99113-28-7Relevant articles and documents
Synthesis and biological evaluations of novel endomorphin analogues containing α-hydroxy-β-phenylalanine (AHPBA) displaying mixed μ/δ opioid receptor agonist and δ opioid receptor antagonist activities
Hu, Miao,Giulianotti, Marc A.,McLaughlin, Jay P.,Shao, Jiaan,Debevec, Ginamarie,Maida, Laura E.,Geer, Phaedra,Cazares, Margaret,Misler, Jaime,Li, Ling,Dooley, Colette,Ganno, Michelle L.,Eans, Shainnel O.,Mizrachi, Elisa,Santos, Radleigh G.,Yongye, Austin B.,Houghten, Richard A.,Yu, Yongping
, p. 270 - 281 (2015/04/21)
A novel series of endomorphin-1 (EM-1) and endomorphin-2 (EM-2) analogues was synthesized, incorporating chiral α-hydroxy-β-phenylalanine (AHPBA), and/or Dmt1-Tic2 at different positions. Pharmacological activity and metabolic stabil
A concise and efficient synthesis of (+)-preussin
Arevalo-Garcia, Enzo B.
, p. 47 - 50 (2014/04/03)
A novel and efficient synthesis of (+)-preussin (7) starting from N-butoxycarbonyl-L-phenylalaninal (1) is described. This natural product was synthesized under mild conditions and with good overall yield.
Enantiospecific formation of 3,6-dihydro-1H-pyridin-2-ones: Low-pressure palladium-catalysed decarboxylative carbonylation of 3-tosyl-5-vinyloxazolidin- 2-ones
Knight, Julian G.,Lawson, Iain M.,Johnson, Christopher N.
, p. 227 - 230 (2007/10/03)
Palladium-catalysed decarboxylative carbonylation of 3-tosyl-5- vinyloxazolidin-2-ones 5 occurs at atmospheric pressure to give 1-tosyl-3,6-dihydro-1H-pyridin-2-ones 6. The reaction proceeds with no loss of enantiopurity and detosylation with sodium napht
Allosteric regulation of the conformational dynamics of a cavitand receptor
Yan, Zhiqing,Chang, Yuning,Mayo, Dennis,Maslak, Veselin,Xia, Shijing,Badjic, Jovica D.
, p. 3697 - 3700 (2007/10/03)
Inspired by allostery in nature, we synthesized cavitand 1 and investigated regulation of its conformational dynamics. Quantitative 1H NMR studies have revealed that the rate of the conformational isomerization of 1 can be modulated using the e
A stereocontrolled synthesis of hapalosin
Oshitari, Tetsuta,Saiyinbilige,Mandai, Tadakatsu
, p. 185 - 190 (2007/10/03)
A facile synthetic method for two components of hapalosin, that is, β-hydroxy-γ-amino acid and β-hydroxy acid, has been established by utilizing chiral building blocks efficiently resolved in a lipase-catalyzed transesterification. Furthermore, the synthe
Lipase-Catalyzed Kinetic Resolution of 4-(N-Boc-amino)-1-alken-3-ols
Oshitari, Tetsuta,Mandai, Tadakatsu
, p. 2374 - 2376 (2007/10/03)
A wide range of 4-(N-Boc-amino)-1-alken-3-ols were efficiently resolved by lipase-catalyzed kinetic resolution. This procedure has been successfully applied to the highly enantioselective synthesis of the taxol side chain.
A Stereoselective Route to Hydroxyethylamine Dipeptide Isosteres
Datta, Apurba,Veeresa, Gududuru
, p. 7609 - 7611 (2007/10/03)
An efficient synthesis of stereodefined hydroxyethylamine dipeptide isosteres has been developed, utilizing a syn-selective Grignard addition and reductive amination as the key reactions.
Ring-closing metathesis strategy to unsaturated γ- and δ-lactones: Synthesis of hydroxyethylene isostere for protease inhibitors
Ghosh, Arun K.,Cappiello, John,Shin, Dongwoo
, p. 4651 - 4654 (2007/10/03)
Ring-closing olefin metathesis of acrylates derived from allylic and homo allylic alcohols in the presence of the Grubbs' catalyst (10-15 mol%) and titanium isopropoxide (0.3-3 equiv) provided ready access to α, β- unsaturated γ and δ-lactones and an important dipeptide isostere intermediate.
Design and synthesis of novel protease inhibitors. Tripeptide α′,ss′-epoxyketones as nanomolar inactivators of the proteasome
Spaltenstein, Andrew,Leban, Johann J.,Huang, Jim J.,Reinhardt, Kelli R.,Viveros, O. Humberto,Sigafoos, Jim,Crouch, Ronald
, p. 1343 - 1346 (2007/10/03)
Tripeptide α′,β′-epoxyketones were prepared stereospecifically starting from Boc-[S]-phenylalanine. Diastereomer 5b inhibited the chymotrypsin-like activity of porcine endothelial cell derived proteasome at low nanomolar concentrations.
Inactivation of serine protease, α-chymotrypsin by fluorinated phenylalanine analogues
Ohba, Tsuyoshi,Ikeda, Eitatsu,Takei, Hisashi
, p. 1875 - 1880 (2007/10/03)
Fluorinated phenylalanine analogues were found to be slow-binding or reversible competitive inhibitors of α-chymotrypsin. A series of these compounds were designed to inactivate α-chymotrypsin as a result of the formation of hydrogen-bonding between fluorine atom of the inhibitors and the amide protons known as oxy-anion hole in the active-site of serine and cysteine proteases.