59854-12-5Relevant articles and documents
Control of conformation in α-helix mimicking aromatic oligoamide foldamers through interactions between adjacent side-chains
Arrata, Irene,Grison, Claire M.,Coubrough, Heather M.,Prabhakaran, Panchami,Little, Marc A.,Tomlinson, Darren C.,Webb, Michael E.,Wilson, Andrew J.
supporting information, p. 3861 - 3867 (2019/04/26)
The design, synthesis and structural characterization of non-natural oligomers that adopt well-defined conformations, so called foldamers, is a key objective in developing biomimetic 3D functional architectures. For the aromatic oligoamide foldamer family
Study of Precatalyst Degradation Leading to the Discovery of a New Ru0 Precatalyst for Hydrogenation and Dehydrogenation
Anaby, Aviel,Schelwies, Mathias,Schwaben, Jonas,Rominger, Frank,Hashmi, A. Stephen K.,Schaub, Thomas
supporting information, p. 2193 - 2201 (2018/07/25)
The complex Ru-MACHO (1) is a widely used precatalyst for hydrogenation and dehydrogenation reactions under basic conditions. In an attempt to identify the active catalyst form, 1 was reacted with a strong base. The formation of previously unreported species was observed by NMR and mass spectrometry. This observation indicated that complex 1 quickly degraded under basic conditions when no substrate was present. X-ray crystallography enabled the identification of three complexes as products of this degradation of complex 1. These complexes suggested degradation pathways which included ligand cleavage and reassembly, along with reduction of the ruthenium atom. One of the decomposition products, the Ru0 complex [Ru(N(CH2CH2PPh2)3)CO] (5), was prepared independently and studied. 5 was found to be active, entirely additive-free, in the acceptorless dehydrogenation of aliphatic alcohols to esters. The hydrogenation of esters catalyzed by 5 was also demonstrated under base-free conditions with methanol as an additive. Protic substrates were shown to add reversibly to complex 5, generating RuII-hydrido species, thus presenting a rare example of reversible oxidative addition from Ru0 to RuII and reductive elimination from RuII to Ru0.
Synthesis and anticancer properties of RGD peptides conjugated to nitric oxide releasing functional groups and abiraterone
Nortcliffe, Andrew,Fleming, Ian N.,Botting, Nigel P.,O'Hagan, David
supporting information, p. 8343 - 8347 (2015/03/05)
A series of analogues of the integrin binding aspartic acid-glycine-arginine (RGD) peptide sequence were synthesised conjugated to nitric oxide (NO) donating functional groups. Also the cytotoxicity of abiraterone, a prostate cancer drug, was explored when it was conjugated in three part constructs to RGD sequences and NO releasing heterocycles. In general the analogues showed integrin binding affinity comparable to RGD reference compounds, and all released NO by the Griess test assay. Two analogues exhibited significant cytotoxic effects against PC3 and MCF7 cell lines.