144239-98-5Relevant academic research and scientific papers
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
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
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
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.
