82389-25-1

Upstream product

• 82400-03-1 phorbol-20-trityl ether 
• 108-24-7 acetic anhydride 

Downstream Products

• 179258-27-6 phorbol 12-phenylacetate 13-acetate 20-tritylether 
• 1026352-27-1 4-Azido-benzoic acid (1aR,1bS,4aR,7aS,7bS,8R,9R,9aS)-9a-acetoxy-4a,7b-dihydroxy-1,1,6,8-tetramethyl-5-oxo-3-trityloxymethyl-1a,1b,4,4a,5,7a,7b,8,9,9a-decahydro-1H-cyclopropa[3,4]benzo[1,2-e]azulen-9-yl ester 
• 1025908-96-6 Cyclohexyl-acetic acid (1aR,1bS,4aR,7aS,7bS,8R,9R,9aS)-9a-acetoxy-4a,7b-dihydroxy-1,1,6,8-tetramethyl-5-oxo-3-trityloxymethyl-1a,1b,4,4a,5,7a,7b,8,9,9a-decahydro-1H-cyclopropa[3,4]benzo[1,2-e]azulen-9-yl ester 
• 561063-31-8 phorbol 12-succinate-13-acetate-20-trityl 
• 561063-27-2 phorbol 12-(8-iodooctanoate)-13-acetate-20-trityl 
• 561063-26-1 phorbol 12-suberamate-13-acetate-20-trityl 
• 561063-32-9 phorbol 12-(allyl adipate)-13-acetate-20-trityl 
• 561063-36-3 Tetradecanedioic acid mono-((1aR,1bS,4aR,7aS,7bS,8R,9R,9aS)-9a-acetoxy-4a,7b-dihydroxy-1,1,6,8-tetramethyl-5-oxo-3-trityloxymethyl-1a,1b,4,4a,5,7a,7b,8,9,9a-decahydro-1H-cyclopropa[3,4]benzo[1,2-e]azulen-9-yl) ester 
• 561063-34-1 phorbol 12-(allyl sebacate)-13-acetate-20-trityl 
• 77495-83-1 phorbol 12,13-diacetate-20-trityl 
• 1173884-69-9 C₄₁H₄₂O₆ 
• 1026257-69-1 C₄₃H₅₁N₃O₁₃ 
• 1025931-88-7 C₄₃H₅₈O₁₃ 

Relevant academic research and scientific papers

Protein kinase C translocation by modified phorbol esters with functionalized lipophilic regions

Several novel phorbol esters were prepared with polar functional groups terminating their C12 and/or C13 acyl chains. Designed to be inhibitory protein kinase C (PKC) ligands, these phorbol analogues contain various polar functional groups (amide, ester,

A novel agonist, phorbol 12-phenylacetate 13-acetate 20-homovanillate, abolishes positive cooperativity of binding by the vanilloid receptor

Capsaicin binds to a specific recognition site, referred to as the vanilloid receptor, which it shares with the natural, ultrapotent agonist resiniferatoxin and with the competitive antagonist capsazepine. Upon binding to its receptor, capsaicin opens a cation channel leading to Ca2+ influx. The binding of capsaicin or resiniferatoxin by the vanilloid receptor follows a sigmoidal saturation curve, indicative of positive cooperativity. The biological significance of this positive cooperative behaviour is unknown, as is the mechanism responsible for it. We have developed a novel ligand, phorbol 12-phenylacetate 13-acetate 20-homovanillate (PPAHV), which binds to cultured rat sensory neurons (with a K(i) of 3.1 ± 0.4 μM), and induces Ca2+ uptake by them (with an ED50 of 1.8 ± 0.3 μM) with similar affinities and in a non-cooperative manner (Hill coefficients are 0.99 and 1.06 for binding and Ca2+ uptake, respectively). The behaviour of PPAHV thus contrasts with resiniferatoxin or capsaicin not only in the lack of cooperativity but also in the relative potencies for resiniferatoxin binding versus Ca2+ uptake (resiniferatoxin is less potent and capsaicin is more potent for induction of Ca2+ uptake than for binding). In further experiments in which the concentration of [3H]resiniferatoxin was varied, 1 μM PPAHV likewise reduced the cooperativity index that characterizes resiniferatoxin binding to rat spinal cord membranes from 2.3 ± 0.1 to 1.1 ± 0.2; in parallel experiments, neither capsaicin nor capsazepine (both at a concentration of 2 μM) affected binding cooperativity. Moreover, PPAHV (1 μM) turned the bi-phasic dissociation curve of resiniferatoxin into a monophasic curve, eliminating the second, slow-dissociation phase. The present results suggest that positive cooperativity is a ligand-induced feature rather than an inherent property of vanilloid receptors. A comparison of the spectrum of biological activity of ligands which bind to vanilloid receptors with different degrees of cooperativity may provide an approach to explore the functional significance of this binding behaviour.