Peptide T
目录号 : GC32309
PeptideT是源自HIV-1gp120的V2区的八肽。PeptideT是CD4受体的配体，可阻止HIV与CD4受体结合。
Cas No.:106362-32-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Cell experiment: | Peripheral blood mononuclear cells are stimulated with PHA (5 mg/mL) along with various concentrations of peptide T (10-6-10-12 M) for 48 h at 37°C. Supernatants are collected and frozen until analysis[3]. |
Animal experiment: | Rats[4]Peptide T (125, 250, 500, 800 μg) is randomly given subcutaneously to Female Lewis rats aged 6-8 weeks in the hind foot flanks in a final volume of 0.2 mL. Control animals receive the same volume of saline alone[4]. |
References: [1]. Ruff MR, et al. Peptide T[4-8] is core HIV envelope sequence required for CD4 receptor attachment. Lancet. 1987 Sep 26;2(8561):751. | |
Peptide T is an octapeptide from the V2 region of HIV-1 gp120. Peptide T is a ligand for the CD4 receptor and prevents binding of HIV to the CD4 receptor.
Peptide T acts to block viral entry as it inhibits in the MAGI cell assay and blocks infection in the luciferase reporter assay using HIV virions pseudotyped with ADA envelope. Peptide T selectively inhibits HIV replication using chemokine receptor CCR5 compared to CXC4[2]. Peptide T at 10-8 M induces IL-10 production by the human Th2 cell line and PBMC. Also peptide T at 10-9 M concentration significantly inhibits IFN-g production by PBMC[3].
Peptide T is administered subcutaneously at different doses and phases of the experimental autoimmune encephalomyelitis (EAE) disease, but Peptide T neither prevents nor ameliorates EAE[4].
[1]. Ruff MR, et al. Peptide T[4-8] is core HIV envelope sequence required for CD4 receptor attachment. Lancet. 1987 Sep 26;2(8561):751. [2]. Ruff MR, et al. Peptide T inhibits HIV-1 infection mediated by the chemokine receptor-5 (CCR5). Antiviral Res. 2001 Oct;52(1):63-75. [3]. Raychaudhuri SP, et al. Immunomodulatory effects of peptide T on Th 1/Th 2 cytokines. Int J Immunopharmacol. 1999 Sep;21(9):609-15. [4]. Sáez-Torres I, et al. Peptide T does not ameliorate experimental autoimmune encephalomyelitis (EAE) in Lewis rats. Clin Exp Immunol. 2000 Jul;121(1):151-6.
| Cas No. | 106362-32-7 | SDF | |
| Canonical SMILES | Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr | ||
| 分子式 | C35H55N9O16 | 分子量 | 857.86 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.1657 mL | 5.8285 mL | 11.6569 mL |
| 5 mM | 0.2331 mL | 1.1657 mL | 2.3314 mL |
| 10 mM | 0.1166 mL | 0.5828 mL | 1.1657 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Update on D-ala-peptide T-amide (DAPTA): a viral entry inhibitor that blocks CCR5 chemokine receptors
Curr HIV Res 2003 Jan;1(1):51-67.PMID:15043212DOI:10.2174/1570162033352066.
Peptide T, named for its high threonine content (ASTTTNYT), was derived by a database search which assumed that a relevant receptor binding epitope within env (gp120) would have sequence homology to a known signaling peptide. Binding of radiolabeled gp120 to brain membranes was displaced by Peptide T and three octapeptide analogs (including "DAPTA", Dala1-peptide T-amide, the protease-resistant analog now in Phase II clinical trials) with the same potency that these four octapeptides blocked infectivity of an early passage patient isolate. This 1986 report was controversial due to a number of laboratories' failure to find Peptide T antiviral effects; we now know that Peptide T is a potent HIV entry inhibitor selectively targeting CCR5 receptors with minimal effects on the X4 tropic lab adapted virus exclusively in use at that time. Early clinical trials, which demonstrated lack of toxicity and focused on neurological and neurocognitive benefits, are reviewed and data from a small ongoing Phase II trial--the first to assess Peptide T's antiviral effects--are presented. Studies using infectivity, receptor binding, chemotaxis, and blockade of gp120-induced neurotoxicity in vitro and in vivo are reviewed, discussed and presented here. Peptide T and analogs of its core pentapeptide, present near the V2 stem of numerous gp120 isolates, are potent ligands for CCR5. Clinical data showing Peptide T's immunomodulation of plasma cytokine levels and increases in the percentage of IFNgamma secreting CD8+ T cells in patients with HIV disease are presented and suggests additional therapeutic mechanisms via regulation of specific immunity.
Cancer immunotherapy: moving forward with Peptide T cell vaccines
Curr Opin Immunol 2017 Aug;47:57-63.PMID:28734176DOI:10.1016/j.coi.2017.07.003.
Recent advances in cancer immunology, such as the discovery of immune checkpoint inhibitors, have validated immune cells as potential key players for effective cancer treatment. The efficacy of these therapies seems to be codependent on a tumor-reactive T lymphocyte response. For many years, numerous attempts and strategies in developing vaccines to generate tumor-reactive T cells have yielded poor results in the clinic due to suboptimal immunogenicity and the inability to overcome an immunosuppressive tumor microenvironment. In this review, we summarize past and current advances in T cell vaccines and describe our experience in developing optimized methods for antigen/adjuvant selection and vaccine administration in order to induce powerful anti-tumor responses.
On the initial trigger of myasthenia gravis and suppression of the disease by antibodies against the MHC peptide region involved in the presentation of a pathogenic T-cell epitope
Crit Rev Immunol 2001;21(1-3):1-27.PMID:11642597doi
Myasthenia gravis (MG) is a disabling autoimmune disease caused by autoantibodies (auto-Abs) against the self-acetylcholine receptor (AChR). Although a great deal of information is known about the molecular and cellular parameters of the disease, its initial trigger, however, is not known. To study the possibility of the involvement of microbial antigens that mimic AChR in triggering MG, we have searched the microbial proteins in the data bank for regions that are similar in structure to the regions of human (h) AChR alpha chain recognized by auto-Abs in MG patients. Hundreds of candidate structures on a large number of bacterial and viral proteins were identified. To test the feasibility of the idea, we synthesized four microbial regions similar to each of the major autodeterminants of hAChR (alpha12-27, alpha111-126, alpha122-138, alpha182-198) and investigated their ability to bind auto-Abs in MG and normal sera controls. It was found that MG sera potentially recognized a significant number of these microbial regions. The results indicate that in some MG cases, immune responses to microbial antigens may cross-react with self-antigen (in this case hAChR) and could constitute initial triggers of the disease. Although anti-AChR Abs directly contribute to the degradation of AChR at the neuromuscular junctions, autoreactive T cells provide help to B cells that synthesize anti-AChR auto-Abs. To cause MG, T cells must recognize the pathogenic epitopes in the context of MHC class II molecules related to MG. The ability to regulate AChR presentation (hence AChR-reactive T-cell activation) could form the basis of an effective strategy for the control of autoimmunity in MG by selectively inhibiting the function of the Ir gene loci linked to disease susceptibility. An animal model of MG (experimental autoimmune MG, EAMG) can be induced in C57BL/6 (B6, H-2b) mice by immunization with Torpedo californica (t) AChR. A mutant mouse of B6, B6.C-H-2bm12 (bm12), which has three amino acid changes (at residues 67, 70, and 71) in the I-A beta(b) subunit, is resistant to EAMG development. Recently, we showed that region 62-76 of I-A beta(b), which contains the above residues, is involved in the binding to a pathogenic T-cell epitope within Peptide T alpha146-162. We have prepared several monoclonal antibodies (mAbs) against peptide I-A beta(b)62-76, which are highly cross-reactive with I-A(b) molecules. These mAbs inhibited in vitro the proliferation of disease-related T cells of B6 specific to tAChR Peptide T alpha146-162. Passive transfer of these mAbs suppressed the occurrence of clinical EAMG, which was accompanied by lower T-cell and Ab responses to tAChR. The results indicated that blocking disease-related MHC by targeting a disease-associated region on MHC molecules could be an effective, straightforward, and feasible strategy for immunointervention in MG.
Folding molecular dynamics simulation of T-peptide, a HIV viral entry inhibitor: Structure, dynamics, and comparison with the experimental data
J Comput Chem 2022 May 30;43(14):942-952.PMID:35333419DOI:10.1002/jcc.26850.
Peptide T is a synthetic octapeptide fragment, which corresponds to the region 185-192 of the gp120 HIV coat protein and functions as a viral entry inhibitor. In this work, a folding molecular dynamics simulation of Peptide T in a membrane-mimicking (DMSO) solution was performed with the aim of characterizing the peptide's structural and dynamical properties. We show that Peptide T is highly flexible and dynamic. The main structural characteristics observed were rapidly interconverting short helical stretches and turns, with a notable preference for the formation of 尾-turns. The simulation also indicated that the C-terminal part appears to be more stable than the rest of the peptide, with the most preferred conformation for residues 5-8 being a 尾-turn. In order to validate the accuracy of the simulations, we compared our results with the experimental NMR data obtained for the T-peptide in the same solvent. In agreement with the simulation, the NMR data indicated the presence of a preferred structure in solution that was consistent with a 尾-turn comprising the four C-terminal residues. An additional comparison between the experimental and simulation-derived chemical shifts also showed a reasonable agreement between experiment and simulation, further validating the simulation-derived structural characterization of the T-peptide. We conclude that peptide folding simulations produce physically relevant results even when performed with organic solvents that were not part of the force field parameterization procedure.
Speculations around the mechanism behind the action of Peptide T in the healing of psoriasis: a minireview
Acta Derm Venereol 1993 Dec;73(6):401-3.PMID:7906447DOI:10.2340/0001555573401403.
Peptide T, the HIV envelope-derived fragment Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr, has already been used to successfully treat psoriatic patients without major side-effects. The underlying reason for the positive effect is, however, at present unknown. In the following minireview, we summarize today's knowledge regarding Peptide T's interaction with other chemical messenger molecules, such as somatostatin, vasoactive intestinal polypeptide (VIP) and epidermal growth factor (EGF), within the human skin, and, finally, speculate about their relationship to each other. In summary, we believe that the clearance effect of Peptide T on psoriasis will open up new avenues with regard to the concept of the pathogenesis of as well as the clinical attendance to this disease.