12771-72-1 Usage
Uses
Used in Research Applications:
Verruculogen is utilized as a research tool for studying the effects of tremorgenic mycotoxins on neurotransmitter release, GABA levels, and DHP receptor interactions. It is also used to investigate the inhibition of Ca2+-activated K+ channels and its role as a cell cycle inhibitor.
Used in Cell Cycle Studies:
In cell cycle research, verruculogen is employed as a compound that arrests mouse mammary carcinoma cells in the M phase of the cell cycle, with a minimum inhibitory concentration (MIC) of 12.2 μM.
Used in Immunocytochemistry and Immunohistochemistry:
Used in Western Blotting:
Used in Taxonomy:
As a compound produced by several species of Penicillium and Aspergillus, verruculogen serves as a useful taxonomic phenotypic marker, aiding in the classification and identification of these fungal species.
Biological Activity
verruculogen is a maxi-k potassium channels inhibitor.maxi-k, a potassium channel characterized by their large conductance for potassium ions through cell membranes, is activated by changes in membrane electrical potential and/or by increases in concentration of intracellular calcium ion. maxi-k channels are critical for the regulation of several key physiological processes, such as smooth muscle tone and neuronal excitability.
Biochem/physiol Actions
The protein encoded by this gene is a G protein-coupled receptor and is a component of the heterodimeric amino acid taste receptor T1R1+3. The T1R1+3 receptor responds to L-amino acids but not to D-enantiomers or other compounds. Most amino acids that are perceived as sweet activate T1R1+3, and this activation is strictly dependent on an intact T1R1+3 heterodimer. Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq]
in vitro
in a previous study, it was found that aflatrem, paspalitrem a, paspalitrem c, penitrem a, and paspalinine could inhibit the binding of [125i]charybdotoxin to maxi-k channels in bovine aortic smooth muscle sarcolemmal membranes. whereas, verruculogen enhanced toxin binding. despite their different effects on binding of [125i]charybdotoxin to maxi-k channels, all tested compounds including verruculogen were able to potently inhibit maxi-k channels in electrophysiological experiments, and other types of voltage-dependent or ca(2+)-activated k+ channels examined were not affected [1].
in vivo
in an animal study, the mechanism of the genesis of tremor induced by verruculogen was investigated. it was found that atropine, glycine, mephenesin, and penicillamine with proven efficacy in relieving tremor of varied etiology, failed to modify verruculogen induced tremor. oxyaminoacetic acid, which raises the cns levels of gaba, and beta (chlorphenyl) gamma aminobutyric acid, which passes the hematoencephalic barrier, completely or partly relieved tremor and other verruculogen-induced symptoms, depending on the dose of the verruculogen administered. picrotoxin, a gaba antagonist, increased the effect of verruculogen in the tested animals [2].
references
[1] knaus, h. g.,mcmanus, o.b.,lee, s.h., et al. tremorgenic indole alkaloids potently inhibit smooth muscle high-conductance calcium-activated potassium channels. biochemistry 33(19), 5819-5828 (1994).[2] hotujac l, stern p. pharmacological examination of verruculogen induced tremor. acta med iugosl. 1974;28(3):223-9.
Check Digit Verification of cas no
The CAS Registry Mumber 12771-72-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,2,7,7 and 1 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 12771-72:
(7*1)+(6*2)+(5*7)+(4*7)+(3*1)+(2*7)+(1*2)=101
101 % 10 = 1
So 12771-72-1 is a valid CAS Registry Number.
InChI:InChI=1/C27H33N3O7/c1-14(2)11-20-29-18-12-15(35-5)8-9-16(18)21-22(29)19(13-26(3,4)37-36-20)30-24(32)17-7-6-10-28(17)25(33)27(30,34)23(21)31/h8-9,11-12,17,19-20,23,31,34H,6-7,10,13H2,1-5H3
12771-72-1Relevant articles and documents
Total synthesis of verruculogen and fumitremorgin a enabled by ligand-controlled C-H borylation
Feng, Yu,Holte, Dane,Zoller, Jochen,Umemiya, Shigenobu,Simke, Leah R.,Baran, Phil S.
, p. 10160 - 10163 (2015/09/01)
Verruculogen and fumitremorgin A are bioactive alkaloids that contain a unique eight-membered endoperoxide. Although related natural products such as fumitremorgins B and C have been previously synthesized, we report the first synthesis of the more complex, endoperoxide-containing members of this family. A concise route to verruculogen and fumitremorgin A relied not only on a hydroperoxide/indole hemiaminal cyclization, but also on the ability to access the seemingly simple starting material, 6-methoxytryptophan. An iridium-catalyzed C-H borylation/Chan-Lam procedure guided by an N-TIPS group enabled the conversion of a tryptophan derivative into a 6-methoxytryptophan derivative, proving to be a general way to functionalize the C6 position of an N,C3-disubstituted indole for the synthesis of indole-containing natural products and pharmaceuticals.
Gene Disruption and Biochemical Characterization of Verruculogen Synthase of Aspergillus fumigatus
Kato, Naoki,Suzuki, Hirokazu,Takagi, Hiroshi,Uramoto, Masakazu,Takahashi, Shunji,Osada, Hiroyuki
experimental part, p. 711 - 714 (2012/01/14)
Three in one: Verruculogen synthase FtmF is a key enzyme to diversify the fumitremorgin biosynthetic pathway in Aspergillus fumigatus: FtmF catalyzes not only endoperoxide bond formation of verruculogen but also the deprenylation and oxidation of fumitremorgin B to yield 12α,13α-dihydroxyfumitremorgin C and 13-oxoverruculogen, respectively.
FtmOx1, a non-heme Fe(ii) and α-ketoglutarate-dependent dioxygenase, catalyses the endoperoxide formation of verruculogen in Aspergillus fumigatus
Steffan, Nicola,Grundmann, Alexander,Afiyatullov, Shamil,Ruan, Hanli,Li, Shu-Ming
supporting information; experimental part, p. 4082 - 4087 (2009/12/06)
Verruculogen is a tremorgenic mycotoxin and contains an endoperoxide bond. In this study, we describe the cloning, overexpression and purification of a non-heme Fe(ii) and α-ketoglutarate-dependent dioxygenase FtmOx1 from Aspergillus fumigatus, which cata
