Cas no 11032-79-4 (α-Bungarotoxin)
α-Bungarotoxin Chemical and Physical Properties
Names and Identifiers
-
- alpha-Bungarotoxin
- A-BUNGAROTOXIN, WHITE LYOPHILIZATED POWDER
- α-Bungarotoxin
- α-Bungotoxin
- α-BuTX
- ALPHA-BGT
- ALPHA-BUTX
- A-BUNGAROTOXIN
- M.W. 7984.14 C338H529N97O105S11
- BUNGARUS MULTICINCTUS TOXIN, ALPHA
- A-BUNGAROTOXIN FROM THE VENOM OF THE
- ALPHA-BUNGAROTOXIN, BUNGARUS MULTICINCTUS
- H-ILE-VAL-CYS-HIS-THR-THR-ALA-THR-SER-PRO-ILE-SER-ALA-VAL-THR-CYS-PRO-PRO-GLY-GLU-ASN-LEU-CYS-TYR-ARG-LYS-MET-TRP-CYS-ASP-ALA-PHE-CYS-SER-SER-ARG-GLY-LYS-VAL-VAL-GLU-LEU-GLY-CYS-ALA-ALA-THR-CYS-PRO-SER-LYS-LYS-PRO-TYR-GLU-GLU-VAL-THR-CYS-CYS-SER-THR-ASP-LYS-CYS-ASN-PRO-HIS-PRO-LYS-GLN-ARG-PRO-GLY-OH
- 2-[(12-Hydroxy-1,3,11,24,31,41,44-heptamethyl-39-oxo-2,6,10,15,19,25,29,34,38,43,47-undecaoxaundecacyclo[26.22.0.03,26.05,24.07,20.09,18.011,16.030,48.033,46.035,44.037,42]pentaconta-21,40-dien-14-yl)methyl]prop-2-enal
- 11032-79-4
- CID 2432
-
- Inchi: 1S/C50H70O14/c1-25(24-51)14-28-17-37(52)50(8)41(54-28)19-33-34(61-50)18-32-29(55-33)10-9-12-46(4)42(58-32)23-49(7)40(62-46)21-39-47(5,64-49)13-11-30-44(60-39)26(2)15-31-36(56-30)22-48(6)38(57-31)20-35-45(63-48)27(3)16-43(53)59-35/h9-10,16,24,26,28-42,44-45,52H,1,11-15,17-23H2,2-8H3
- InChI Key: LYTCVQQGCSNFJU-UHFFFAOYSA-N
- SMILES: O1C2(C)CCC3C(C(C)CC4C(CC5(C)C(CC6C(C(C)=CC(=O)O6)O5)O4)O3)OC2CC2C1(C)CC1C(C)(CC=CC3C(CC4C(CC5C(C)(C(CC(CC(=C)C=O)O5)O)O4)O3)O1)O2
Computed Properties
- Exact Mass: 894.47655690g/mol
- Monoisotopic Mass: 894.47655690g/mol
- Isotope Atom Count: 0
- Hydrogen Bond Donor Count: 1
- Hydrogen Bond Acceptor Count: 14
- Heavy Atom Count: 64
- Rotatable Bond Count: 3
- Complexity: 1940
- Covalently-Bonded Unit Count: 1
- Defined Atom Stereocenter Count: 0
- Undefined Atom Stereocenter Count : 23
- Defined Bond Stereocenter Count: 0
- Undefined Bond Stereocenter Count: 1
- XLogP3: 3.7
- Topological Polar Surface Area: 156?2
Experimental Properties
- Color/Form: Lyophilized powder. A neurotoxin obtained from snake venom, a polypeptide consisting of 74 amino acid residues
- Solubility: Not determined
α-Bungarotoxin Pricemore >>
| Related Categories | No. | Product Name | Cas No. | Purity | Specification | Price | update time | Inquiry |
|---|---|---|---|---|---|---|---|---|
| ChemScence | CS-0029186-1mg |
α-Bungarotoxin |
11032-79-4 | 1mg |
$550.0 | 2022-04-28 | ||
| WU HAN AN JIE KAI Biomedical Technology Co., Ltd. | ajci5094-1mg |
α-Bungarotoxin |
11032-79-4 | 98% | 1mg |
¥3300.00 | 2023-09-10 | |
| SHANG HAI MAI KE LIN SHENG HUA Technology Co., Ltd. | B938688-1mg |
alpha-Bungarotoxin |
11032-79-4 | 1mg |
¥2,699.10 | 2022-09-02 | ||
| MedChemExpress | HY-P1264-1mg |
α-Bungarotoxin |
11032-79-4 | ≥99.0% | 1mg |
¥3300 | 2024-04-20 | |
| SHENG KE LU SI SHENG WU JI SHU | sc-202897-1mg |
α-Bungarotoxin, |
11032-79-4 | 1mg |
¥2512.00 | 2023-09-05 | ||
| SHENG KE LU SI SHENG WU JI SHU | sc-202897-1 mg |
α-Bungarotoxin, |
11032-79-4 | 1mg |
¥2,512.00 | 2023-07-11 | ||
| TargetMol Chemicals | TP2077-1 mg |
α-Bungarotoxin |
11032-79-4 | 98% | 1mg |
¥ 8,800 | 2023-07-11 | |
| TargetMol Chemicals | TP2077-5 mg |
α-Bungarotoxin |
11032-79-4 | 98% | 5mg |
¥ 23,980 | 2023-07-11 | |
| TargetMol Chemicals | TP2077-10 mg |
α-Bungarotoxin |
11032-79-4 | 98% | 10mg |
¥ 38,368 | 2023-07-11 | |
| 1PlusChem | 1P01EHJF-1mg |
alpha-Bungarotoxin - Bio-X |
11032-79-4 | 97% | 1mg |
$581.00 | 2023-12-26 |
α-Bungarotoxin Related Literature
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Long Deng,Qian Zou,Biao Liu,Wenhui Ye,Chengfei Zhuo,Li Chen,Ze-Yuan Deng,Ya-Wei Fan,Jing Li Food Funct., 2018,9, 4234-4245
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Yukiya Kitayama Polym. Chem., 2014,5, 2784-2792
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Ana G. Neo,Ana Bornadiego,Jesús Díaz,Stefano Marcaccini,Carlos F. Marcos Org. Biomol. Chem., 2013,11, 6546-6555
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Zhixia Liu,Tingjian Chen,Floyd E. Romesberg Chem. Sci., 2017,8, 8179-8182
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Marcin Czapla,Jack Simons Phys. Chem. Chem. Phys., 2018,20, 21739-21745
Additional information on α-Bungarotoxin
α-Bungarotoxin (CAS No. 11032-79-4): A Comprehensive Overview
The compound α-Bungarotoxin (CAS No. 11032-79-4) is a highly potent neurotoxin derived from the venom of the Bungarus multicinctus snake, commonly known as the multi-banded krait. This protein has garnered significant attention in the field of neuroscience and pharmacology due to its unique ability to bind specifically to nicotinic acetylcholine receptors (nAChRs). Its structural and functional properties have made it an invaluable tool in both research and therapeutic development.
α-Bungarotoxin is a member of the beta-neurotoxin family, characterized by its complex tertiary structure, which includes three disulfide bonds stabilizing its conformation. This structural integrity allows it to exhibit high affinity and specificity for nAChRs, particularly the α7 subtype. The toxin's mechanism of action involves irreversible blocking of the receptor, leading to neuromuscular blockade and, in higher concentrations, central nervous system effects.
The study of α-Bungarotoxin has been instrumental in advancing our understanding of nAChR function and dysfunction. Recent research has highlighted its potential in modeling neurodegenerative diseases such as Alzheimer's and Parkinson's. For instance, studies have demonstrated that α-Bungarotoxin can induce synaptic changes that mimic early stages of neurodegeneration, providing a valuable model system for drug screening and therapeutic intervention.
In addition to its neurobiological significance, α-Bungarotoxin has been explored for its pharmacological applications. Its high selectivity for nAChRs makes it a promising candidate for developing treatments targeting various neurological disorders. For example, research has focused on modulating nAChR activity to alleviate symptoms in conditions like nicotine addiction and myasthenia gravis. The toxin's ability to form stable complexes with receptors has also been leveraged in the development of novel diagnostic tools, such as biosensors for detecting nAChR-related diseases.
The structural elucidation of α-Bungarotoxin has been a cornerstone in computational chemistry and molecular modeling. Advanced techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy have provided detailed insights into its three-dimensional structure. These insights have not only enhanced our understanding of toxin-receptor interactions but also facilitated the design of synthetic analogs with tailored properties. Such analogs could potentially offer improved efficacy and reduced side effects in therapeutic applications.
The synthesis and modification of α-Bungarotoxin have been areas of active investigation. Chemists have developed methodologies to produce recombinant forms of the toxin, which offer greater purity and consistency compared to natural sources. Additionally, site-directed mutagenesis has been employed to alter specific amino acid residues, yielding variants with modified binding affinities or functional properties. These modifications have opened new avenues for drug development, particularly in the realm of targeted therapies.
The toxicological profile of α-Bungarotoxin has been thoroughly characterized, providing critical data for safety assessments and potential therapeutic use. Studies have examined its potency, toxicity, and metabolic pathways, contributing to a comprehensive understanding of its biological effects. This information is crucial for developing safe dosing regimens and minimizing adverse reactions in clinical settings.
The role of α-Bungarotoxin in basic research extends beyond neuroscience. Its unique binding properties have been utilized in studies exploring synaptic transmission and neuromodulation. Researchers have employed α-Bungarotoxin-labeled antibodies and fluorescently tagged variants to visualize nAChR distribution and function in vivo. These techniques have provided novel insights into neural circuitry and have been instrumental in uncovering the complexities of neural communication.
The future directions for research on α-Bungarotoxin are multifaceted. Efforts are ongoing to develop more selective analogs with enhanced therapeutic potential while minimizing off-target effects. Additionally, interdisciplinary approaches combining chemistry, biology, and medicine are being pursued to explore novel applications of this remarkable toxin. The integration of cutting-edge technologies such as CRISPR-Cas9 gene editing and artificial intelligence-driven drug discovery is expected to accelerate progress in this field.
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