CN107602677B - B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof - Google Patents
B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof Download PDFInfo
- Publication number
- CN107602677B CN107602677B CN201710942502.XA CN201710942502A CN107602677B CN 107602677 B CN107602677 B CN 107602677B CN 201710942502 A CN201710942502 A CN 201710942502A CN 107602677 B CN107602677 B CN 107602677B
- Authority
- CN
- China
- Prior art keywords
- enterococcus faecalis
- protein
- cell epitope
- epitope peptide
- resin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
Images
Abstract
The invention provides a B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and a kit thereof, wherein the core amino acid sequence of the B cell epitope peptide for detecting the enterococcus faecalis gelatinase protein is as follows: AMRYGETSTPTGKTYAS are provided. The B cell epitope peptide of the technical scheme of the invention is used for detecting enterococcus faecalis gelatinase protein, has high titer, good repeatability and specificity, can be used for detecting enterococcus faecalis virulence protein gelE, and has great clinical value.
Description
Technical Field
The invention relates to an epitope peptide, in particular to a B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and a kit thereof.
Background
Enterococci is generally considered to be a conditional pathogen and is often planted in oral cavities, normal intestinal mucosa, female genital tracts and other parts of people and animals. Enterococcus is a common pathogenic bacterium of nosocomial infection at present, and can cause infection of urinary tract, respiratory tract, abdominal cavity, pelvic cavity and other parts. Enterococcus infection is mainly seen in patients with low immunity or excessive use of antibiotics, and can also cause blood stream infection, endocarditis and the like to endanger life, and the death rate can reach 21.0-27.5%. Enterococcus in nosocomial infectious pathogens of China is 3 rd in gram-positive bacteria and is only behind staphylococci and streptococci. The clinical specimens of the Shenzhen Hospital clinical laboratory at Beijing university identified 184 enterococci separated from the hospital between 10 and 2008, and as a result, 133 enterococci faecalis (72.3%), 32 enterococci faecium (17.4%), and 19 enterococci of other species (10.3%) among the 184 enterococci, which showed that the enterococci infection rate was significantly increased. As enterococcus has the characteristics of natural drug resistance and acquired drug resistance, particularly natural drug resistance to cephalosporins drugs, hospital infection becomes one of the problems of clinical treatment and is increasingly paid more attention to by people. Vancomycin-resistant Enterococci (VRE) has been one of the major pathogens in outbreaks of nosocomial infections.
Enterococcus faecalis is currently the most common pathogenic bacterium for enterococcus infections, and may account for 80-90% of enterococcus infections. In the study on enterococcus blood stream infection reported in 2014, enterococcus faecalis is also significantly more than enterococcus faecium. Therefore, enterococcus faecalis bloodstream infections have been in the hospital setting, and have gained increasing importance. In clinical infected patients, the positive rate of blood culture is low, so that the pathogen of blood stream infection cannot be diagnosed clearly at an early stage, thereby delaying clinical treatment or causing misdiagnosis and mistreatment.
In recent years, in the clinical isolated enterococcus faecalis strains, there are continuous research reports that the virulence factors related to the enterococcus faecalis are detected. Cosentino S et al detected virulence factors cylA, gelE, esp and efaA in a clinically isolated 91 strain of enterococcus faecalis, where the cylA or gelE positive rate was higher than the other factors. In 2014, Medeeros AW et al detected positive cylA, gelE and esp in 57 clinical isolates of enterococcus faecalis, and the positive rates of cylA and esp in clinical isolates were higher than those of food-derived strains. While Strateva T et al reported in the last 2016 that among 510 clinically isolated enterococcus strains, the relevant virulence factors were detected: esp-44.3%, efaA-85.9%, gelE-64.3%, and cylA-47.1%. Moreover, the positive rate of the virulence factors in the enterococcus faecalis strain is higher than that of the enterococcus faecium. Therefore, the finding of molecular markers for early diagnosis of enterococcus faecalis blood stream infection, monitoring and evaluating the curative effect, and predicting the clinical prognosis of treatment is becoming more urgent and important.
Disclosure of Invention
Aiming at the technical problems, the invention discloses a B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and a kit thereof, which are combined with an enzyme-linked immunoassay method and can be used for detecting the enterococcus faecalis with gelE virulence protein in blood stream.
In contrast, the technical scheme adopted by the invention is as follows:
a B cell epitope peptide for detecting enterococcus faecalis gelatinase protein, which has a core amino acid sequence as follows: AMRYGETSTPTGKTYAS (shown as SEQ ID No. 1), GIRNLQTPSKHGQPETMAQY (shown as SEQ ID No. 2), VDEQHPDAYDNAFWD (shown as SEQ ID No. 3) or SGASNPEIGADTQSVDRKT (shown as SEQ ID No. 4).
Preferably, the core amino acid sequence of the B cell epitope peptide for detecting the enterococcus faecalis gelatinase protein is as follows: AMRYGETSTPTGKTYAS (shown in SEQ ID No. 1).
In vitro immunology experimental research, zoology experiments, specificity experiments and repeatability experiments detected by applying an ELISA method find that the synthetic peptide containing the core amino acid sequence has high titer and good specificity and repeatability.
Furthermore, at least one end of the B cell epitope peptide sequence for detecting the enterococcus faecalis gelatinase protein is connected with a protective peptide with no more than 5 amino acids.
Furthermore, the N end of the B cell epitope peptide sequence for detecting the enterococcus faecalis gelatinase protein is connected with two amino acids HS.
Furthermore, the C end of the B cell epitope peptide sequence for detecting the enterococcus faecalis gelatinase protein is connected with GG.
The invention also discloses an antigen for detecting the enterococcus faecalis gelatinase protein, which is prepared by coupling the B cell epitope peptide for detecting the enterococcus faecalis gelatinase protein and a carrier protein.
Further, the carrier protein is KLH.
The invention also discloses a kit for detecting the enterococcus faecalis gelatinase protein, which contains the coating material of the B cell epitope peptide for detecting the enterococcus faecalis gelatinase protein.
Compared with the prior art, the invention has the beneficial effects that:
the B cell epitope peptide of the technical scheme of the invention is used for detecting enterococcus faecalis gelatinase protein, has high titer, good repeatability and specificity, can be used for detecting enterococcus faecalis virulence protein gelE, and has great clinical value.
Drawings
FIG. 1 is a graph showing the change in OD value of the synthetic peptide P1 in response to mouse serum, which was detected by indirect ELISA method before and after immunization according to the present invention.
FIG. 2 is a graph showing the change in OD value of the reaction of the synthetic peptide P2 with mouse serum, which was detected by indirect ELISA before and after immunization according to the present invention.
FIG. 3 is a graph showing the change in OD value of the synthetic peptide P3 in response to mouse serum measured by indirect ELISA method before and after immunization according to the present invention.
FIG. 4 is a graph showing the change in OD value of the synthetic peptide P4 in response to mouse serum measured by indirect ELISA method before and after immunization according to the present invention.
FIG. 5 is a graph showing the results of the indirect ELISA method of the present invention for detecting the cross-reaction of the synthetic peptide P1 with large intestine, Staphylococcus aureus, pneumococcal, pulmonary chain, Bacillus subtilis, and Candida albicans.
Detailed Description
Preferred embodiments of the present invention will be described in further detail below.
Example 1
The synthetic peptide P1 was prepared using solid phase synthesis according to the following procedure, the amino acid sequence of the synthetic peptide P1 being:
synthetic peptide P1: AMRYGETSTPTGKTYAS (shown as SEQ ID No. 1)
Step S1: fmoc-amino acids are attached to the resin
Adding 1.0g (the substitution degree is 1.08mmol/g) of 2-chloro-triphenyl-chlorine resin CTC resin into a solid phase synthesis reaction tube, soaking the CTC resin in 30ml of N, N' -dicyclohexylcarbodiimide DCM for 30min to fully swell the CTC resin, and activating the CTC resin for later use. Then, 1.5mmol of Fmoc-amino acid-OH, 15ml of dichloromethane and 0.42ml of N, N-diisopropylethylamine DIPEA were added, and the mixture was reacted for 3 hours with shaking. After the reaction, the liquid was filtered off, and the resin was washed with methanol and dichloromethane in sequence 3 times each, and then drained for use.
Step S2: stepwise linkage of amino acids
15ml of 20% piperidine-DMF solution was added to the resin obtained in step S1, followed by shaking reaction for 30 min. The weighed Fmoc-amino acid (2eq) and 1-hydroxybenzotriazole HOBt (3eq) are mixed and dissolved in 5ml of N, N-dimethylformamide DMF solution, then N, N' -dicyclohexylcarbodiimide DCC (3eq) and 15ml of dichloromethane are added, and the mixture is shaken for reaction for 30 min. And removing Fmoc by using 15ml of 20% piperidine-DMF solution, then activating the next Fmoc-amino acid, filtering the activated solution into a solid-phase reaction tube, carrying out shake reaction for 2 hours, and washing 3 times by using DMF and dichloromethane after the reaction is finished. The deprotection → condensation → deprotection is repeated according to the sequence shown in SEQ ID No.1 until all amino acids are connected, and the reacted resin is obtained.
Step S3: liberating the polypeptide from the resin using a dilute acid system
After the reaction in step S2, 30ml of a solvent (volume ratio) of acetic acid, trifluoroethanol and dichloromethane (volume ratio) was added to the resin, the mixture was shaken for 1 hour, filtered, the resin was washed with dichloromethane 3 times, and the filtrate was concentrated (during which toluene was added to remove residual acetic acid) to obtain a crude protected polypeptide. And adding 20ml of trifluoroacetic acid TFA and DCM (volume ratio) solvent, stirring and reacting for 30min, concentrating to obtain a crude target polypeptide product, and purifying by preparative high performance liquid chromatography to obtain a pure synthetic peptide P1.
Example 2
The synthetic peptide P2 was prepared using solid phase synthesis according to the following procedure, the amino acid sequence of the synthetic peptide P2 being:
synthetic peptide P2: GIRNLQTPSKHGQPETMAQY (shown as SEQ ID No. 2)
Step S1: fmoc-amino acids are attached to the resin
Adding 1.0g (the substitution degree is 1.08mmol/g) of 2-chloro-triphenyl-chlorine resin CTC resin into a solid phase synthesis reaction tube, soaking the CTC resin in 30ml of N, N' -dicyclohexylcarbodiimide DCM for 30min to fully swell the CTC resin, and activating the CTC resin for later use. Then, 1.5mmol of Fmoc-amino acid-OH, 15ml of dichloromethane and 0.42ml of N, N-diisopropylethylamine DIPEA were added, and the mixture was reacted for 3 hours with shaking. After the reaction, the liquid was filtered off, and the resin was washed with methanol and dichloromethane in sequence 3 times each, and then drained for use.
Step S2: stepwise linkage of amino acids
15ml of 20% piperidine-DMF solution was added to the resin obtained in step S1, followed by shaking reaction for 30 min. The weighed Fmoc-amino acid (2eq) and 1-hydroxybenzotriazole HOBt (3eq) are mixed and dissolved in 5ml of N, N-dimethylformamide DMF solution, then N, N' -dicyclohexylcarbodiimide DCC (3eq) and 15ml of dichloromethane are added, and the mixture is shaken for reaction for 30 min. And removing Fmoc by using 15ml of 20% piperidine-DMF solution, then activating the next Fmoc-amino acid, filtering the activated solution into a solid-phase reaction tube, carrying out shake reaction for 2 hours, and washing 3 times by using DMF and dichloromethane after the reaction is finished. The deprotection → condensation → deprotection is repeated according to the sequence shown in SEQ ID No.2 until all amino acids are connected, and the reacted resin is obtained.
Step S3: liberating the polypeptide from the resin using a dilute acid system
After the reaction in step S2, 30ml of a solvent (volume ratio) of acetic acid, trifluoroethanol and dichloromethane (volume ratio) was added to the resin, the mixture was shaken for 1 hour, filtered, the resin was washed with dichloromethane 3 times, and the filtrate was concentrated (during which toluene was added to remove residual acetic acid) to obtain a crude protected polypeptide. And adding 20ml of trifluoroacetic acid TFA and DCM (volume ratio) solvent, stirring and reacting for 30min, concentrating to obtain a crude target polypeptide product, and purifying by preparative high performance liquid chromatography to obtain a pure synthetic peptide P2.
Example 3
The synthetic peptide P3 was prepared using solid phase synthesis according to the following procedure, the amino acid sequence of the synthetic peptide P3 being:
synthetic peptide P3: VDEQHPDAYDNAFWD (shown as SEQ ID No. 3)
Step S1: fmoc-amino acids are attached to the resin
Adding 1.0g (the substitution degree is 1.08mmol/g) of 2-chloro-triphenyl-chlorine resin CTC resin into a solid phase synthesis reaction tube, soaking the CTC resin in 30ml of N, N' -dicyclohexylcarbodiimide DCM for 30min to fully swell the CTC resin, and activating the CTC resin for later use. Then, 1.5mmol of Fmoc-amino acid-OH, 15ml of dichloromethane and 0.42ml of N, N-diisopropylethylamine DIPEA were added, and the mixture was reacted for 3 hours with shaking. After the reaction, the liquid was filtered off, and the resin was washed with methanol and dichloromethane in sequence 3 times each, and then drained for use.
