709-86-4Relevant academic research and scientific papers
A TiO2 immobilized Ru(ii) polyazine complex: A visible-light active photoredox catalyst for oxidative cyanation of tertiary amines
Kumar, Pawan,Varma, Sanny,Jain, Suman L.
, p. 4514 - 4519 (2014)
A chemically functionalized nanocrystalline TiO2 grafted ruthenium(ii) polyazine complex was found to be an efficient visible light photoredox catalyst for the oxidative cyanation of tertiary amines to the corresponding α-aminonitriles in high to excellent yields, using molecular oxygen as an oxidant and sodium cyanide in acetic acid as a cyanide source. The developed photoredox catalyst could be easily recovered by simple filtration and reused for several runs with consistent catalytic activity.
A fragment-like approach to PYCR1 inhibition
Milne, Kirsty,Sun, Jianhui,Zaal, Esther A.,Mowat, Jenna,Celie, Patrick H.N.,Fish, Alexander,Berkers, Celia R.,Forlani, Giuseppe,Loayza-Puch, Fabricio,Jamieson, Craig,Agami, Reuven
supporting information, p. 2626 - 2631 (2019/07/30)
Pyrroline-5-carboxylate reductase 1 (PYCR1) is the final enzyme involved in the biosynthesis of proline and has been found to be upregulated in various forms of cancer. Due to the role of proline in maintaining the redox balance of cells and preventing apoptosis, PYCR1 is emerging as an attractive oncology target. Previous PYCR1 knockout studies led to a reduction in tumor growth. Accordingly, a small molecule inhibitor of PYCR1 could lead to new treatments for cancer, and a focused screening effort identified pargyline as a fragment-like hit. We report the design and synthesis of the first tool compounds as PYCR1 inhibitors, derived from pargyline, which were assayed to assess their ability to attenuate the production of proline. Structural activity studies have revealed the key determinants of activity, with the most potent compound (4) showing improved activity in vitro in enzyme (IC50 = 8.8 μM) and pathway relevant effects in cell-based assays.
Synthesis, biological evaluation and quantitative structure activity relationship analysis of nuclearsubstituted pargylines as competitive inhibitors of MAO-A and MAO-B
Ali,Robinson
, p. 750 - 757 (2007/10/02)
A series of nuclear substituted derivatives of pargyline has been prepared and tested (under controlled conditions designed to measure the competitive component of the inhibition) as competitive inhibitors of MAO-A and -B. Adequate correlation of the biological data with the physicochemical constants of substituent groups was obtained only when the m- and p-substituted derivatives were considered separately. Due to the narrow range of activity displayed by the p-substituted derivates when inhibiting MAO-B, meaningful correlations were not found. However, the inhibition of MAO-B by the m-substituted derivatives required the inclusion of the Verloop L parameter for adequate correlation suggesting that the inhibitor binding site of MAO-B is present within a cavity of more limited lateral dimensions than that present on the MAO-A surface. Inhibition of both MAO-A and -B demonstrated a parabolic relationship between inhibitory activity and Π. Whereas this parabolic relationship showed a maximal value for inhibition of MAO-A (mean Π0 = 0.86), inhibition of MAO-B demonstrated a minimal value of Π(Π(min) = -0.5)i.e.the optimal value of Π for inhibition of MAO-B has not been achieved for this series of compounds but such would be greater than that demonstrated for MAO-A. The Hammett σ function was important or significant only in the inhibition of MAO-A by the p-substituted derivatives.
