin is the (Tianjin 2-Chlorotrityl Chloride Resin that degree of substitution is 1.03mmol/g
Compositech Inc. of Nankai of city), amino acid be Fmoc-Phe-OH (the sincere promise in Chengdu,>99%), Fmoc-Arg (pbf)-OH
(the sincere promise in Chengdu,>99%), Fmoc-Ala-OH (the sincere promise in Chengdu,>99%) etc..
Synthetic agent：DMF (source area South Korea), DCM (source area South Korea), MEOH (source area Japan), (the new Dehua DIEA
Work, 99%), HBTU (vast and boundless sail biotechnology, 99%).
Deprotecting regent：Piperidines (Chinese medicines group Solution on Chemical Reagents in Shanghai company, 99%).
Detection reagent：Phenol reagent, pyridine reagent, ninhydrin reagent.
Lytic reagent：95% cutting liquid：TFA (J.T.Baker, 99%), TIS (Shanghai reach at auspicious fine chemistry industry, 98%),
EDT (Shanghai reach at auspicious fine chemistry industry, 98%), anhydrous ether (test, and actual measurement is 99.7%) by Shanghai.
Nitrogen：(newly joining gas).
Instrument：(the semi-automatic polypeptide of Shanghai Qiangyao Biotechnology Co., Ltd. closes 12 channel semi-automatic polypeptide synthesizers
Cheng Yi)；SHIMADZU high performance liquid chromatograph (models：Preparative, analytic type, software：Class-VP.Sevial System,
Manufacturer：SHIMADZU)；LABCONCO freeze dryer (models：Freezone.Plus.6, manufacturer：LABCONCO)；Centrifuge (Shanghai
Pacify pavilion scientific instrument factory model：TDL-40B)
Steps are as follows for Peptide systhesis：By taking polypeptide 04010029962 as an example, synthesis sequence：From C-terminal to N-terminal.
(1) resin swelling
2-Chlorotrityl Chloride Resin are put into reaction tube, DCM (15ml/g) is added, vibrate 30min；
(2) first amino acid is connect
Solvent is leached out by husky core, the Fmoc-Phe-OH amino acid of 3 times of molar excess is added, DMF dissolvings are added, then
The DIEA of 10 times of molar excess is added, vibrates 60min, is closed with methanol；
(3) it is deprotected
Remove DMF, 20% Piperidine/DMF solution (15ml/g), 5min is added to remove and add 20% Piperidine/DMF solution (15ml/ again
G), 15min.
(4) it detects
Piperidine solution is taken out, more than ten grainy resins are taken, is washed three times with ethyl alcohol, detection reagent is added and detects, 105 DEG C~110 DEG C
5min is heated, change navy blue is positive reaction；
(5) it elutes
Twice with DMF (10ml/g) elutions, DCM (10ml/g) is eluted twice, and DMF (10ml/g) is eluted twice；
(6) it is condensed
Protected amino acid three times are excessive, and HBTU three times are excessive, with DMF dissolvings are lacked as possible, reaction tube are added, is added immediately
Ten times of excess of DIEA react 30min；
(7) it detects
More than ten grainy resins are taken, are washed three times with ethyl alcohol, detection reagent detection is added, 105 DEG C -110 DEG C are heated 5min, colourless
For negative reaction；
(8) it elutes
It is washed once with DMF (10ml/g), DCM (10ml/g) is washed twice, and DMF (10ml/g) is washed twice；
(9) operation of three to six steps, the amino acid being sequentially connected from right to left in sequence are repeated；
(10) it drains, washes resin in following manner
Twice, twice, twice, DCM (10ml/g) twice, is drained DMF (10ml/g) methanol (10ml/g) DMF (10ml/g)
10min；
(11) polypeptide is cut from resin
Prepare cutting liquid (10/g), TFA 95%；Water 1%；EDT 2%；TIS 2%, clipping time：120min；
(12) drying washing
Lysate is dried up as possible with nitrogen, is washed six times with ether, then room temperature volatilizes；
(13) analysis purification：
Crude product is purified with high performance liquid chromatography；
(14) it is lyophilized
Collection target polypeptides solution, which is put into freeze dryer, to be concentrated, and white powder is lyophilized into.
Embodiment 2, CRAMP cyclisation processing
Since that there are side effects is big by linear CRAMP, and the problem of stability difference, the present embodiment research cyclisation processing CRAMP
Antibacterium biomembrane activity and stability.
The head and the tail of GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ (SEQ ID NO.1) sequence are connect respectively first
Upper Cys (cysteine), the sequence of acquisition are：CGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQC(SEQ ID
NO.2), it is cyclized using DMSO oxidizing process, buffer salt pH=8,10% DMSO is as cosolvent, magnetic agitation reaction
10h obtains cyclic peptide CRAMP, and amino acid sequence is as shown in SEQ ID NO.1.
Embodiment 3, verification cyclic peptide CRAMP biomembrane scavenging effect
The cyclic peptide CRAMP that embodiment 1 synthesizes is carried out anti-P.a biomembranes to wild type strain PAO1 to study, specially：?
It is parallel every time to be 2 rows in 96 porocyte culture plates, 48h maturation PAO1 biomembranes are pre-formed, are added after the cleaning of PBS liquid dense
After degree acts on 1h for 0 μM, 0.62 μM, 1.25 μM, 2.5 μM, 5 μM, 10 μM and 20 μM of cyclic peptide CRAMP, examined using crystal violet method
Survey biomembrane amount (biofilm mass), another mining TSA tablet test biology film viable counts, be independently repeated 3 times it is above,
The results are shown in Figure 2.The results show that gradually decreasing (broken line), biofilm biomass as cyclic peptide CRAMP concentration increases PAO1 viable counts
When concentration is higher than 1.25 μM, also gradually decreased (block diagram) as concentration increases biofilm biomass, biomembrane when concentration is more than 5 μM
Amount reduces apparent.Show cyclic peptide CRAMP to biofilm have apparent scavenging effect, and concentration be more than 5 μM of concentration when, ring
Peptide C RAMP has significant scavenging effect to PAO1 biomembranes.
Embodiment 4 verifies study on the stability of the cyclic peptide CRAMP to enzyme
Study on the stability method is under 37 DEG C of water bath conditions, is the neutral proteinase of 1mg/mL with reaction density
(Neutral protease), pepsin (Pepsase), trypsase (Trypsase) handle CRAMP and cyclic peptide respectively
CRAMP30min is control to be not added with enzymatic treatment.Then, then bacteriostasis to E.coli is observed, the results are shown in Figure 3.
As a result, it has been found that CRAMP is unstable to pepsin, trypsase, and after cyclisation processing, stability significantly improves.Therefore, it uses
It is cyclized the CRAMP processing not only scavenging effect with biomembrane, and stability is significantly improved.
Finally illustrate, preferred embodiment above is merely illustrative of the technical solution of the present invention and unrestricted, although logical
It crosses above preferred embodiment the present invention is described in detail, however, those skilled in the art should understand that, can be
Various changes are made to it in form and in details, without departing from claims of the present invention limited range.
Sequence table
<110>Southwestern University
<120>The application of antimicrobial peptide CRAMP and its cyclic peptide in the drug for preparing bacteria removal biomembrane
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 34
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Gly Leu Leu Arg Lys Gly Gly Glu Lys Ile Gly Glu Lys Leu Lys Lys
1 5 10 15
Ile Gly Gln Lys Ile Lys Asn Phe Phe Gln Lys Leu Val Pro Gln Pro
20 25 30
Glu Gln
<210> 2
<211> 36
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 2
Cys Gly Leu Leu Arg Lys Gly Gly Glu Lys Ile Gly Glu Lys Leu Lys
1 5 10 15
Lys Ile Gly Gln Lys Ile Lys Asn Phe Phe Gln Lys Leu Val Pro Gln
20 25 30
Pro Glu Gln Cys
35
Claims (7)
1. applications of the antimicrobial peptide CRAMP in the drug for preparing bacteria removal biomembrane, it is characterised in that：It is described to resist micro- life
The amino acid sequence of object Peptide C RAMP is as shown in SEQ ID NO.1.
2. application according to claim 1, it is characterised in that：The bacterium is pseudomonas aeruginosa.
3. applications of the antimicrobial peptide CRAMP in the drug for preparing cystic fibrosis pneumonia, it is characterised in that：It is described to resist micro- life
The amino acid sequence of object Peptide C RAMP is as shown in SEQ ID NO.1.