Step S2: stepwise linkage of amino acids
15ml of 20% piperidine-DMF solution was added to the resin obtained in step S1, followed by shaking reaction for 30 min. The weighed Fmoc-amino acid (2eq) and 1-hydroxybenzotriazole HOBt (3eq) are mixed and dissolved in 5ml of N, N-dimethylformamide DMF solution, then N, N' -dicyclohexylcarbodiimide DCC (3eq) and 15ml of dichloromethane are added, and the mixture is shaken for reaction for 30 min. And removing Fmoc by using 15ml of 20% piperidine-DMF solution, then activating the next Fmoc-amino acid, filtering the activated solution into a solid-phase reaction tube, carrying out shake reaction for 2 hours, and washing 3 times by using DMF and dichloromethane after the reaction is finished. The deprotection → condensation → deprotection is repeated according to the sequence shown in SEQ ID No.3 until all amino acids are connected, and the reacted resin is obtained.
Step S3: liberating the polypeptide from the resin using a dilute acid system
After the reaction in step S2, 30ml of a solvent (volume ratio) of acetic acid, trifluoroethanol and dichloromethane (volume ratio) was added to the resin, the mixture was shaken for 1 hour, filtered, the resin was washed with dichloromethane 3 times, and the filtrate was concentrated (during which toluene was added to remove residual acetic acid) to obtain a crude protected polypeptide. And adding 20ml of trifluoroacetic acid TFA and DCM (volume ratio) solvent, stirring and reacting for 30min, concentrating to obtain a crude target polypeptide product, and purifying by preparative high performance liquid chromatography to obtain a pure synthetic peptide P3.
Example 4
The synthetic peptide P4 was prepared using solid phase synthesis according to the following procedure, the amino acid sequence of the synthetic peptide P4 being:
synthetic peptide P3: SGASNPEIGADTQSVDRKT (shown as SEQ ID No. 4)
Step S1: fmoc-amino acids are attached to the resin
Adding 1.0g (the substitution degree is 1.08mmol/g) of 2-chloro-triphenyl-chlorine resin CTC resin into a solid phase synthesis reaction tube, soaking the CTC resin in 30ml of N, N' -dicyclohexylcarbodiimide DCM for 30min to fully swell the CTC resin, and activating the CTC resin for later use. Then, 1.5mmol of Fmoc-amino acid-OH, 15ml of dichloromethane and 0.42ml of N, N-diisopropylethylamine DIPEA were added, and the mixture was reacted for 3 hours with shaking. After the reaction, the liquid was filtered off, and the resin was washed with methanol and dichloromethane in sequence 3 times each, and then drained for use.
Step S2: stepwise linkage of amino acids
15ml of 20% piperidine-DMF solution was added to the resin obtained in step S1, followed by shaking reaction for 30 min. The weighed Fmoc-amino acid (2eq) and 1-hydroxybenzotriazole HOBt (3eq) are mixed and dissolved in 5ml of N, N-dimethylformamide DMF solution, then N, N' -dicyclohexylcarbodiimide DCC (3eq) and 15ml of dichloromethane are added, and the mixture is shaken for reaction for 30 min. And removing Fmoc by using 15ml of 20% piperidine-DMF solution, then activating the next Fmoc-amino acid, filtering the activated solution into a solid-phase reaction tube, carrying out shake reaction for 2 hours, and washing 3 times by using DMF and dichloromethane after the reaction is finished. The deprotection → condensation → deprotection is repeated according to the sequence shown in SEQ ID No.4 until all amino acids are connected, and the reacted resin is obtained.
Step S3: liberating the polypeptide from the resin using a dilute acid system
After the reaction in step S2, 30ml of a solvent (volume ratio) of acetic acid, trifluoroethanol and dichloromethane (volume ratio) was added to the resin, the mixture was shaken for 1 hour, filtered, the resin was washed with dichloromethane 3 times, and the filtrate was concentrated (during which toluene was added to remove residual acetic acid) to obtain a crude protected polypeptide. And adding 20ml of trifluoroacetic acid TFA and DCM (volume ratio) solvent, stirring and reacting for 30min, concentrating to obtain a crude target polypeptide product, and purifying by preparative high performance liquid chromatography to obtain a pure synthetic peptide P4.
Example 5
And (3) an indirect ELISA method is used for detecting the antibody titer.
By adopting an indirect ELISA method for detection, before immunization, after 2 nd immunization and last immunization of 8 randomly drawn mice respectively corresponding to the synthetic peptides P1, P2, P3 and P4, OD450nm values of the 8 mice are measured under a series of dilutions, and curve change graphs before immunization, 2 times immunization and last immunization are drawn, as shown in figure 1, figure 2, figure 3 and figure 4.
As can be seen from fig. 1, 2, 3 and 4, the titer of the mouse serum antibody was significantly improved after the immunization. By comparison, the potency of the synthetic peptide P1 was significantly greater than that of the other three synthetic peptides, and P1 was selected as the epitope peptide coating in the following experiment for subsequent specificity and reproducibility evaluation.
Example 6
Synthetic peptide P1_ ELISA specific experiment.
The synthetic peptide P1 was subjected to ELISA reaction with sera from mice infected with large intestine, Staphylococcus aureus, pneumocandin, Bacillus subtilis, Candida albicans, and enterococcus faecalis, and the OD values thereof were measured, respectively, as shown in Table 1 and FIG. 5.
TABLE 1 Cross-reactivity test data
As can be seen from table 1 and fig. 5, the OD values for detection of large intestine, staphylococcus aureus, pneumocandin, bacillus subtilis and candida albicans were all very low, and there was no significant cross reaction, P <0.001, and therefore, the specificity of the gelE protein epitope peptide P1 of enterococcus faecalis good.
Example 7
Synthetic peptide P1_ ELISA replicate evaluation experiments.
The synthetic peptide P1 was evaluated for reproducibility by coefficient of variation calculation. The results are shown in Table 2, and it can be seen that the coefficient of variation is 6.2% -9.1%, and the repeatability is good.
TABLE 2 synthetic peptide P1_ ELISA repeatability assessment experiment results
The foregoing is a more detailed description of the invention in connection with specific preferred embodiments and it is not intended that the invention be limited to these specific details. For those skilled in the art to which the invention pertains, several simple deductions or substitutions can be made without departing from the spirit of the invention, and all shall be considered as belonging to the protection scope of the invention.
Sequence listing
<110> Shenzhen south mountain region people hospital
<120> B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof
<160>4
<170>SIPOSequenceListing 1.0
<210>1
<211>17
<212>PRT
<213> Artificial Sequence (Artificial Sequence)
<400>1
Ala Met Arg Tyr Gly Glu Thr Ser Thr Pro Thr Gly Lys Thr Tyr Ala
1 5 10 15
Ser
<210>2
<211>20
<212>PRT
<213> Artificial Sequence (Artificial Sequence)
<400>2
Gly Ile Arg Asn Leu Gln Thr Pro Ser Lys His Gly Gln Pro Glu Thr
1 5 10 15
Met Ala Gln Tyr
20
<210>3
<211>15
<212>PRT
<213> Artificial Sequence (Artificial Sequence)
<400>3
Val Asp Glu Gln His Pro Asp Ala Tyr Asp Asn Ala Phe Trp Asp
1 5 10 15
<210>4
<211>19
<212>PRT
<213> Artificial Sequence (Artificial Sequence)
<400>4
Ser Gly Ala Ser Asn Pro Glu Ile Gly Ala Asp Thr Gln Ser Val Asp
1 5 10 15
Arg Lys Thr
Claims (4)
1. A B cell epitope peptide for detecting enterococcus faecalis gelatinase protein is characterized in that the amino acid sequence of the B cell epitope peptide is as follows: AMRYGETSTPTGKTYAS are provided.
2. An antigen for use in the detection of enterococcus faecalis gelatinase protein, comprising: which is prepared by coupling the B-cell epitope peptide for the detection of enterococcus faecalis gelatinase protein according to claim 1 with a carrier protein.
3. The antigen for the detection of enterococcus faecalis gelatinase protein according to claim 2, wherein: the carrier protein is KLH.
