69693-11-4Relevant articles and documents
Application of hansch's model to capsaicinoids and capsinoids: A study using the quantitative structure-activity relationship. A novel method for the synthesis of capsinoids
Barbero, Gerardo F.,Molinillo, Jose M. G.,Varela, Rosa M.,Palma, Miguel,MacIas, Francisco A.,Barroso, Carmelo G.
experimental part, p. 3342 - 3349 (2011/07/30)
We describe a synthetic approach for two families of compounds, the capsaicinoids and capsinoids, as part of a study of the quantitative relationship between structure and activity. A total of 14 capsaicinoids of increasing lateral chain lengths, from 2 to 16 carbon atoms, were synthesized. In addition, 14 capsinoids with identical lateral chains, as well as capsiate and dihydrocapsiate, have been synthesized, and a new method for the synthesis of these compounds has been developed. The yields range from 48.35 to 98.98%. It has been found that the synthetic capsaicinoids and capsinoids present a lipophilia similar to those of the natural compounds and present similar biological activity. The bioactivity of the synthetic capsaicinoids and capsinoids decreases proportionally to the degree of difference in lipophilia (higher or lower) compared to the natural compounds. Biological activity was determined using the etiolated wheat (Triticum aestlvum L.) coleoptiles bioassay and by comparing results of the synthesis with those presented by their counterpart natural compounds. The bioactivities found correlated directly to the lipophilic properties of the synthesized compounds.
A novel acylase from Streptomyces mobaraensis that efficiently catalyzes hydrolysis/synthesis of capsaicins as well as N-acyl-L-amino acids and N-acyl-peptides
Koreishi, Mayuko,Zhang, Demin,Imanaka, Hiroyuki,Imamura, Koreyoshi,Adachi, Shuji,Matsuno, Ryuichi,Nakanishi, Kazuhiro
, p. 72 - 78 (2007/10/03)
A novel enzyme that catalyzes efficient hydrolysis of capsaicin (8-methyl-N-vanillyl-6-nonenamide) was isolated from the culture broth of Streptomyces mobaraensis. The enzyme consisted of two dissimilar subunits with molecular masses of 61 and 19 KDa. The enzyme was activated and stabilized in the presence of Co2+. It showed a pH optimum of about 8 and was stable at temperatures of up to 55°C for 1 h at pH 7.8. The specific activity of the enzyme for the hydrolysis of capsaicin was 10 2-104 times higher than those for the enzymes reported to date. In an aqueous/n-hexane biphasic system, capsaicin analogues such as octanoyl, decanoyl, and lauroyl vanillylamides were synthesized from the corresponding fatty acids and vanillylamine at yields of 50% or greater. In addition, the enzyme catalyzed the deacylation of N-lauroyl-L-amino acids and N-lauroyl-L-dipeptides and the efficient synthesis of Nα-lauroyl-L-lysine, Nε-lauroyl-L-lysine, and various N-lauroyl-peptides in aqueous solution in both the absence and the presence of glycerol.
Vanilloids. 1. Analogs of Capsaicin with Antinociceptive and Antiinflammatory Activity
Janusz, John M.,Buckwalter, Brian L.,Young, Patricia A.,LaHann, Thomas R.,Farmer, Ralph W.,et al.
, p. 2595 - 2604 (2007/10/02)
As part of a program to establish structure-activity relationships for vanilloids, analogs of the pungent principle capsaicin, the alkyl chain portion the parent structure (and related compounds derived from homovanillic acid) was varied.In antinociceptive and antiinflammatory assays (rat and mouse hot plate and croton oil-inflamed mouse ear), compounds with widely varying alkyl chain structures were active.Short-chain compounds were active by systemic administration in the assays mentioned above but they retained the high pungency and acute toxicity characteristic of capsaicin.In contrast, the long chain cis-unsaturates, NE-19550 (vanillyloleamide) and NE-28345 (oleylhomovanillamide), were orally active, less pungent, and less acutely toxic than capsaicin.The potential of these compounds as antiinflammatory/analgesic agents is discussed in light of recent data on the mechanism of action of vanilloids on sensory nerve fibers.
