1217531-78-6Relevant articles and documents
The discovery and optimization of benzimidazoles as selective NaV1.8 blockers for the treatment of pain
Brown, Alan D.,Bagal, Sharan K.,Blackwell, Paul,Blakemore, David C.,Brown, Bruce,Bungay, Peter J.,Corless, Martin,Crawforth, James,Fengas, David,Fenwick, David R.,Gray, Victoria,Kemp, Mark,Klute, Wolfgang,Malet Sanz, Laia,Miller, Duncan,Murata, Yoshihisa,Payne, C. Elizabeth,Skerratt, Sarah,Stevens, Edward B.,Warmus, Joseph S.
supporting information, p. 230 - 239 (2018/12/11)
The voltage gated sodium channel NaV1.8 has been postulated to play a key role in the transmission of pain signals. Core hopping from our previously reported phenylimidazole leads has allowed the identification of a novel series of benzimidazole NaV1.8 blockers. Subsequent optimization allowed the identification of compound 9, PF-06305591, as a potent, highly selective blocker with an excellent preclinical in vitro ADME and safety profile.
Total Synthesis of Skyllamycins A–C
Giltrap, Andrew M.,Haeckl, F. P. Jake,Kurita, Kenji L.,Linington, Roger G.,Payne, Richard J.
, p. 15046 - 15049 (2017/10/31)
The skyllamycins are a family of highly functionalized non-ribosomal cyclic depsipeptide natural products which contain the extremely rare α-OH-glycine functionality. Herein the first total synthesis of skyllamycins A–C is reported, together with the biofilm inhibitory activity of the natural products. Linear peptide precursors for each natural product were prepared through an efficient solid-phase route incorporating a number of synthetic modified amino acids. A novel macrocyclization step between a C-terminal amide and an N-terminal glyoxylamide moiety served as a key transformation to install the unique α-OH-glycine unit and generate the natural products in the final step of the synthesis.
Synthesis, structure-activity, and structure-stability relationships of 2-substituted-n-(4-oxo-3-oxetanyl) n-acylethanolamine acid amidase (NAAA) inhibitors
Vitale, Romina,Ottonello, Giuliana,Petracca, Rita,Bertozzi, Sine Mandrup,Ponzano, Stefano,Armirotti, Andrea,Berteotti, Anna,Dionisi, Mauro,Cavalli, Andrea,Piomelli, Daniele,Bandiera, Tiziano,Bertozzi, Fabio
supporting information, p. 323 - 336 (2014/04/03)
N-Acylethanolamine acid amidase (NAAA) is a cysteine amidase that preferentially hydrolyzes saturated or monounsaturated fatty acid ethanolamides (FAEs), such as palmitoylethanolamide (PEA) and oleoylethanolamide (OEA), which are endogenous agonists of nu
