108384-35-6Relevant articles and documents
Asymmetric Synthesis of N-Substituted γ-Amino Esters and γ-Lactams Containing α,γ-Stereogenic Centers via a Stereoselective Enzymatic Cascade
Li, Ming,Cui, Yunfeng,Xu, Zefei,Chen, Xi,Feng, Jinhui,Wang, Min,Yao, Peiyuan,Wu, Qiaqing,Zhu, Dunming
supporting information, p. 372 - 379 (2021/10/25)
γ-Amino esters and γ-lactams containing α,γ-stereogenic centers are widely used as chiral intermediates in various bioactive compounds, while their efficient synthesis remains a challenge. Herein, an enzymatic cascade reaction involving an ene reductase (
Biocatalytic synthesis of chiral cyclic γ-oxoesters by sequential C-H hydroxylation, alcohol oxidation and alkene reduction
Brenna, Elisabetta,Crotti, Michele,Gatti, Francesco G.,Monti, Daniela,Parmeggiani, Fabio,Pugliese, Andrea,Tentori, Francesca
supporting information, p. 5122 - 5130 (2017/11/09)
A three-step biocatalytic procedure is described for the conversion of methyl and ethyl cyclopentene- and cyclohexenecarboxylates into both the enantiomers of the corresponding chiral 3-oxoesters, which are useful building blocks for the synthesis of active pharmaceutical ingredients. The allylic hydroxylation of the starting cycloalkenecarboxylates is carried out by using R. oryzae resting cells entrapped in alginate beads, in acetate buffer solution at 25 °C. The oxidation of the intermediate allylic alcohols to unsaturated ketones, performed by the laccase/TEMPO system, and the ene-reductase mediated hydrogenation of the alkene bond were carried out in the same reaction vessel in a sequential mode at 30 °C. Being entirely biocatalytic, our multistep procedure provides considerable advantages in terms of selectivity and environmental impact over reported chemical methods.
Molecular Hybridization of Potent and Selective γ-Hydroxybutyric Acid (GHB) Ligands: Design, Synthesis, Binding Studies, and Molecular Modeling of Novel 3-Hydroxycyclopent-1-enecarboxylic Acid (HOCPCA) and trans-γ-Hydroxycrotonic Acid (T-HCA) Analogs
Krall, Jacob,Jensen, Claus Hatt,Bavo, Francesco,Falk-Petersen, Christina Birkedahl,Haugaard, Anne St?hr,Vogensen, Stine Byskov,Tian, Yongsong,Nittegaard-Nielsen, Mia,Sigurdardóttir, Sara Bj?rk,Kehler, Jan,Kongstad, Kenneth Thermann,Gloriam, David E.,Clausen, Rasmus Pr?torius,Harps?e, Kasper,Wellendorph, Petrine,Fr?lund, Bente
, p. 9022 - 9039 (2017/11/14)
γ-Hydroxybutyric acid (GHB) is a neuroactive substance with specific high-affinity binding sites. To facilitate target identification and ligand optimization, we herein report a comprehensive structure-affinity relationship study for novel ligands targeting these binding sites. A molecular hybridization strategy was used based on the conformationally restricted 3-hydroxycyclopent-1-enecarboxylic acid (HOCPCA) and the linear GHB analog trans-4-hydroxycrotonic acid (T-HCA). In general, all structural modifications performed on HOCPCA led to reduced affinity. In contrast, introduction of diaromatic substituents into the 4-position of T-HCA led to high-affinity analogs (medium nanomolar Ki) for the GHB high-affinity binding sites as the most high-affinity analogs reported to date. The SAR data formed the basis for a three-dimensional pharmacophore model for GHB ligands, which identified molecular features important for high-affinity binding, with high predictive validity. These findings will be valuable in the further processes of both target characterization and ligand identification for the high-affinity GHB binding sites.