4. A kit for detecting enterococcus faecalis gelatinase protein is characterized in that: which comprises a coating of the B-cell epitope peptide of claim 1 for use in the detection of enterococcus faecalis gelatinase protein.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201710942502.XA CN107602677B (en) | 2017-10-11 | 2017-10-11 | B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201710942502.XA CN107602677B (en) | 2017-10-11 | 2017-10-11 | B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN107602677A CN107602677A (en) | 2018-01-19 |
| CN107602677B true CN107602677B (en) | 2020-05-26 |
Family
ID=61068677
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201710942502.XA Active CN107602677B (en) | 2017-10-11 | 2017-10-11 | B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN107602677B (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108707186B (en) * | 2018-05-28 | 2021-11-09 | 桂林医学院 | Human sperm specific antigen epitope peptide, polymer and application thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2010089340A3 (en) * | 2009-02-05 | 2010-12-09 | Intercell Ag | Peptides protective against e. faecalis, methods and uses relating thereto |
| CN102304527A (en) * | 2003-05-30 | 2012-01-04 | 英特塞尔股份公司 | Enterococcus antigens |
-
2017
- 2017-10-11 CN CN201710942502.XA patent/CN107602677B/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102304527A (en) * | 2003-05-30 | 2012-01-04 | 英特塞尔股份公司 | Enterococcus antigens |
| WO2010089340A3 (en) * | 2009-02-05 | 2010-12-09 | Intercell Ag | Peptides protective against e. faecalis, methods and uses relating thereto |
Non-Patent Citations (3)
| Title |
|---|
| Enterococcus faecalis with the gelatinase phenotype regulated by the fsr operon and with biofilm-forming capacity are common in the agricultural environment;Macovei L等;《Environmental Microbiology》;20090630;第1540-1547页 * |
| 粪肠球菌抗体间接ELISA检测方法的建立及应用;周霞等;《中国兽医科学》;20081231;第417-421页 * |
| 鹅源粪肠球菌毒力因子gelE的克隆、原核表达及生物信息学分析;孟庆君;《中国优秀硕士学位论文全文数据库 农业科学辑》;20150615;D050-19 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN107602677A (en) | 2018-01-19 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Pancholi et al. | Isolation and characterization of the cell-associated region of group A streptococcal M6 protein | |
| Otvos et al. | Insect peptides with improved protease-resistance protect mice against bacterial infection | |
| JP5572207B2 (en) | Binding molecules for human factor VIII and factor VIII-like proteins | |
| CN101516905A (en) | Borrelia antigens | |
| DK2236608T3 (en) | New peptides for the treatment and prevention of immune-related diseases, including the treatment and prevention of infection by modulating natural immunity | |
| CN107602677B (en) | B cell epitope peptide for detecting enterococcus faecalis gelatinase protein and kit thereof | |
| JP2010505395A (en) | Novel peptides for the treatment and prevention of immune related disease disorders, including treatment and prevention of infections by modulating innate immunity | |
| BG60621B1 (en) | New polypeptide and anti hiv medicament produced from it | |
| CN110563802B (en) | Group of antibacterial peptide analogues containing N-methylated amino acid and N-terminal fatty acid modification, and synthetic method and application thereof | |
| CN113150077B (en) | Cyclohexapeptide compound desotamide A4 and application thereof in preparation of antibacterial drugs | |
| CN106866793B (en) | Polypeptide compound and preparation method and application thereof | |
| EP0642348A1 (en) | Antibiotic cryptdin peptides and methods of their use | |
| CN107827961B (en) | B cell epitope peptide for detecting Staphopain B protein of staphylococcus aureus and kit thereof | |
| CN109485713A (en) | Dimerization modified antimicrobial peptide analogues and its synthesis and application with strong antibacterial activity and hypotoxicity | |
| Drijfhout et al. | Solid-phase synthesis and applications of N-(S-acetylmercaptoacetyl) peptides | |
| WO2017190619A1 (en) | Chemosynthetic cyclo-heptamodified peptide capable of inhibiting toxin of staphylococcus aureus and use thereof | |
| CN103833831A (en) | Method for preparing carbetocin | |
| CN113621034A (en) | Novel coronavirus B-cell antigens with immunoreactivity | |
| KR20040015128A (en) | Crohn's disease antibody-binding peptide and method of examining crohn's disease | |
| CN116063408A (en) | Foot-and-mouth disease virus A type ELISA antibody detection kit and preparation method and application thereof | |
| Paquette et al. | RpoN-Based stapled peptides with improved DNA binding suppress Pseudomonas aeruginosa virulence | |
| Haramura et al. | Design and synthesis of N-terminal cyclic motilin partial peptides: a novel pure motilin antagonist | |
| CN109796523B (en) | Cyclic polypeptide for resisting candida albicans and preparation method thereof | |
| CN111153960B (en) | A-type botulinum toxin inhibitor and preparation method and application thereof | |
| CN112521458B (en) | Synthetic peptide Sao for detecting s.suis 2 infection355~372And uses thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |