CN110194793A - It is a kind of inhibit actin recombination polypeptide and application - Google Patents
It is a kind of inhibit actin recombination polypeptide and application Download PDFInfo
- Publication number
- CN110194793A CN110194793A CN201810159838.3A CN201810159838A CN110194793A CN 110194793 A CN110194793 A CN 110194793A CN 201810159838 A CN201810159838 A CN 201810159838A CN 110194793 A CN110194793 A CN 110194793A
- Authority
- CN
- China
- Prior art keywords
- cell
- actin
- polypeptide
- hiv
- recombination
- 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.)
- Granted
Links
Classifications
-
- 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
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a kind of polypeptide of inhibition actin recombination and application, amino acid sequence is to encode the nucleotide sequence of the gene of ABS1p as shown in SEQ ID NO.2 shown in SEQ ID NO.1.ABS1p, can be with primary CD4 based on the ABS of ABD sequence in non-flesh type α-actinin+F-actin is combined in T cell.It is experimentally confirmed that ABS1p inhibits the infection of the recombination and HIV-1 of T cell F-actin to T cell, it is expected to develop into the inhibitor for having the function for the treatment of AIDS, or can be combined with other inhibitor and reach ideal therapeutic effect.
Description
Technical field
The invention belongs to bio-pharmaceutical engineer technology domains, and in particular to it is a kind of inhibit actin recombination polypeptide and answer
With polypeptide provided by the invention is by inhibiting actin recombination that HIV-1 is inhibited to infect.
Background technique
Human immunodeficiency virus (Human Immunodeficiency Virus, HIV) is infection human immune system
The slow virus of cell belongs to Retroviridae, lentivirus, and body can be made to generate " acquired immunodeficiency syndrome "
(Acquir ed Immune Deficiency Syndrome, AIDS), i.e. AIDS.Body immune system is caused to damage, it is right
Human health causes greatly to threaten.
Currently, anti-AIDS drug is broadly divided into: reverse transcriptase inhibitor, protease inhibitors, integrase inhibitor and
Four major class of entry inhibitor.Different from preceding three classes drug, entry inhibitor targets the early stage of virus infection.According to medicine target
Enter three steps of cell to HIV, entry inhibitor is divided into adsorption inhibitor, accessory receptor inhibitor and fusion again and inhibits
Agent.
Cytoskeleton is a dynamic structure, includes microfilament, intermediate filament and three kinds of micro-pipe compositions.Main function includes dimension
Hold the form of cell, the movement of mediated cell and macromolecular and the transport of organelle etc..Microfilament by actin (actin),
Actin binding protein and myosin (myosin) are constituted.Actin monomers form a string of actins one by one
Chain, the such actin chain of two strings wind mutually the helical fiber being assembled into and are known as fiber shape actin (Fibrous
Actin, F-actin).Actin F-actin is the basis of cell movement and migration, and is related to host cell immune response
Multiple processes.In course of infection of the virus to target cell, the actin of host cell is cell entry host cell
The first line of defence.As inalienable part in intracellular molecules network, actin cytoskeleton is also the target of pathogen.
Since actin can be with the interaction of many protein non-specifics, and the influencing mechanism that actin infects HIV-1
And it is indefinite, so that people are not high to the research interest of cytoskeleton.In addition, the cytotropic basis of target constitutes and will cause seriously
Cytotoxicity be therefore usually under suspicion for the antiviral therapy of actin.
Recent studies suggest that mammalian cell cortex F-actin is height change, the time of half-life period is 20-
25s is adjusted by cofilin, α-actinin etc..α-actinine (α-actinin) is that one kind makes the bundles of guarantor of actin
Albumen is kept, there are two actin binding sites apart from each other, belong to highly conserved Actin binding protein family-blood shadow egg
White superfamily is a kind of important actin crosslinking protein in cytoskeleton.α-actinin and intracellular integrin, calcium are viscous
The synergistic effect such as signaling molecule in element and signal transduction pathway can stablize cell adherence, adjust cell shape and movement.
It is analyzed by applicant, α-actinin is made of 3 structural domains, and N-terminal is actin binding structural domain
(actin-bin ding domain, ABD), in ABD containing 3 actin binding sites (Actin-binding sites,
ABS), it is distributed in the surface ABD (actin binding domain, be made of CH1 and CH2), is ABS1, ABS2 and A respectively
BS3.Wherein ABS1 is distributed in the intersection of CH1 and CH2；ABS2, which is distributed in, is divided into the surface CH1 and part positioned at C H1 and CH2
Intersection；ABS3 is located at the surface CH2.Since ABS is the binding site of actin Yu α-actinin, and ABS is in α-actinin
Steric hindrance is not present in the surface of albumin A BD structural domain in conjunction with actin.Therefore, screening act in is combined with α-actinin
Inhibitor, can by introduce external source ABS peptide fragment, competitively in conjunction with actin, to inhibit endogenous α-actinin
And the combination of actin.The design of peptide inhibitor can be carried out based on this 3 amino acid sequences of ABS1, ABS2 and ABS3
Optimization screens the affinity ratio α-actinin and the stronger candidate inhibitor of actin of be inhibited agent and actin, to play
Competitive binding and then the effect inhibited.
It there is no the combination of Competitive assays α-actinin and actin both at home and abroad at present and play and inhibit the more of F-actin recombination
Peptide medicament.Therefore, the present invention is to be put forward for the first time the concept of the competitive inhibitor.Agent designs peptide inhibitor based on ABS,
Other amino acid are not added, can be more applicable for clinical application to avoid causing unnecessary immunogenicity to occur.Of the invention
Inhibitor derives from the ABS of α-actinin, and immunogenicity is low, and the inhibitor is solvable, is conducive to patent medicine.Biochemical test and in real time
Tracer confirms that the inhibitor ABS1p screened based on ABS can influence the recombination of F-actin and α-actinin in T cell, and
The infection of HIV-1 is had a significant impact.In addition, the peptide inhibitor that the present invention designs, to inhibit F-actin to recombinate the side of specifying
To.
Summary of the invention
The present invention provides a kind of polypeptide A BS1p for inhibiting actin recombination and HIV-1 infection, and amino acid sequence is such as
Shown in SEQ ID NO.1.
It is another object of the present invention to provide the nucleotide sequence of polypeptide A BS1p shown in coding SEQ ID NO.1,
As long as the nucleotide sequence for encoding the polypeptide is the content that the present invention protects, it is preferred that the nucleotides sequence is classified as SEQ
Shown in ID NO.2.
Final object of the present invention is the provision of the application of polypeptide A BS1p, including the use of polypeptide of the invention
ABS1p is prepared into the drug for inhibiting actin recombination, or is prepared into the drug or of the invention for inhibiting HIV-1 infection
Polypeptide A BS1p and other combination of active principles are prepared as inhibiting the drug of actin recombination and HIV-1 infection.
In order to achieve the above object, the present invention takes following technical measures:
A kind of polypeptide A BS1p, amino acid sequence such as SEQ ID NO.1 inhibiting actin recombination and HIV-1 infection
Shown, the polypeptide is by being commercially synthesized to obtain.
The nucleotide sequence of polypeptide A BS1p shown in coding SEQ ID NO.1 is also the content that the present invention protects, it is preferred that
The nucleotides sequence is classified as shown in SEQ ID NO.2.
The application of polypeptide A BS1p is prepared into the medicine for inhibiting actin recombination including the use of polypeptide A BS1p of the invention
Object, or it is prepared into the drug for inhibiting HIV-1 infection or polypeptide A BS1p of the invention and the preparation of other combination of active principles
For the drug for inhibiting actin recombination and HIV-1 infection.
Compared with prior art, the present invention having the following advantages that and effect:
A, polypeptide provided by the invention, compared to other extensive actin related inhibitors, molecular weight is smaller (1819Da), and
Specific binding capacity is stronger.
B, the present invention based on the ABS on α-actinin, by introduce external source ABS peptide fragment, competitively with
Actin is combined, and is expected to develop into the entry inhibitor for inhibiting HIV-1, and ABS1p derives from α-actinin, immunogenicity phase
To weaker.
C, polypeptide A BS1p contains only 15 amino acid residues, and length is shorter, at low cost, the period is short, is appropriate for quickly big rule
Mould
Production.
Detailed description of the invention
Figure 1A is that various concentration ABS1p enters CD4 to HIV-1+The influence result figure of T cell.
Figure 1B is the influence result figure that various concentration ABS1p enters CEM-ss cell to HIV-1.
Fig. 2A is that Kymograph analysis HIV-1 infects CD4+The mutual variation of F-actin and α-actinin is closed in T cell
System's figure.
Fig. 2 B is that Kymograph analysis ABS1p infects CD4 to HIV-1+F-actin and α-actinin under the influence of T cell
Mutual variation relation figure.
Fig. 3 A is the mutual variation that Kymograph analyzes that HIV-1 infects F-actin and α-actinin in CEM-ss cell
Relational graph.
Fig. 3 B is that Kymograph analysis ABS1p infects F-actin and α-actinin under CEM-ss impact cell to HIV-1
Mutual variation relation figure.
Specific embodiment
By following detailed description combination attached drawing it will be further appreciated that the features and advantages of the invention.Provided implementation
Example is only the explanation to the method for the present invention, remaining content without limiting the invention in any way announcement.The embodiment of the present invention
The technical solution is if not otherwise specified the conventional scheme of this field.The ammonia of polypeptide A BS1p used in the embodiment of the present invention
Base acid sequence is to be obtained shown in SEQ ID NO.1 by being commercially synthesized.
Embodiment 1:
ABS1p enters CD4 to HIV-1+The inhibiting effect of T cell or CEM-ss cell
Research ABS1p enters CD4 to HIV-1+When T cell or the inhibiting effect of CEM-ss cell, cell is first adjusted separately
Concentration is to 1 × 106Cells/mL, every group of cell volume are 2mL；Polypeptide A BS1p is added in cell system, is placed in 37 DEG C of cultures
Case is incubated for 1h；After pretreatment, cell is added in 200ng p24HIV-1, sets 37 DEG C, 5%CO2Under the conditions of infect 3h；Infect completion
Afterwards, with PBS rinse cell 3 times, fresh culture medium is added, makes cell concentration 1 × 106Cells/mL continues to be placed in 37 DEG C,
5%CO2Under the conditions of cultivate 48h.
When measuring infectious effect of the virus to cell, virus infection is detected using Intracellular p24staining
Intracellular p24 content afterwards.Cells following viral infection, PBS rinse cell 3 times, further according to Anti-HIV- are collected in experiment first
The antigen-antibody reaction of 1p24antibody and intracellular p24 carry out intracellular p24 dyeing.Steps are as follows for its experiment: (1)
It is fixed: cell after cleaning being centrifuged 5min in 200 × g, collects cell precipitation；(2) 4% poly first is added in collecting cell
Aldehyde, featheriness mix, the fixed cell 30min of room temperature；(3) penetrating: cell after fixation being centrifuged 5min in 200 × g, it is heavy to collect cell
It forms sediment, 0.5%Triton PBS is added, in the penetrating 10min of room temperature；(4) it washs: being washed cell 2 times with the PBS containing 4%BSA, received
Collect cell precipitation；(5) one anti-bindings: discarding cleaning solution, leaves the PBS containing 4%BSA of about 100 μ L, cell is resuspended, and be added
0.5 μ L Anti-HIV-1p24antibody (Abcam, ab9044), is incubated overnight in 4 DEG C；(6) it is washed with the PBS containing 4%BSA
It washs cell 3 times；(7) two anti-bindings: abandoning cleaning solution, and the diluted Anti-mouse IgG of 1:1000 is added in cell
Fab2Alexa Fluor (R) 555Molecular Probes (Cell Signaling Technology, 4409S), room temperature is incubated
Educate 30min；(8) it washs: being washed cell 2 times with the PBS containing 4%BSA, add Hank solution and wash cell 2 times；(9) it abandons and washes
Liquid is washed, cell is resuspended with 500 μ L, 1% paraformaldehyde, is analyzed using FACS (BD Biosciences).
As a result such as Figure 1A -1B, in CD4+In T cell, when ABS1p concentration is 10 μ g/mL and 1 μ g/mL, to HIV-1's
Infection has significant impact (Figure 1A).In T cell system CEM-ss cell, when ABS1p concentration is 10 μ g/mL, to HIV-1
Infection have significantly affect (Figure 1B).
Embodiment 2:
ABS1p influences the recombination of F-actin and α-actinin in T cell:
In order in CD4+The dynamic relationship of F-actin and α-actinin is studied in T cell, T cell system CEM-ss cell,
By plasmid pECFP-C1-lifeact and piRFP- α-actinin cotransfection CD4+T cell or CEM-ss cell are, it can be achieved that living thin
The fluorescent marker of born of the same parents F-actin and α-actinin.Specific implementation process are as follows: (1) to 100 μ L room temperatures
The CD4 that Solution is resuspended+2 μ g pECFP-C1-Lifeact and 2 μ g piRFP- α-are added in T cell or CEM-ss cell
Actinin is mixed gently；(2) bioblast mixture is added in the sulculus of electric revolving cup, covers electric revolving cup cap；(3) it is arranged
LONZA consideration convey instrument program: selection V-024 program will be inserted into consideration convey instrument slot, operation selection equipped with the electric revolving cup of cell and plasmid
Program；(4) EP (end of program) immediately takes out electric revolving cup, adds 500 μ L RPMI-1640 culture mediums into electric revolving cup, gently
Cell suspension is sucked out, is added in the capsule of the RPMI 1640 containing 10%FBS of pre-equilibration, sets 37 DEG C, 5%CO2Condition training
Feeding 6h makes gene expression；(5) after 6h, the RPMI 1640 containing 10%FBS, in 37 DEG C, 5%CO are replaced2CMC model；(6)24h
After collect cell, be centrifuged 10min in 200 × g, 100 μ L HIV-1-QDs viruses are added, gently to 100 μ L in adjustment cell volume
It is uniformly mixed, sets laser co-focusing glass bottom capsule, sealed with paraffin, be incubated for 30min under the conditions of 4 DEG C.ABS1p is verified to disease
When the influence of poison infection, 10 μ g/mL polypeptide A BS1p are first added in cell system, is placed in 37 DEG C of incubators and is incubated for 1h, then in
200 × g centrifuge cell 10min, adjustment cell volume to 100 μ L are added the pretreated HIV-1-QDs virus of 100 μ L, are gently mixed
Even, paraffin seal glass bottom capsule is incubated for 30min under the conditions of 4 DEG C.(7) it is observed under transposition laser confocal microscope, image
Data are statisticallyd analyze using Volocity software.
As a result such as Fig. 2A -2B and 3A-3B, HIV-1-QDs is added in label cell system, it is thin to observe viruses adsorption in real time
The fluorescence signal in born of the same parents region changes, and research is found: in cell entry region, CD4+T cell (Fig. 2A) and T cell system CEM-ss are thin
Asynchronous trend, and aggregation of the α-actinin prior to F-actin is presented in F-actin and α-actinin in born of the same parents (Fig. 3 A)；And
Viruses adsorption region on the cell of polypeptide A BS1p processing, CD4+T cell (Fig. 2 B) and T cell system CEM-ss cell (Fig. 3 B)
Middle F-actin and α-actinin is in synchronous regime.Should the result shows that, polypeptide A BS1p has good Competitive assays activity,
Its as it is a kind of have potential F-actin recombinant inhibitor be worth carrying out deeper into research and development, to inhibit HIV-1 sense
Have a finger in every pie bright new research direction.
Sequence table
<110>Wuhan Virology Institute,Chinan academy of Sciences
<120>a kind of polypeptide for inhibiting actin recombination and application
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 15
<212> PRT
<213>artificial sequence (Artificial Sequence)
<400> 1
Arg Lys Thr Phe Thr Ala Trp Cys Asn Ser His Leu Arg Lys Ala
1 5 10 15
<210> 2
<211> 45
<212> DNA
<213>artificial sequence (Artificial Sequence)
<400> 2
agaaagacat tcacggcatg gtgtaactcc cacctccgga aggcg 45
Claims (6)
1. a kind of polypeptide for inhibiting actin recombination, the polypeptid acid sequence is as shown in SEQ ID NO.1.
2. encoding the nucleotide sequence of polypeptide described in claim 1.
3. nucleotide sequence according to claim 2, the sequence is shown in SEQ ID NO.2.
4. polypeptide described in claim 1 or nucleotides sequence as claimed in claim 2, which are listed in preparation, inhibits actin recombination medicine
Application in object.
Inhibit in HIV-1 infection medicine 5. polypeptide described in claim 1 or nucleotides sequence as claimed in claim 2 are listed in preparation
Application.
6. application according to claim 4 or 5, the drug is pharmaceutically acceptable preparation.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201810159838.3A CN110194793B (en) | 2018-02-26 | 2018-02-26 | Polypeptide for inhibiting actin recombination and application |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201810159838.3A CN110194793B (en) | 2018-02-26 | 2018-02-26 | Polypeptide for inhibiting actin recombination and application |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN110194793A true CN110194793A (en) | 2019-09-03 |
| CN110194793B CN110194793B (en) | 2020-12-01 |
Family
ID=67751244
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201810159838.3A Active CN110194793B (en) | 2018-02-26 | 2018-02-26 | Polypeptide for inhibiting actin recombination and application |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN110194793B (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1342668A (en) * | 2000-09-12 | 2002-04-03 | 上海博德基因开发有限公司 | Polypeptide-F actin binding factor 32.78 and polynucleotide for coding it |
| CN1425687A (en) * | 2001-12-19 | 2003-06-25 | 复旦大学 | Polypeptide-protein-70.95 containing actin binding structural domain and polynucleotide for encoding such polypeptide |
| US20100292181A1 (en) * | 2006-05-05 | 2010-11-18 | George Mason Intellectual Properties, Inc. | Compositions and methods for detecting and treating hiv infections |
| CN106397548A (en) * | 2015-07-29 | 2017-02-15 | 复旦大学 | Polypeptide for inhibiting HIV infection, and pharmaceutical uses thereof |
| US20180002390A1 (en) * | 2016-07-02 | 2018-01-04 | Virongy L.L.C. | Compositions and methods for using actin-based peptides to modulate cellular bioactivity and cellular susceptibility to intracellular pathogens |
-
2018
- 2018-02-26 CN CN201810159838.3A patent/CN110194793B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1342668A (en) * | 2000-09-12 | 2002-04-03 | 上海博德基因开发有限公司 | Polypeptide-F actin binding factor 32.78 and polynucleotide for coding it |
| CN1425687A (en) * | 2001-12-19 | 2003-06-25 | 复旦大学 | Polypeptide-protein-70.95 containing actin binding structural domain and polynucleotide for encoding such polypeptide |
| US20100292181A1 (en) * | 2006-05-05 | 2010-11-18 | George Mason Intellectual Properties, Inc. | Compositions and methods for detecting and treating hiv infections |
| CN106397548A (en) * | 2015-07-29 | 2017-02-15 | 复旦大学 | Polypeptide for inhibiting HIV infection, and pharmaceutical uses thereof |
| US20180002390A1 (en) * | 2016-07-02 | 2018-01-04 | Virongy L.L.C. | Compositions and methods for using actin-based peptides to modulate cellular bioactivity and cellular susceptibility to intracellular pathogens |
Non-Patent Citations (5)
| Title |
|---|
| B. SJÇBLOM等: "a-Actinin structure and regulation", 《CELLULAR AND MOLECULAR LIFE SCIENCES》 * |
| MÓNICA GORDÓN-ALONSO等: "Actin-binding Protein Drebrin Regulates HIV-1-triggered Actin Polymerization and Viral Infection", 《THE JOURNAL OF BIOLOGICAL CHEMISTRY》 * |
| WEN YIN等: "Real-time imaging of individual virion-triggered cortical actin dynamics for human immunodeficiency virus entry into resting CD4 T cells", 《NANOSCALE》 * |
| 任敏: "HIV-1与CD4+T细胞F-actin相互作用的实时动态成像研究", 《万方数据》 * |
| 王卓: "HIV感染者趋化因子变化及其对杀伤细胞功能和HIV感染的作用及机制研究", 《中国博士学位论文全文数据库（电子期刊） 医药卫生科技辑》 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN110194793B (en) | 2020-12-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Ding et al. | Enfuvirtide (T20)-based lipopeptide is a potent HIV-1 cell fusion inhibitor: implications for viral entry and inhibition | |
| US7829683B2 (en) | Polynucleotides encoding modified HIV-1 gp41 membrane polypeptides | |
| CA2092519C (en) | Synthetic polypeptides as inhibitors of hiv-1 | |
| A Yi et al. | Inhibition of HIV entry by targeting the envelope transmembrane subunit gp41 | |
| US8354498B2 (en) | CD4 mimic peptides and their uses | |
| Nishikawa et al. | Electrostatically constrained α-helical peptide inhibits replication of HIV-1 resistant to enfuvirtide | |
| US11203617B2 (en) | Immunogenic trimers | |
| Schnur et al. | NMR mapping of RANTES surfaces interacting with CCR 5 using linked extracellular domains | |
| Lusso et al. | Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity | |
| Secchi et al. | Enhancement of anti-HIV-1 activity by hot spot evolution of RANTES-derived peptides | |
| CN105646717B (en) | Long-acting HIV fusion inhibitor and application thereof | |
| CN110194793A (en) | It is a kind of inhibit actin recombination polypeptide and application | |
| CN102471372A (en) | Alphabodies for HIV entry inhibition | |
| CN106397548A (en) | Polypeptide for inhibiting HIV infection, and pharmaceutical uses thereof | |
| Bolton et al. | Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines | |
| Boucher et al. | Immune response and epitope mapping of a candidate HIV‐1 p17 vaccine HGP30 | |
| Li et al. | A simple, rapid, and sensitive system for the evaluation of anti-viral drugs in rats | |
| Fiorentini et al. | Synthetic peptide AT20 coupled to KLH elicits antibodies against a conserved conformational epitope from a major functional area of the HIV-1 matrix protein p17 | |
| WO2010041237A2 (en) | Cyclic v3 peptides for anti hiv-1 vaccine | |
| CN110087679A (en) | The virus-like particle with high density coating for induction of antibodies expression | |
| CN113461811A (en) | Bispecific anti-HIV-1 antibody | |
| Izumi et al. | Mechanism of resistance to S138A substituted enfuvirtide and its application to peptide design | |
| Zhu et al. | HIV-1 gp120-CXCR4 recognition probed with synthetic nanomolar affinity D-peptides containing fragments of gp120 V3 loop | |
| CN104892744A (en) | Active polypeptide with function of antagonizing chemokine receptor CXCR4 as well as design preparation and biomedical application of active polypeptide | |
| CN106132981B (en) | β-hair clip peptide with the ntiviral characteristic for dengue virus |
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 |