3588-57-6Relevant articles and documents
Chiral tetraaryl-and tetraalkynylborates as chiral solvating agents for tetraalkylammonium salts
Tayama, Eiji,Sugawara, Takeshi
supporting information, p. 803 - 811 (2019/01/18)
The application of tetracarbon-substituted chiral borate sodium salts (NaBR*4) as NMR chiral solvating agents for various tetraalkylammonium salts (R4NX) has been successfully demonstrated. Ion exchange between R4NX and NaBR*4 proceeded in excellent yields and provided the corresponding dia-stereomeric salts (R4NBR*4). The ee values of the R4NX salts were determined by1H NMR analysis of R4NBR*4. Two types of chiral borates, tetraaryl-and tetraalkynylborates with optically active 1,1′-binaphthyl components were used. At the beginning of this research, we investigated the efficacy of a known chiral tetraar-ylborate developed by Pommerening et al. for R4NX. To expand the possibility of further structural design of the chiral borate, we designed chiral tetraalkynylborates as a new structure. Their synthesis and application are also described.
Synthesis, screening and docking of small heterocycles as Glycogen Phosphorylase inhibitors
Schweiker, Stephanie S.,Loughlin, Wendy A.,Lohning, Anna S.,Petersson, Maria J.,Jenkins, Ian D.
, p. 584 - 594 (2015/03/14)
A series of morpholine substituted amino acids (phenylalanine, leucine, lysine and glutamic acid) was synthesized. A fragment-based screening approach was then used to evaluate a series of small heterocycles, including morpholine, oxazoline, dihydro-1,3-oxazine, tetrahydro-1,3-oxazepine, thiazoline, tetrahydro-1,3-pyrimidine, tetrahydro-1,3-diazepine and hexahydro-1H-benzimidazole, as potential inhibitors of Glycogen Phosphorylase a. Thiazoline 7 displayed an improved potency (IC50 of 25 μM) and had good LE and LELP values, as compared to heterocycles 1, 5, 9e13 and 19 (IC50 values of 1.1 mM e23.9 mM). A docking study using the crystal structure of human liver Glycogen Phosphorylase, provided insight into the interactions of heterocycles 5, 7, 9e13 and 19 with Glycogen Phosphorylase.
Resolution of non-proteinogenic amino acids via microbial lipase-catalyzed enantioselective transesterification
Miyazawa, Toshifumi,Mio, Motoe,Watanabe, Yuko,Yamada, Takashi
, p. 219 - 224 (2008/09/20)
A number of non-proteinogenic amino acids bearing aliphatic side chains were resolved with moderate to good enantioselectivities (E = 15-42) through the Burkholderia cepacia lipase-catalyzed enantioselective transesterification of the 2,2,2-trifluoroethyl esters of their N-benzyloxycarbonyl derivatives with methanol as a nucleophile in diisopropyl ether.