73340-78-0Relevant articles and documents
Formation and propagation of well-defined Pd nanoparticles (PdNPs) during C-H bond functionalization of heteroarenes: Are nanoparticles a moribund form of Pd or an active catalytic species?
Baumann, Christoph G.,De Ornellas, Sara,Reeds, Jonathan P.,Storr, Thomas E.,Williams, Thomas J.,Fairlamb, Ian J.S.
, p. 6174 - 6187 (2015/04/14)
Abstract Examination of a series of C-H bond functionalization reactions of heteroarenes (e.g., indole, benzoxazole, benzthiazole, benzimidazole and purine derivatives) mediated by Pd(OAc), a commonly used C-H bond functionalization catalyst, reveals that well-defined Pd nanoparticles (PdNPs) are rapidly formed under working catalyst conditions. The PdNPs can be characterized ex situ after entrapment in a polymer matrix (polyvinylpyrrolidinone, PVP). Independently synthesized Pd(PVP)NPs are catalytically competent species, exhibiting catalyst activity commensurate with Pd(OAc) in several C-H bond functionalization reactions. Across a range of reactions, Pd concentration is a common variable, which can be linked to the propagation of PdNPs under working catalytic conditions using polar solvents like DMF, DMSO and acetic acid.
Two-step synthesis of novel, bioactive derivatives of the ubiquitous cofactor nicotinamide adenine dinucleotide (NAD)
Pesnot, Thomas,Kempter, Julia,Schemies, J?rg,Pergolizzi, Giulia,Uciechowska, Urszula,Rumpf, Tobias,Sippl, Wolfgang,Jung, Manfred,Wagner, Gerd K.
supporting information; experimental part, p. 3492 - 3499 (2011/07/30)
We report the design and concise synthesis, in two steps from commercially available material, of novel, bioactive derivatives of the enzyme cofactor nicotinamide adenine dinucleotide (NAD). The new synthetic dinucleotides act as sirtuin (SIRT) inhibitors and show isoform selectivity for SIRT2 over SIRT1. An NMR-based conformational analysis suggests that the conformational preferences of individual analogues may contribute to their isoform selectivity.
New insights into the design of inhibitors of human S-adenosylmethionine decarboxylase: studies of adenine C8 substitution in structural analogues of S-adenosylmethionine
McCloskey, Diane E.,Bale, Shridhar,Secrist III, John A.,Tiwari, Anita,Moss III, Thomas H.,Valiyaveettil, Jacob,Brooks, Wesley H.,Guida, Wayne C.,Pegg, Anthony E.,Ealick, Steven E.
scheme or table, p. 1388 - 1407 (2009/12/07)
S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and depends on a pyruvoyl group for the decarboxylation process. The crystal structures of the enzyme with various inhibitors at the active site have shown that the adenine base of the ligands adopts an unusual syn conformation when bound to the enzyme. To determine whether compounds that favor the syn conformation in solution would be more potent AdoMetDC inhibitors, several series of AdoMet substrate analogues with a variety of substituents at the 8-position of adenine were synthesized and analyzed for their ability to inhibit hAdoMetDC. The biochemical analysis indicated that an 8-methyl substituent resulted in more potent inhibitors, yet most other 8-substitutions provided no benefit over the parent compound. To understand these results, we used computational modeling and X-ray crystallography to study C8-substituted adenine analogues bound in the active site.
