1428671-06-0Relevant articles and documents
(3S,4S)-N-substituted-3,4-dihydroxypyrrolidines as ligands for the enantioselective Henry reaction
Rénio, Márcia R.R.,Sousa, Francisco J.P.M.,Tavares, Nélia C.T.,Valente, Artur J.M.,da Silva Serra, M. Elisa,Murtinho, Dina
, (2021)
The enantioselective Henry reaction is a very important and useful carbon–carbon bond forming reaction. The execution of this reaction requires the use of efficient chiral catalysts. In this work, in situ formed complexes of N-substituted dihydroxypyrrolidines, chiral ligands derived from L-tartaric acid and amines, were evaluated as catalysts in the enantioselective Henry reaction. The results showed that the nature of the N-substituent on the ligand significantly influences the outcome of the reaction. Best results were obtained using a Cu (II) complex of (3S,4S)-N-benzyl-3,4-dihydroxypyrrolidine, in the presence of DIPEA, for the reaction of aromatic aldehydes with nitromethane, at room temperature, originating products with er up to 92:8 (R:S) and conversions up to 96%. The interaction between the pyrrolidine ligand and the copper ion, in isopropanol, was followed by UV-vis spectrophotometry, showing a 1:1 stoichiometry and a binding constant of 4.4. The results obtained will contribute to the design and development of more efficient chiral catalysts for this type of reaction.
Five-membered iminocyclitol α-glucosidase inhibitors: Synthetic, biological screening and in silico studies
Guerreiro, Luis R.,Carreiro, Elisabete P.,Fernandes, Luis,Cardote, Teresa A.F.,Moreira, Rui,Caldeira, Ana T.,Guedes, Rita C.,Burke
, p. 1911 - 1917 (2013/04/23)
The design and synthesis of a small library of pyrrolidine iminocyclitol inhibitors with a structural similarity to 1,4-dideoxy-1,4-imino-d-arabitol (DAB-1) is reported. This library was specifically designed to gain a better insight into the mechanism of inhibition of glycosidases by polyhydroxylated pyrrolidines or iminocyclitols. Pyrrolidine-3,4-diol 15a and pyrrolidine-3,4-diol diacetate 15b had emerged as the most potent α-glucosidase inhibitors in the series. Docking studies performed with an homology model of α-glucosidase disclosed binding poses for compounds 15a, 15b, 16a, and 16a′ occupying the same region as the NH group of the terminal ring of acarbose and suggest a closer and stronger binding of compound 15a and 15b with the enzyme active site residues. Our studies indicate that 2 or 5-hydroxyl substituents appear to be vital for high inhibitory activity.
