63991-99-1Relevant academic research and scientific papers
Synthesis and aminopeptidase n inhibiting activity of 3-(nitrophenoxymethyl)-[1,3,2]dioxaborolan-2-OLS and their open analogues
Farsa, Oldrich,Kana, Jakub,Macku, Irena,Zelazkova, Jana,Podlipna, Jana,Cirkva, Ales,Maxa, Jaroslav,Stastny, Kamil
, p. 127 - 135 (2017/01/21)
Aminopeptidase N (APN) represents a class of zinc metallopeptidases with broad substrate specifity. This enzyme is involved in control of angioneogenesis in cancer and microvascular conditions. It also serves as a superficial cellular receptor that enables attachment of some viruses including coronaviruses to the host cell. APN takes part also in metabolism of some important neuropeptides. That is why APN can be a promising therapeutic target and compounds which influence its activity interesting potential drugs. Here, synthesis of compounds which in most contain 3-phenoxypropan-1,2 diol moiety and evaluation of their inhibition activity against APN is described. 4-[1-, 2- and 3-(Nitrophenoxymethyl)]-[1,3,2]dioxaborolan-2-ols are novel compounds which have never been previously reported in the literature. 3-(Aminophenoxy)propyl-1,2-diols revealed greater activity than both 3-(nitrophenoxy)propyl-1,2-diols and 3-(nitrophenoxymethyl)-[1,3,2]dioxaborolan-2-ols. A QSAR study revealed a linear correlation between lipophilicity and inhibition activity.
A rare case of facial selectivity inversion for Sharpless asymmetric dihydroxylation in a series of structurally homogeneous substrates: Synthesis of non-racemic 3-(nitrophenoxy)-propane-1,2-diols
Bredikhina, Zemfira A.,Kurenkov, Alexey V.,Antonovich, Olga A.,Pashagin, Alexander V.,Bredikhin, Alexander A.
, p. 1015 - 1021 (2014/08/18)
Asymmetric dihydroxylation of mono nitrophenyl allyl ethers leads to the corresponding non-racemic 3-(nitrophenoxy)-propane-1,2-diols 1a-c. As this takes place, regardless of the reagent used (AD-mix-α or AD-mix-β), the configuration of the predominant enantiomer for the para- and meta-nitrosubstituted products is opposite to the configuration of the ortho-nitrophenyl derivative. A correlation between the melting points and vibrational spectra of the racemic and enantiopure diols 1a-c allowed us to establish that all of the chiral substances investigated formed stable racemic compounds in the solid phase.
An unusual (R)-selective epoxide hydrolase with high activity for facile preparation of enantiopure glycidyl ethers
Zhao, Jing,Chu, Yan-Yan,Li, Ai-Tao,Ju, Xin,Kong, Xu-Dong,Pan, Jiang,Tang, Yun,Xu, Jian-He
, p. 1510 - 1518 (2011/08/03)
A novel epoxide hydrolase (BMEH) with unusual (R)-enantioselectivity and very high activity was cloned from Bacillus megaterium ECU1001. Highest enantioselectivities (E>200) were achieved in the bioresolution of ortho-substituted phenyl glycidyl ethers and para-nitrostyrene oxide. Worthy of note is that the substrate structure remarkably affected the enantioselectivities of the enzyme, as a reversed (S)-enantiopreference was unexpectedly observed for the ortho-nitrophenyl glycidyl ether. As a proof-of-concept, five enantiopure epoxides (>99% ee) were obtained in high yields, and a gram-scale preparation of (S)-ortho-methylphenyl glycidyl ether was then successfully performed within a few hours, indicating that BMEH is an attractive biocatalyst for the efficient preparation of optically active epoxides. Copyright
Baker's yeast mediated stereoselective biotransformation of 1-acetoxy-3-aryloxypropan-2-ones
Egri, Gabriella,Kolbert, Attila,Balint, Jozsef,Fogassy, Elemer,Novak, Lajos,Poppe, Laszlo
, p. 271 - 283 (2007/10/03)
A series of 1-acetoxy-3-aryloxypropan-2-ones 1a-m were synthesized and subjected to biotransformation by baker's yeast yielding optically active monoacetates 5 or ent-5 and/or diols 4 of moderate to excellent enantiomeric purity. The dependence of the reduction/hydrolysis ratio and stereoselectivity on the size and substitution pattern of the aromatic moiety in the substrate is also discussed.
