Chemistry:AG 489
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| Preferred IUPAC name
N-(20-Amino-4-hydroxy-4,8,12,17-tetraazaicosan-1-yl)-2-(9H-purin-3-yl)acetamide | |
| Other names
Agatoxin 489
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| Identifiers | |
3D model (JSmol)
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| ChemSpider | |
PubChem CID
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| UNII | |
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| Properties | |
| C26H47N7O2 | |
| Molar mass | 489.709 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
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| Infobox references | |
AG 489 (or agatoxin 489) is a component of the venom produced by Agelenopsis aperta,[1] a North American funnel web spider. It inhibits the ligand gated ion channel TRPV1 through a pore blocking mechanism.[2]
Discovery
Template:Unclear-section To identify new inhibitors, capsaicin receptor channels (TRPV1) were screened with a venom library for activity against these channels. In result, the robust inhibitory activity was found in the venom. Venom fractionation using reversed phase HPLC allowed the purification of two acylpolyamine toxins, AG489 and AG505.[2]
Chemical structure of agatoxin 505
Both of these inhibit the TRPV1 channels[3] from the extracellular membrane side. From the pore blocking mechanism, the pore mutations that change toxic affinity were identified. As a result, the four mutants decreased toxic affinity and several mutants increased it. Therefore, this was consistent with the scanned TM5-TM6 linker region[4] being the outer vestibule of the channels and further confirming that AG489 is a pore blocker.
See also
References
- ↑ "Anesthesia and muscle relaxation with intrathecal injections of AR636 and AG489, two acylpolyamine spider toxins, in rat". Anesthesiology 77 (3): 507–12. September 1992. doi:10.1097/00000542-199209000-00016. PMID 1519789.
- ↑ 2.0 2.1 "An inhibitor of TRPV1 channels isolated from funnel Web spider venom". Biochemistry 44 (47): 15544–9. November 2005. doi:10.1021/bi051494l. PMID 16300403.
- ↑ "Transient receptor potential (TRP) channels: a clinical perspective". British Journal of Pharmacology 171 (10): 2474–507. May 2014. doi:10.1111/bph.12414. PMID 24102319.
- ↑ "Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel--an overview of the current mutational data". Molecular Pain 9: 30. June 2013. doi:10.1186/1744-8069-9-30. PMID 23800232.
External links
- AG+489 at the US National Library of Medicine Medical Subject Headings (MeSH)
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