Category: 37905-02-5

Photoaffinity Analogues of Farnesyl Pyrophosphate Transferable by Protein Farnesyl Transferase was written by Chehade, Kareem A. H.;Kiegiel, Katarzyna;Isaacs, Richard J.;Pickett, Jennifer S.;Bowers, Katherine E.;Fierke, Carol A.;Andres, Douglas A.;Spielmann, H. Peter. And the article was included in Journal of the American Chemical Society in 2002.Recommanded Product: 37905-02-5 The following contents are mentioned in the article:

Farnesylation is a posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins in a reaction catalyzed by protein farnesyltransferase (FTase). We synthesized analogs (3-6) of farnesyl pyrophosphate (FPP) to probe the range of modifications possible to the FPP skeleton which allow for efficient transfer by FTase. Photoaffinity analogs of FPP (5, 6) were prepared by substituting perfluorophenyl azide functional groups for the 蠅-terminal isoprene of FPP. Substituted anilines replace the 蠅-terminal isoprene in analogs 3 and 4. Compounds 3-5 were prepared by reductive amination of the appropriate anilines with 8-oxo-geranyl acetate, followed by ester hydrolysis, chlorination, and pyrophosphorylation. Addnl. substitution of three methylenes for the 尾-isoprene of FPP gave photoprobe 6 in nine steps. Preparation of the analogs required TiCl₄-mediated imine formation prior to NaBH(OAc)₃ reduction for anilines with a pK_a < 1. The azide moiety was not affected by Ph₃PCl₂ conversion of allylic alcs. 13-16 into corresponding chlorides 17-20. Analogs 3-6 are efficiently transferred to target N-dansyl-GCVLS peptide substrate by mammalian FTase. Comparison of analog structures and kinetics of transfer to those of FPP reveals that ring fluorination and para substituents have little effect on the affinity of the analog pyrophosphate for FTase and its transfer efficiency. These results are also supported with models of the analog binding modes in the active site of FTase. The transferable azide photoprobe 5 photoinactivates FTase. Transferable analogs 5 and 6 allow the formation of appropriately posttranslationally modified photoreactive peptide probes of isoprene function. This study involved multiple reactions and reactants, such as (2E,6E)-3,7-Dimethyl-8-oxoocta-2,6-dien-1-yl acetate (cas: 37905-02-5Recommanded Product: 37905-02-5).

(2E,6E)-3,7-Dimethyl-8-oxoocta-2,6-dien-1-yl acetate (cas: 37905-02-5) belongs to esters. Esters typically have a pleasant smell; those of low molecular weight are commonly used as fragrances and are found in essential oils and pheromones. Acyl chlorides and acid anhydrides alcoholysis is another way to produce esters. Acyl chlorides and acid anhydrides react with alcohols to produce esters. Anydrous conditions are recommended since both acyl chlorides and acid anhydrides react with water.Recommanded Product: 37905-02-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics

Design and Synthesis of a Transferable Farnesyl Pyrophosphate Analogue to Ras by Protein Farnesyltransferase was written by Chehade, Kareem A. H.;Andres, Douglas A.;Morimoto, Hiromi;Spielmann, H. Peter. And the article was included in Journal of Organic Chemistry in 2000.SDS of cas: 37905-02-5 The following contents are mentioned in the article:

The posttranslational addition of a farnesyl moiety to the Ras oncoprotein is essential for its membrane localization and is required for both its biol. activity and ability to induce malignant transformation. We describe the design and synthesis of a farnesyl pyrophosphate (FPP) analog, 8-anilinogeranyl pyrophosphate, PhNHCH2CMe:CH(CH₂)₂CMe:CHCH₂OP₂O₆H₃ [AGPP (I)], in which the 蠅-terminal isoprene unit of the farnesyl group has been replaced with an aniline functionality. The key steps in the synthesis are the reductive amination of the 伪,尾-unsaturated aldehyde, OHCCMe:CH(CH₂)₂CMe:CHCH₂OAc-(E,E), to form the lipid analog, PhNHCH₂CMe:CH(CH₂)₂CMe:CHCH₂OAc-(E,E), and the subsequent conversion of the allylic alc., PhNHCH₂CMe:CH(CH₂)₂CMe:CHCH₂OH-(E,E), to the chloride, PhNHCH₂CMe:CH(CH₂)₂CMe:CHCH₂Cl-(E,E), via Ph₃PCl₂ followed by displacement with [(n-Bu)₄N]₃HP₂O₇ to give I. I is a substrate for protein farnesyltransferase (FTase) and is transferred to Ras by FTase with the same kinetics as the natural substrate, FPP. I is highly selective, showing little inhibitory activity against either geranylgeranyl-protein transferase type I (GGTase I) (K_i = 0.06 渭M, IC₅₀ = 20 渭M) or squalene synthase (IC₅₀ = 1000 渭M). I is the first efficiently transferable analog of FPP to be modified at the 蠅-terminus that provides a platform from which addnl. analogs can be made to probe the biol. function of protein farnesylation. I is the first example of a class of compounds that are alternate substrates for protein isoprenylation that are not inhibitors of squalene synthase. This study involved multiple reactions and reactants, such as (2E,6E)-3,7-Dimethyl-8-oxoocta-2,6-dien-1-yl acetate (cas: 37905-02-5SDS of cas: 37905-02-5).

(2E,6E)-3,7-Dimethyl-8-oxoocta-2,6-dien-1-yl acetate (cas: 37905-02-5) belongs to esters. Esters typically have a pleasant smell; those of low molecular weight are commonly used as fragrances and are found in essential oils and pheromones. Cyclic esters are called lactones, regardless of whether they are derived from an organic or inorganic acid. One example of an organic lactone is 纬-valerolactone.SDS of cas: 37905-02-5

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics