117657-37-1Relevant articles and documents
Ni complexes of an alane/tris(phosphine) ligand built around a strongly Lewis acidic tris(: N -pyrrolyl)aluminum
Lai, Qingheng,Cosio, Mario N.,Ozerov, Oleg V.
, p. 14845 - 14848 (2020)
Syntheses of a new tripodal alane/tris(phosphine) ligand (AlP3) based on 2-(diisopropylphosphino)pyrrole, and AlP3-supported Ni complexes are reported. The central tris(pyrrolyl)aluminum moiety acts as a stronger Lewis acid towards Ni than other related group 13 element-centered tripodal ligands, as demonstrated by the binding of H2 to Ni and the ease of reduction. This journal is
Synthesis of α-monobrominated pyrrole derivatives
Groenendaal,Van Loo,Vekemans,Meijer
, p. 1589 - 1600 (1995)
Surprisingly stable N-t-BOC-2-bromo-4-hexyl-pyrrole is prepared from N-t-BOC-2-trimethylstannyl-4-hexyl-pyrrole using N-bromosuccinimide as reagent. The bromo-stannyl exchange reaction is performed quantitatively in THF at -70°C under inert atmosphere. Si
Transformation of the non-selective aminocyclohexanol-based Hsp90 inhibitor into a Grp94-seletive scaffold
Mishra, Sanket J.,Ghosh, Suman,Stothert, Andrew R.,Dickey, Chad A.,Blagg, Brian S. J.
, p. 244 - 253 (2017/12/30)
Glucose regulated protein 94 kDa, Grp94, is the endoplasmic reticulum (ER) localized isoform of heat shock protein 90 (Hsp90) that is responsible for the trafficking and maturation of toll-like receptors, immunoglobulins, and integrins. As a result, Grp94 has emerged as a therapeutic target to disrupt cellular communication, adhesion, and tumor proliferation, potentially with fewer side effects compared to pan-inhibitors of all Hsp90 isoforms. Although, the N-terminal ATP binding site is highly conserved among all four Hsp90 isoforms, recent cocrystal structures of Grp94 have revealed subtle differences between Grp94 and other Hsp90 isoforms that has been exploited for the development of Grp94-selective inhibitors. In the current study, a structure-based approach has been applied to a Grp94 nonselective compound, SNX 2112, which led to the development of 8j (ACO1), a Grp94-selective inhibitor that manifests -440 nM affinity and ≥200-fold selectivity against cytosolic Hsp90 isoforms.
