S3 peptide TFA
S3 peptide is a multifunctional synthetic peptide that acts as a LIMK1 inhibitor with an IC50 of 40 μg/mL. S3 peptide blocks cofilin phosphorylation and SDF-1α (HY-P4911)-induced T cell chemotaxis, and reduces viral particle production of HIV-1 and M-PMV. S3 peptide forms dimers via intermolecular disulfide bonds to bind and disrupt LPS micelles, exerting anti-Gram-negative bacterial activity. S3 peptide serves as a targeting moiety for NKA α1 and is used for the construction of PET tracers. S3 peptide is applicable to research related to HIV-1 infection, M-PMV infection, breast cancer, liver cancer and non-small cell lung cancer.
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- Formule: C174H282N52O41S2·xC2HF3O2
- Masse moléculaire:3822.55 (free base)
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Stockage:
Please store the product under the recommended conditions in the Certificate of Analysis.
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Activité biologique
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Chemical Information
- Pureté et documentation
- Références
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Help & FAQs
Activité biologique
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human LIMK1 40 μg/mL (IC50) |
HIV-1 |
S3 peptide (30 μM; 24 h) potently inhibits LIMK1-mediated phosphorylation of cofilin in HeLa and Cos-1 cells[1].
The S3 peptide (10-40 μg/mL) potently inhibits the in vitro kinase activity of LIMK1 isolated from SDF-1α (HY-P4911)-stimulated Jurkat human leukemia T cells in a dose-dependent manner[2].
S3 peptide (40 μg/mL; 30 min) inhibits SDF-1α-induced phosphorylation of cofilin and actin rearrangement in Jurkat human leukemia T cells, while induces chemotactic responses and reduces cell migration levels to near basal levels[2].
The S3 peptide (0.2 μM) binds to negatively charged PC/PG large unilamellar vesicles via a simple adhesion process, with a partition coefficient of 3.8×104, and does not form large aggregates[3].
The S3 peptide (0.2 μM) localizes to the surface of negatively charged PC/PG large unilamellar vesicles, where it interacts specifically with the wild-type S4 peptide (but not with S4 mutants), alters its localization state, and partially protects it from cleavage by proteinase K[3].
The S3 peptide (0.2 μM) specifically co-assembles with the wild-type S4 peptide on negatively charged PC/PG giant unilamellar vesicles, but does not co-assemble with the S4 mutant[3].
The S3 peptide (29.1 μM) specifically interacts with the wild-type S4 peptide in negatively charged PC/PG giant unilamellar vesicles, but does not bind to the S4 mutant, resulting in a moderate increase in the helicity of the peptide complex[3].
S3 peptide (with peptide/lipid molar ratios up to 0.24) does not permeabilize negatively charged PC/PG large unilamellar vesicles, but in this membrane environment, it dose-dependently inhibits the membrane permeabilizing activity of wild-type S4 peptide (but not S4 mutants)[3].
The S3 peptide (0.125-4.00 μM; 3 h) exhibits higher binding affinity for immobilized E. coli O111:B4 LPS than its monomeric form, and reaches binding saturation at 2 μM in ELISA-based LPS binding assays[4].
The S3 peptide (5-20 μg/μL; 30 min pre-incubation, 3-4 h phage incubation) mediates the specific binding of S3 phages to MDA-MB-231 breast cancer cells; a dose-dependent inhibitory effect on phage binding is observed[5].
S3 peptide (80 μM; 4 h) colocalizes with NKA α1 in MDA-MB-231 breast cancer cells[5].
The S3 peptide targets NKA α1 as its primary target, since knockout of NKA α1 in MDA-MB-231 breast cancer cells reduces the binding rate of S3 phage by 2.7 to 4.4-fold[5].
The S3 peptide is associated with S3 phage binding activity, which is positively correlated with the expression of NKA α1 in 9 breast cancer cell lines, with a Pearson correlation coefficient of 0.9705[5].
S3 peptide (30 μM; 48 h) significantly reduces the release of HIV-1 particles in HeLa cells[1].
S3 peptide (30 μM; 48 h) significantly reduces the release of M-PMV particles in Cos-1 cells[1].
S3 peptide (30 μM; 2 h) induces statistically significant clustering of HIV-1 Gag punctate structures on the plasma membrane of HeLa cells[1].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Cell Line:Jurkat human leukemic T cells
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Concentration:40 μg/mL
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Incubation Time:30 min (preincubation prior to 1 min SDF-1α stimulation)
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Result:Completely inhibited the SDF-1α-induced increase in β-actin (filamentous actin) staining observed in control cells at 1 min post-stimulation.
Completely inhibited the SDF-1α-induced increase in P-cofilin staining observed in control cells at 1 min post-stimulation.
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Cell Line:Jurkat human leukemic T cells
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Concentration:40 μg/mL
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Incubation Time:30 min (preincubation prior to 3 h chemotaxis assay)
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Result:Reduced SDF-1α-induced chemotaxis to near basal levels.
Reduced chemotaxis to ~150% of control, compared to ~300% of control with SDF-1α alone.
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Cell Line:E. coli
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Concentration:0.125, 0.25, 0.5, 1, 2 and 4 μM
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Incubation Time:3 h
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Result:Exhibited significantly higher binding affinity for immobilized E. coli O111:B4 LPS than its monomeric counterpart (S3-C27S mutant) over a concentration range of 0.125-4.00 μM following a 3-hour incubation at room temperature.
Reached binding saturation at 2 μM, whereas the monomeric S3-C27S peptide continued to bind in a linear fashion without reaching saturation under the same conditions.
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Cell Line:MDA-MB-231 breast cancer cells
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Concentration:5 μg/μL, 10 μg/μL, 20 μg/μL (pre-incubated for 30 min)
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Incubation Time:3-4 h (phage incubation)
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Result:Reduced S3 phage binding to ~70% at 5 μg/μL.
Reduced S3 phage binding to ~55% at 10 μg/μL.
Reduced S3 phage binding to ~40% at 20 μg/μL.
Exhibited highest binding affinity to MDA-MB-231 cells among six tested high-repeat phage clones, with an OD450nm value ~2.5.
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Cell Line:MDA-MB-231 breast cancer cells
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Concentration:80 μM
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Incubation Time:4 h
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Result:Co-localized with NKA α1 protein in MDA-MB-231 cells, as visualized by overlapping green (streptavidin-FITC) and red (AF594) fluorescence signals in merged confocal images.
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Animal Model:Mice were subcutaneously injected with 1 × 107 MDA-MB-231 cells mixed with 20% Matrigel to establish a breast cancer xenograft model, and the mice were subjected to imaging experiments when tumor volumes reached approximately 300 mm3[5]
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Dosage:1×1010 PFU (S3 phage); 0.5 mg/kg (Cy5-S3); 3.7 MBq (18F-AlF-NOTA-S3); 200 μg (unlabelled S3 peptide for blocking)
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Administration:i.v.; single dose (S3 phage allowed to circulate for 2 h; unlabelled S3 peptide administered 30 min before radiotracer)
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Result:Accumulated at significantly higher levels in tumor tissue (21.5×106 pfu/g) compared to lung (4.3×106 pfu/g), heart (3.5×106 pfu/g), and brain (5.4×106 pfu/g).
Showed high tumor-specific accumulation at 24 hours post-injection, with radiant efficiency in tumors (8×109) dramatically higher than in normal organs (heart, liver, spleen, lung, kidney, brain all <1×109).
Reached peak tumor uptake at 60 minutes post-injection, with tumor uptake measured at 5.1378 %ID/g.
Tumor-to-skin, tumor-to-heart, tumor-to-liver, and tumor-to-bone ratios at 60 minutes were 7.74226, 4.8665, 4.3864, and 2.073, respectively.
Reduced tumor uptake to 2.0133 %ID/g when pre-injected as unlabelled peptide for blocking studies.
Chemical Information
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Masse moléculaire 3822.55 (free base)
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Formule C174H282N52O41S2·xC2HF3O2
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SMILES
O=C(N[C@@H](C)C(N[C@@H](CO)C(NCC(N[C@@H](C(C)C)C(N[C@@H](C)C(N[C@@H](C(C)C)C(N[C@@H](CO)C(N[C@@H](CC(O)=O)C(NCC(N[C@@H](C(C)C)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CCCCN)C(N[C@@H](C(C)C)C(N[C@@H](CC1=CC=CC=C1)C(N[C@@H](CC(N)=O)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCC(N)=O)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CCCCN)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CC2=CNC3=CC=CC=C23)C(N[C@@H](CC4=CC=CC=C4)C(N[C@@H](CCC(N)=O)C(N[C@@H](CC(N)=O)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCSC)C(N[C@@H](CCCCN)C(N[C@@H](CC5=CNC6=CC=CC=C56)C(N[C@@H](CCCCN)C(N[C@@H](CCCCN)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)[C@H](CCSC)N.O=C(O)C(F)(F)F.[x]
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Sequence
Met-Ala-Ser-Gly-Val-Ala-Val-Ser-Asp-Gly-Val-Ile-Lys-Val-Phe-Asn-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys
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Sequence Shortening
MASGVAVSDGVIKVFNRQIKIWFQNRRMKWKK
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Livraison
Room temperature in continental US; may vary elsewhere.
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Stockage
Please store the product under the recommended conditions in the Certificate of Analysis.
Pureté et documentation
Références
[1]. Wen X, et al. ROCK1 and LIM kinase modulate retrovirus particle release and cell-cell transmission events. Journal of virology. 2014 Jun;88(12):6906-21. [Content Brief]
[2]. Nishita M, et al. Stromal cell-derived factor 1alpha activates LIM kinase 1 and induces cofilin phosphorylation for T-cell chemotaxis. Molecular and cellular biology. 2002 Feb;22(3):774-83. [Content Brief]
[3]. Verma R, et al. Phospholipid membrane-interaction of a peptide from S4 segment of KvAP K(+) channel and the influence of the positive charges and an identified heptad repeat in its interaction with a S3 peptide. Biochimie. 2011 Jun;93(6):1001-11. [Content Brief]
[4]. Li P, et al. Perturbation of Lipopolysaccharide (LPS) Micelles by Sushi 3 (S3) antimicrobial peptide. The importance of an intermolecular disulfide bond in S3 dimer for binding, disruption, and neutralization of LPS. J Biol Chem. 2004 Nov 26;279(48):50150-6. [Content Brief]
[5]. Wang Q, et al. Identification of a sodium pump Na/K ATPase α1-targeted peptide for PET imaging of breast cancer. Journal of controlled release : official journal of the Controlled Release Society. 2018 Jul 10;281:178-188. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
S3 peptide TFA Related Classifications
HY-P12114 Related Classifications
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