Discovery of Reversible Inhibitors of KDM1A Efficacious in Acute Myeloid Leukemia Models was written by Romussi, Alessia;Cappa, Anna;Vianello, Paola;Brambillasca, Silvia;Cera, Maria Rosaria;Dal Zuffo, Roberto;Faga, Giovanni;Fattori, Raimondo;Moretti, Loris;Trifiro, Paolo;Villa, Manuela;Vultaggio, Stefania;Cecatiello, Valentina;Pasqualato, Sebastiano;Dondio, Giulio;So, Chi Wai Eric;Minucci, Saverio;Sartori, Luca;Varasi, Mario;Mercurio, Ciro. And the article was included in ACS Medicinal Chemistry Letters in 2020.SDS of cas: 103-16-2 The following contents are mentioned in the article:
Lysine-specific demethylase 1 (LSD1 or KDM1A) is a FAD-dependent enzyme that acts as a transcription corepressor or coactivator by regulating the methylation status of histone H3 lysines K4 and K9, resp. KDM1A represents an attractive target for cancer therapy. While, in the past, the main medicinal chem. strategy toward KDM1A inhibition was based on the optimization of ligands that irreversibly bind the FAD cofactor within the enzyme catalytic site, we and others have also identified reversible inhibitors. Herein we reported the discovery of 5-imidazolylthieno[3,2-b]pyrroles, a new series of KDM1A inhibitors endowed with picomolar inhibitory potency, active in cells and efficacious after oral administration in murine leukemia models. This study involved multiple reactions and reactants, such as 4-Benzyloxyphenol (cas: 103-16-2SDS of cas: 103-16-2).
4-Benzyloxyphenol (cas: 103-16-2) belongs to ethers. Esters typically have a pleasant smell; those of low molecular weight are commonly used as fragrances and are found in essential oils and pheromones. Esters are more polar than ethers but less polar than alcohols. They participate in hydrogen bonds as hydrogen-bond acceptors, but cannot act as hydrogen-bond donors, unlike their parent alcohols. This ability to participate in hydrogen bonding confers some water-solubility.SDS of cas: 103-16-2
Referemce:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem