Chlorotoxin TFA

Modify Date: 2024-01-10 14:24:32

Chlorotoxin TFA Structure
Chlorotoxin TFA structure
Common Name Chlorotoxin TFA
CAS Number 163515-35-3 Molecular Weight 3995.70000
Density N/A Boiling Point N/A
Molecular Formula C158H249N53O47S11 Melting Point N/A
MSDS Chinese USA Flash Point N/A

 Use of Chlorotoxin TFA


Chlorotoxin is a 36 amino-acid peptide from the venom of the Israeli scorpion Leiurus quinquestriatus with anticancer activity. Chlorotoxin is a chloride channel blocker.

 Names

Name Chlorotoxin
Synonym More Synonyms

 Chlorotoxin TFA Biological Activity

Description Chlorotoxin is a 36 amino-acid peptide from the venom of the Israeli scorpion Leiurus quinquestriatus with anticancer activity. Chlorotoxin is a chloride channel blocker.
Related Catalog
Target

Target: Chloride Channel[1]

In Vitro Chlorotoxin (Chlorotoxin) preferentially binds to tumor cells and has been harnessed to develop an imaging agent to help visualize tumors during surgical resection. In addition, chlorotoxin has potential as a vehicle to deliver anti-cancer drugs specifically to cancer cells. Chlorotoxin is shown to bind glioma cells, but is unable to bind normal rat astrocytes and Te671, a human rhabdomyosarcoma cell line. Chlorotoxin inhibits the migration of U251MG (glioma) cells, with an IC50 of 600 nM[2]. Chlorotoxin binds to glioma cells is specific and involves high affinity (Kd=4.2 nM) and low affinity (Kd=660 nM) binding sites[3].Small conductance chloride channels are shown to be potently blocked by Chlorotoxin. Chlorotoxin has been used as a general pharmacological tool to investigate the function of chloride channels[4].
In Vivo Chlorotoxin shows insecticidal activity on insects and other invertebrates. After the administration of I-Chlorotoxin to tumor-bearing mice, the peptides accumulated within the tumor[2].Chlorotoxin selectively accumulates in the brain of tumor-bearing mice with calculated brain: muscle ratios of 36.4% of injected dose/g (ID/g), as compared to 12.4%ID/g in control animals[3].
Animal Admin Mouse: At 24, 48, 72, and 96 h after tumor-bearing and control SCID mice are injected with 125l-labeled Chlorotoxin, they are anesthetized and imaged. Both 125I- and 131l-labeled Chlorotoxin-injected animals and their control counterparts are killed at indicated time points for biodistribution studies[3].
References

[1]. DeBin JA, et al. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am J Physiol. 1993 Feb;264(2 Pt 1):C361-9.

[2]. Ojeda PG, et al. Chlorotoxin: Structure, activity, and potential uses in cancer therapy. Biopolymers. 2016 Jan;106(1):25-36.

[3]. Soroceanu L, et al. Use of chlorotoxin for targeting of primary brain tumors. Cancer Res. 1998 Nov 1;58(21):4871-9.

[4]. Dardevet L, et al. Chlorotoxin: a helpful natural scorpion peptide to diagnose glioma and fight tumor invasion. Toxins (Basel). 2015 Mar 27;7(4):1079-101.

 Chemical & Physical Properties

Molecular Formula C158H249N53O47S11
Molecular Weight 3995.70000
Exact Mass 3992.50000
PSA 2001.75000
Storage condition -20°C

 Safety Information

Personal Protective Equipment Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
RIDADR NONH for all modes of transport

 Articles2

More Articles
Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion.

Am. J. Physiol. 264 , C361, (1993)

We have previously demonstrated that the venom of the scorpion Leiurus quinquestriatus blocks small-conductance Cl- channels, derived from epithelial cells, when applied to the cytoplasmic surface. We...

Expression of voltage-activated chloride currents in acute slices of human gliomas.

Neuroscience 83 , 1161-1173, (1998)

Using whole-cell patch-clamp recordings, we identified a novel voltage-activated chloride current that was selectively expressed in glioma cells from 23 patient biopsies. Chloride currents were identi...

 Synonyms

Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-His-Gln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-Cys-Gly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-Gly-Pro-Gln-Cys-Leu-Cys-Arg
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