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Usage

Uses

Used in Anticancer Applications:
2,6,10-Dodecatriene-1-thiol, 3,7,11-trimethyl-, (E,E)is used as an inhibitor for human isoprenylcysteine carboxyl methyltransferase (Icmt) protein. The inhibition of Icmt can be a promising approach to developing new anticancer drugs. By targeting this protein, (E,E)-Farnesyl Thiol may contribute to the development of novel therapeutic strategies against cancer.
Used in Pharmaceutical Research:
In the pharmaceutical industry, 2,6,10-Dodecatriene-1-thiol, 3,7,11-trimethyl-, (E,E)is used as a key compound for the development of new drugs. Its unique structure and properties make it an interesting candidate for further research and potential applications in drug discovery.
If there are different applications in different industries, they are listed separately:
Used in Chemical Synthesis:
2,6,10-Dodecatriene-1-thiol, 3,7,11-trimethyl-, (E,E)can be used as a building block or intermediate in the synthesis of various organic compounds. Its unique structure and functional groups make it a valuable starting material for the development of new molecules with potential applications in various fields.
Used in Material Science:
The compound may also find applications in material science, where its unique properties could be utilized in the development of new materials with specific characteristics, such as improved stability or reactivity.

Upstream product

• 340701-35-1 S-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl) ethanethioate 
• 106-28-5 Farnesol 

Downstream Products

• 148892-52-8 N-Boc-S-all-trans-farnesyl-L-cysteine 
• 142022-11-5 2,6-Dimethyl-4[[1-methyl-1-[(3,7,11-trimethyl-2,6,10-dodecatrienyl)thio]ethyl]thio]phenol 

Relevant academic research and scientific papers

Antiparasitic activity of sulfur- and fluorine-containing bisphosphonates against trypanosomatids and apicomplexan parasites

Based on crystallographic data of the complexes 2-alkyl(amino)ethyl-1,1-bisphosphonates-Trypanosoma cruzi farnesyl diphosphate synthase, some linear 1,1-bisphosphonic acids and other closely related derivatives were designed, synthesized and biologically evaluated against T. cruzi, the responsible agent of Chagas disease and against Toxoplasma gondii, the etiologic agent of toxoplasmosis and also towards the target enzymes farnesyl pyrophosphate synthase of T. cruzi (TcFPPS) and T gondii (TgFPPS), respectively. The isoprenoid-containing 1,1-bisphosphonates exhibited modest antiparasitic activity, whereas the linear α-fluoro-2-alkyl(amino)ethyl-1,1-bisphosphonates were unexpectedly devoid of antiparasitic activity. In spite of not presenting efficient antiparasitic activity, these data turned out to be very important to establish a structural activity relationship.

Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: Versatile and switchable access to functionalized proteins

An efficient and robust oxidative elimination of cysteine to dehydroalanine has been discovered. The reaction is induced by O-mesitylenesulfonylhydroxylamine (MSH) and is compatible with methionine. The key elimination has been executed on protein surfaces and allows ready access to different post-translationally modified proteins through conjugate addition of sulfur nucleophiles to dehydroalanine. Treatment of the resulting thioether with MSH results in regeneration of dehydroalanine, allowing a "functional switch" by subsequent addition of a different thiol. Copyright

Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase

Structure-activity studies were performed on the retinal rod outer segment isoprenylated protein methyltransferase that transfers a methyl group from S-adenosylmethionine (AdoMet) to the carboxyl group of isoprenylated (farnesylated or geranylgeranylated) cysteine residues. This methyltransferase enzyme has been shown to methylate N-acetyl-S-farnesyl-L-cysteine (L-AFC, 1) and S-(farnesyl-3-thio)propionic acid (FTP, 2). It is shown here that the enzyme does not enzymatically process D-AFC (8), although D-AFC (8) is a mixed-type inhibitor of the enzyme. Small modifications in the FTP (2) structural series generally lead to inactive substrates. For example, neither the cis- nor the trans-acrylate derivatives of FTP (2) are substrates of the enzyme, but both are inhibitors of it. Alkyl substitutions at the 3-position of FTP (2), moreover, lead to inhibitors of the methyltransferase. Substituents at the 2-position of FTP (2), as in 2-methyl-S-(farnesyl-3-thio)propionic acid (MFTP, 28) or S-farnesyl-2-(thiomethyl)acrylic acid (FTMA, 31), produce active substrates. Modifications at the carboxyl moiety produce neither substrates nor inhibitors of the enzyme. The conclusion from this and earlier studies is that the methyltransferase is selective for an isoprenylated thiopropionate moiety. Small deviations from this minimally essential structure lead to the abolition of substrate activity.