4. applications of the antimicrobial cyclic peptide CRAMP in the drug for preparing bacteria removal biomembrane, it is characterised in that：It is described anti-micro-
The amino acid sequence of biological Peptide C RAMP is as shown in SEQ ID NO.1.
5. application according to claim 2, it is characterised in that：The bacterium is pseudomonas aeruginosa.
6. application according to claim 3, it is characterised in that：The effective dose concentration of the antimicrobial cyclic peptide CRAMP
More than 5 μM.
7. applications of the antimicrobial cyclic peptide CRAMP in the drug for preparing cystic fibrosis pneumonia, it is characterised in that：It is described anti-micro-
The amino acid sequence of biocycle Peptide C RAMP is as shown in SEQ ID NO.1.
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| CN201810701474.7A CN108752433B (en) | 2018-06-29 | 2018-06-29 | Antimicrobial peptide CRAMP and application of cyclic peptide thereof in preparation of drugs for removing bacterial biofilms |
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|---|---|---|---|
| CN201810701474.7A CN108752433B (en) | 2018-06-29 | 2018-06-29 | Antimicrobial peptide CRAMP and application of cyclic peptide thereof in preparation of drugs for removing bacterial biofilms |
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| CN108752433A true CN108752433A (en) | 2018-11-06 |
| CN108752433B CN108752433B (en) | 2020-12-22 |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112961246A (en) * | 2021-02-07 | 2021-06-15 | 西南大学 | Nano microsphere anti-biofilm peptide CRAMP and preparation method and application thereof |
Citations (4)
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|---|---|---|---|---|
| US20100048480A1 (en) * | 2006-11-22 | 2010-02-25 | Bettina Bommarius | Production of anti-microbial peptides |
| CN104387452A (en) * | 2014-11-25 | 2015-03-04 | 中国人民解放军第三军医大学第一附属医院 | Biological film inhibiting peptide and application thereof |
| CN105566452A (en) * | 2016-01-22 | 2016-05-11 | 北京农学院 | Antibacterial peptide with annular structure and preparation method and application thereof |
| CN107405377A (en) * | 2015-03-12 | 2017-11-28 | 三井化学株式会社 | The destruction methods of excretion body, the separation method for destroying kit and the excretion body from normal cell of excretion body |
-
2018
- 2018-06-29 CN CN201810701474.7A patent/CN108752433B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20100048480A1 (en) * | 2006-11-22 | 2010-02-25 | Bettina Bommarius | Production of anti-microbial peptides |
| CN104387452A (en) * | 2014-11-25 | 2015-03-04 | 中国人民解放军第三军医大学第一附属医院 | Biological film inhibiting peptide and application thereof |
| CN107405377A (en) * | 2015-03-12 | 2017-11-28 | 三井化学株式会社 | The destruction methods of excretion body, the separation method for destroying kit and the excretion body from normal cell of excretion body |
| CN105566452A (en) * | 2016-01-22 | 2016-05-11 | 北京农学院 | Antibacterial peptide with annular structure and preparation method and application thereof |
Non-Patent Citations (5)
| Title |
|---|
| HONGWEI CHEN 等: ""Inhibition and Eradication of Pseudomonas aeruginosa Biofilms by Host Defence Peptides"", 《SCI REP》 * |
| JOERG OVERHAGE 等: ""Human Host Defense Peptide LL-37 Prevents Bacterial Biofilm Formation"", 《INFECTION AND IMMUNITY》 * |
| KATRIJN DE BRUCKER 等: ""Derivatives of the Mouse Cathelicidin-Related Antimicrobial Peptide (CRAMP) Inhibit Fungal and Bacterial Biofilm Formation"", 《ANTIMICROB AGENTS CHEMOTHER》 * |
| 刘培培 等: ""抗茵肽在下呼吸道感染茵中的"", 《中国医师进修杂志》 * |
| 王宏岩 等: ""抗菌肽抑制细菌生物膜的研究现状"", 《中国微生态学杂志》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112961246A (en) * | 2021-02-07 | 2021-06-15 | 西南大学 | Nano microsphere anti-biofilm peptide CRAMP and preparation method and application thereof |
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