CN107602677A - A kind of B cell antigen epi-position peptide and its kit for enterococcus faecalis gelatinase Protein Detections - Google Patents
A kind of B cell antigen epi-position peptide and its kit for enterococcus faecalis gelatinase Protein Detections Download PDFInfo
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- CN107602677A CN107602677A CN201710942502.XA CN201710942502A CN107602677A CN 107602677 A CN107602677 A CN 107602677A CN 201710942502 A CN201710942502 A CN 201710942502A CN 107602677 A CN107602677 A CN 107602677A
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- enterococcus faecalis
- cell antigen
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Abstract
The invention provides a kind of B cell antigen epi-position peptide and its kit for enterococcus faecalis gelatinase Protein Detections, the core amino acid sequence of the B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections is：AMRYGETSTPTGKTYAS.The B cell antigen epi-position peptide of technical scheme is used for enterococcus faecalis gelatinase Protein Detections, and potency is high, and repeatability and specificity are good, can be used to detect enterococcus faecalis virulence protein gelE, have very big clinical value.
Description
Technical field
The present invention relates to a kind of epitope peptide, more particularly to it is a kind of for enterococcus faecalis gelatinase Protein Detections
B cell antigen epi-position peptide and its kit.
Background technology
It has been generally acknowledged that enterococcus is conditioned pathogen, often field planting is in the oral cavity of humans and animals, normal bowel mucous membrane, Nv Xingsheng
The position such as grow.Enterococcus is currently the encountered pathogenic bacteria of nosocomial infection, can often cause the urinary tract, respiratory tract, intraperitoneal, pelvic cavity
The infection at the position such as interior.Enterococcal infection is mainly seen in hypoimmunity or the patient of antibiotic is excessively used, and can also cause
Bloodstream infection, endocarditis etc. are so as to threat to life, and the death rate is up to 21.0%~27.5%.In China's nosocomial infection pathogen
Enterococcus spp occupies the 3rd in gram positive bacteria, is only located at after staphylococcus, streptococcus.Examine BeiJing University ShenZhen Hospital
Section identifies to 184 plants of enterococcus are isolated in August, 2008 from institute's clinical samples in October, 2005, as a result 184
Enterococcus faecalis 133 plants (72.3%) in strain enterococcus, VREF 32 plants (17.4%), other kind of 19 plants of Isolation
(10.3%), display enterococcal infection rate substantially rises.It is special because enterococcus has the characteristic of natural drug resistance and acquired resistance
It is not the natural drug resistance for cephalosporins medicine, hospital infection caused by making turns into one of clinical treatment stubborn problem, increasingly
It is valued by people.And the enterococcus (vancomycin-resistant Enterococci, VRE) of vancomycin resistance,
It is one of main pathogens of hospital infection eruption and prevalence.
Enterococcus faecalis is currently the most common pathogenic bacteria of enterococcal infection, can account for the 80-90% of enterococcal infection.And
In the enterococcus bloodstream infection research of report in 2014, enterococcus faecalis will also be significantly more than VREF.Therefore, enterococcus faecalis
Bloodstream infection is in nosocomial infection, in occupation of increasingly consequence.And in clinical infection patient, due to blood culture
Positive rate is relatively low, the pathogen for the bloodstream infection that causes to clarify a diagnosis in early days, so as to be delayed clinical treatment or cause mistaken diagnosis to miss
Control.
In recent years in the enterococcus faecalis strain being clinically separated, constantly studies have reported that detecting the related virulence of enterococcus faecalis
The factor.Cosentino S etc. in 91 plants of enterococcus faecalis being clinically separated, detect virulence factor cylA, gelE, esp and
EfaA, wherein cylA or gelE positive rates are higher than other factors.Medeiros AW in 2014 etc. are clinically separated excrement intestines ball at 57 plants
In bacterial strain, cylA, gelE and esp positive are detected, and cylA the and esp positive rates in clinical separation strain are higher than food
Source bacterial strain.And nearest Strateva T in 2016 etc. are reported in 510 plants of clinical separating sausage coccus strains, related virulence is detected
The factor：Esp-44.3%, efaA-85.9%, gelE-64.3%, and cylA-47.1%.And these virulence factors are in excrement intestines
Positive rate in coccus strain is higher than VREF.Therefore, the molecular labeling of enterococcus faecalis bloodstream infection can be early diagnosed by finding
Thing, and curative effect can be monitored and assess, the clinical prognosis situation of predicted treatment is more and more urgent and significant so as to seem.
The content of the invention
For above technical problem, the invention discloses a kind of B for enterococcus faecalis gelatinase Protein Detections is thin
Extracellular antigen epitope peptide and its kit, with reference to enzyme-linked immunosorbent assay, available for the excrement intestines ball for having gelE virulence proteins in blood flow
The detection of bacterium.
On the other hand, the technical solution adopted by the present invention is：
A kind of B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections, its core amino acid sequence
For：AMRYGETSTPTGKTYAS (as shown in SEQ ID No.1), GIRNLQTPSKHGQPETMAQY are (such as SEQ ID No.2 institutes
Show), VDEQHPDAYDNAFWD (as shown in SEQ ID No.3) or SGASNPEIGADTQSVDRKT be (such as SEQ ID No.4 institutes
Show).
Preferably, the core amino of the B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections
Acid sequence is：AMRYGETSTPTGKTYAS (as shown in SEQ ID No.1).
In vitro in immunological experiment research, the Experiment of Zoology, specificity experiments and the repetition that are detected using ELISA method
Property it was found that, synthetic peptide potency containing above-mentioned core amino acid sequence is high, and with good specific and repeated.
Further, the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections is extremely
Few one end is connected with the protection peptide no more than 5 amino acid.
Further, the N-terminal of the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections
It is connected with two amino acid HS.
Further, the C-terminal of the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections
It is connected with GG.
The invention also discloses a kind of antigen for enterococcus faecalis gelatinase Protein Detections, it is by using such as
The upper described B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections is prepared with carrier protein couplet
's.
Further, the carrier protein is KLH.
The invention also discloses a kind of kit for enterococcus faecalis gelatinase Protein Detections, it contains as above institute
The coating thing for the B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections stated.
Compared with prior art, beneficial effects of the present invention are：
The B cell antigen epi-position peptide of technical scheme is used for enterococcus faecalis gelatinase Protein Detections, potency
Height, repeatability and specificity are good, can be used to detect enterococcus faecalis virulence protein gelE, have very big clinical value.
Brief description of the drawings
Fig. 1 is the synthetic peptide P1 and the OD value changes of mice serum reaction of the immune front and rear indirect elisa method detection of the present invention
Figure.
Fig. 2 is the synthetic peptide P2 and the OD value changes of mice serum reaction of the immune front and rear indirect elisa method detection of the present invention
Figure.
Fig. 3 is the synthetic peptide P3 and the OD value changes of mice serum reaction of the immune front and rear indirect elisa method detection of the present invention
Figure.
Fig. 4 is the synthetic peptide P4 and the OD value changes of mice serum reaction of the immune front and rear indirect elisa method detection of the present invention
Figure.
Fig. 5 be indirect elisa method of the present invention detection synthetic peptide P1 with large intestine, golden Portugal, lung gram, lung chain, bacillus subtilis,
The cross reaction test result figure of Candida albicans.
Embodiment
The preferably embodiment of the present invention is described in further detail below.
Embodiment 1
Synthetic peptide P1 is prepared according to following steps using solid-phase synthesis, the amino acid sequence of the synthetic peptide P1 is：
Synthetic peptide P1：AMRYGETSTPTGKTYAS (as shown in SEQ ID No.1)
Step S1：Fmoc- amino acid is connected with resin
2- chlorine triphenyl chlorine resin CTC resin 1.0g (substitution value 1.08mmol/g) are taken to be added to solid phase synthesis pipe
In, CTC resins is fully swelled with N, N'- dicyclohexylcarbodiimide DCM 30ml immersions 30min, activation is stand-by.Then add
Enter 1.5mmol Fmoc- amino acid-OH, dichloromethane 15ml, N, N- diisopropyl ethyl amine DIPEA 0.42ml, concussion is instead
Answer 3h.After reaction terminates, liquid is filtered off, resin is washed each 3 times with methanol, dichloromethane successively, drains stand-by.
Step S2：The progressively connection of amino acid
20% piperidines-DMF solution 15ml, concussion reaction 30min are added in the resin that step S1 reacts to obtain.It will weigh
Good Fmoc- amino acid (2eq) and 1- hydroxy benzo triazoles HOBt (3eq) are miscible in 5ml DMFs DMF
In solution, N, N'- dicyclohexylcarbodiimides DCC (3eq), dichloromethane 15ml, concussion reaction 30min are added.It is used in combination
20% piperidines-DMF solution 15ml sloughs Fmoc, then by next Fmoc- activations of amino acid, activating solution is filtered anti-to solid phase
Ying Guanzhong, concussion reaction 2h, respectively washed 3 times with DMF, dichloromethane after completion of the reaction.According to the sequence as shown in SEQ ID No.1
Row so repeat deprotection → condensation → deprotection, are finished until all amino acid connect, resin after being reacted.
Step S3：Polypeptide is dissociated from resin using diluted acid system
Add acetic acid in resin after above-mentioned steps S2 reactions: trifluoroethanol: dichloromethane=1: 1: 8 (volume ratio) it is molten
Agent common 30ml, oscillating reactions 1h, filtering, resin are washed 3 times with dichloromethane again, and (it is residual that period adds toluene removing to concentration filtrate
Stay acetic acid) obtain the polypeptide crude product with protection.And the solvent of trifluoroacetic acid TFA: DCM=1: 3 (volume ratio) is added in crude product
Common 20ml, stirring reaction 30min, are concentrated to give target polypeptides crude product, then with preparative efficient liquid phase purify and to obtain sterling and synthesize
Peptide P1.
Embodiment 2
Synthetic peptide P2 is prepared according to following steps using solid-phase synthesis, the amino acid sequence of the synthetic peptide P2 is：
Synthetic peptide P2：GIRNLQTPSKHGQPETMAQY (as shown in SEQ ID No.2)
Step S1：Fmoc- amino acid is connected with resin
2- chlorine triphenyl chlorine resin CTC resin 1.0g (substitution value 1.08mmol/g) are taken to be added to solid phase synthesis pipe
In, CTC resins is fully swelled with N, N'- dicyclohexylcarbodiimide DCM 30ml immersions 30min, activation is stand-by.Then add
Enter 1.5mmol Fmoc- amino acid-OH, dichloromethane 15ml, N, N- diisopropyl ethyl amine DIPEA 0.42ml, concussion is instead
Answer 3h.After reaction terminates, liquid is filtered off, resin is washed each 3 times with methanol, dichloromethane successively, drains stand-by.
Step S2：The progressively connection of amino acid
20% piperidines-DMF solution 15ml, concussion reaction 30min are added in the resin that step S1 reacts to obtain.It will weigh
Good Fmoc- amino acid (2eq) and 1- hydroxy benzo triazoles HOBt (3eq) are miscible in 5ml DMFs DMF
In solution, N, N'- dicyclohexylcarbodiimides DCC (3eq), dichloromethane 15ml, concussion reaction 30min are added.It is used in combination
20% piperidines-DMF solution 15ml sloughs Fmoc, then by next Fmoc- activations of amino acid, activating solution is filtered anti-to solid phase
Ying Guanzhong, concussion reaction 2h, respectively washed 3 times with DMF, dichloromethane after completion of the reaction.According to the sequence as shown in SEQ ID No.2
Row so repeat deprotection → condensation → deprotection, are finished until all amino acid connect, resin after being reacted.
Step S3：Polypeptide is dissociated from resin using diluted acid system
Add acetic acid in resin after above-mentioned steps S2 reactions: trifluoroethanol: dichloromethane=1: 1: 8 (volume ratio) it is molten
Agent common 30ml, oscillating reactions 1h, filtering, resin are washed 3 times with dichloromethane again, and (it is residual that period adds toluene removing to concentration filtrate
Stay acetic acid) obtain the polypeptide crude product with protection.And the solvent of trifluoroacetic acid TFA: DCM=1: 3 (volume ratio) is added in crude product
Common 20ml, stirring reaction 30min, are concentrated to give target polypeptides crude product, then with preparative efficient liquid phase purify and to obtain sterling and synthesize
Peptide P2.
Embodiment 3
Synthetic peptide P3 is prepared according to following steps using solid-phase synthesis, the amino acid sequence of the synthetic peptide P3 is：
Synthetic peptide P3：VDEQHPDAYDNAFWD (as shown in SEQ ID No.3)
Step S1：Fmoc- amino acid is connected with resin
2- chlorine triphenyl chlorine resin CTC resin 1.0g (substitution value 1.08mmol/g) are taken to be added to solid phase synthesis pipe
In, CTC resins is fully swelled with N, N'- dicyclohexylcarbodiimide DCM 30ml immersions 30min, activation is stand-by.Then add
Enter 1.5mmol Fmoc- amino acid-OH, dichloromethane 15ml, N, N- diisopropyl ethyl amine DIPEA 0.42ml, concussion is instead
Answer 3h.After reaction terminates, liquid is filtered off, resin is washed each 3 times with methanol, dichloromethane successively, drains stand-by.
Step S2：The progressively connection of amino acid
20% piperidines-DMF solution 15ml, concussion reaction 30min are added in the resin that step S1 reacts to obtain.It will weigh
Good Fmoc- amino acid (2eq) and 1- hydroxy benzo triazoles HOBt (3eq) are miscible in 5ml DMFs DMF
In solution, N, N'- dicyclohexylcarbodiimides DCC (3eq), dichloromethane 15ml, concussion reaction 30min are added.It is used in combination
20% piperidines-DMF solution 15ml sloughs Fmoc, then by next Fmoc- activations of amino acid, activating solution is filtered anti-to solid phase
Ying Guanzhong, concussion reaction 2h, respectively washed 3 times with DMF, dichloromethane after completion of the reaction.According to such as SEQ ID No:Sequence shown in 3
Row so repeat deprotection → condensation → deprotection, are finished until all amino acid connect, resin after being reacted.
Step S3：Polypeptide is dissociated from resin using diluted acid system
Add acetic acid in resin after above-mentioned steps S2 reactions: trifluoroethanol: dichloromethane=1: 1: 8 (volume ratio) it is molten
Agent common 30ml, oscillating reactions 1h, filtering, resin are washed 3 times with dichloromethane again, and (it is residual that period adds toluene removing to concentration filtrate
Stay acetic acid) obtain the polypeptide crude product with protection.And the solvent of trifluoroacetic acid TFA: DCM=1: 3 (volume ratio) is added in crude product
Common 20ml, stirring reaction 30min, are concentrated to give target polypeptides crude product, then with preparative efficient liquid phase purify and to obtain sterling and synthesize
Peptide P3.
Embodiment 4
Synthetic peptide P4 is prepared according to following steps using solid-phase synthesis, the amino acid sequence of the synthetic peptide P4 is：
Synthetic peptide P3：SGASNPEIGADTQSVDRKT (as shown in SEQ ID No.4)
Step S1：Fmoc- amino acid is connected with resin
2- chlorine triphenyl chlorine resin CTC resin 1.0g (substitution value 1.08mmol/g) are taken to be added to solid phase synthesis pipe
In, CTC resins is fully swelled with N, N'- dicyclohexylcarbodiimide DCM 30ml immersions 30min, activation is stand-by.Then add
Enter 1.5mmol Fmoc- amino acid-OH, dichloromethane 15ml, N, N- diisopropyl ethyl amine DIPEA 0.42ml, concussion is instead
Answer 3h.After reaction terminates, liquid is filtered off, resin is washed each 3 times with methanol, dichloromethane successively, drains stand-by.
Step S2：The progressively connection of amino acid
20% piperidines-DMF solution 15ml, concussion reaction 30min are added in the resin that step S1 reacts to obtain.It will weigh
Good Fmoc- amino acid (2eq) and 1- hydroxy benzo triazoles HOBt (3eq) are miscible in 5ml DMFs DMF
In solution, N, N'- dicyclohexylcarbodiimides DCC (3eq), dichloromethane 15ml, concussion reaction 30min are added.It is used in combination
20% piperidines-DMF solution 15ml sloughs Fmoc, then by next Fmoc- activations of amino acid, activating solution is filtered anti-to solid phase
Ying Guanzhong, concussion reaction 2h, respectively washed 3 times with DMF, dichloromethane after completion of the reaction.According to such as SEQ ID No:Sequence shown in 4
Row so repeat deprotection → condensation → deprotection, are finished until all amino acid connect, resin after being reacted.
Step S3：Polypeptide is dissociated from resin using diluted acid system
Add acetic acid in resin after above-mentioned steps S2 reactions: trifluoroethanol: dichloromethane=1: 1: 8 (volume ratio) it is molten
Agent common 30ml, oscillating reactions 1h, filtering, resin are washed 3 times with dichloromethane again, and (it is residual that period adds toluene removing to concentration filtrate
Stay acetic acid) obtain the polypeptide crude product with protection.And the solvent of trifluoroacetic acid TFA: DCM=1: 3 (volume ratio) is added in crude product
Common 20ml, stirring reaction 30min, are concentrated to give target polypeptides crude product, then with preparative efficient liquid phase purify and to obtain sterling and synthesize
Peptide P4.
Embodiment 5
Indirect elisa method detection antibody titer experiment.
Detected using indirect ELISA method, synthetic peptide P1, P2, P3, P4 are respectively with its respective sets mouse before immune, the 2nd
After secondary immune and final immunization, measurement OD450nm values, the drafting under a series of dilution factors of 8 mouse randomly selected are exempted from
Before epidemic disease, 2 times immune and final immunization after curvilinear motion figure, as shown in Figure 1, Figure 2, Figure 3 and Figure 4.
Visible by Fig. 1, Fig. 2, Fig. 3 and Fig. 4, after immune, the potency of mice serum antibody significantly improves.By than
Compared with wherein synthetic peptide P1 potency is significantly greater than the other three synthetic peptide, and experiment below chooses P1 as epitope peptide coating, enters
The follow-up specificity of row and repeatability are assessed.
Embodiment 6
Synthetic peptide P1_ELISA specificity experiments.
Synthetic peptide P1 is infected into large intestine, golden Portugal, lung gram, lung chain, bacillus subtilis, Candida albicans, excrement with oneself respectively
Enterococcal mice serum carries out ELISA reactions and detects its OD value, the results are shown in Table shown in 1 and Fig. 5.
The cross reaction test data of table 1.
From table 1 and Fig. 5, large intestine, golden Portugal, lung gram, lung chain, bacillus subtilis, Candida albicans detection OD values are all
It is very low, all without notable cross reaction, * *, P<0.001, therefore, enterococcus faecalis gelE protein epitope peptides P1 specificity is good.
Embodiment 7
Synthetic peptide P1_ELISA repeatability assesses experiment.
Synthetic peptide P1 is calculated through the coefficient of variation and assesses repeatability.The results are shown in Table 2, it is seen then that the coefficient of variation 6.2%~
9.1%, repeatability is good.
Table is 2-in-1 to assess experimental result into peptide P1_ELISA repeatability
Above content is to combine specific preferred embodiment further description made for the present invention, it is impossible to is assert
The specific implementation of the present invention is confined to these explanations.For general technical staff of the technical field of the invention,
On the premise of not departing from present inventive concept, some simple deduction or replace can also be made, should all be considered as belonging to the present invention's
Protection domain.
Sequence table
<110>Nanshan District, Shenzhen City the People's Hospital
<120>A kind of B cell antigen epi-position peptide and its kit for enterococcus faecalis gelatinase Protein Detections
<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 (7)
- A kind of 1. B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections, it is characterised in that its core ammonia Base acid sequence is：AMRYGETSTPTGKTYAS.
- 2. the B cell antigen epi-position peptide according to claim 1 for enterococcus faecalis gelatinase Protein Detections, it is special Sign is：At least one end connection of the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections There is the protection peptide no more than 5 amino acid.
- 3. the B cell antigen epi-position peptide according to claim 2 for enterococcus faecalis gelatinase Protein Detections, it is special Sign is：The N-terminal of the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections is connected with two Amino acid HS.
- 4. the B cell antigen epi-position peptide according to claim 2 for enterococcus faecalis gelatinase Protein Detections, it is special Sign is：The C-terminal of the B cell antigen epi-position peptide sequence for enterococcus faecalis gelatinase Protein Detections is connected with GG.
- A kind of 5. antigen for enterococcus faecalis gelatinase Protein Detections, it is characterised in that：It is by making claim The B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections described in 1 is prepared with carrier protein couplet 's.
- 6. the antigen according to claim 5 for enterococcus faecalis gelatinase Protein Detections, it is characterised in that：It is described Carrier protein is KLH.
- A kind of 7. kit for enterococcus faecalis gelatinase Protein Detections, it is characterised in that：It contains such as claim 1 The coating thing of the described B cell antigen epi-position peptide for enterococcus faecalis gelatinase Protein Detections.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108707186A (en) * | 2018-05-28 | 2018-10-26 | 桂林医学院 | Human spermatogoa specific antigen epitope peptide and its polymer and application |
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 |
|---|
| MACOVEI L等: "Enterococcus faecalis with the gelatinase phenotype regulated by the fsr operon and with biofilm-forming capacity are common in the agricultural environment", 《ENVIRONMENTAL MICROBIOLOGY》 * |
| 周霞等: "粪肠球菌抗体间接ELISA检测方法的建立及应用", 《中国兽医科学》 * |
| 孟庆君: "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", 《中国优秀硕士学位论文全文数据库 农业科学辑》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108707186A (en) * | 2018-05-28 | 2018-10-26 | 桂林医学院 | Human spermatogoa specific antigen epitope peptide and its polymer and application |
| CN108707186B (en) * | 2018-05-28 | 2021-11-09 | 桂林医学院 | Human sperm specific antigen epitope peptide, polymer and application thereof |
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