159766-56-0Relevant articles and documents
Towards a selective Boc deprotection on acid cleavable Wang resin
Lejeune, Valérie,Martinez, Jean,Cavelier, Florine
, p. 4757 - 4759 (2003)
Deprotection of the Boc group of an amino acid attached to the Wang resin has been investigated. Several conditions, including bases, solvents and reaction time, were studied. Quantitative yield of Boc deprotection was achieved with less than 10% loss of resin loading with trimethylsilyltriflate. This reagent allows the replacement of tert-butyl to TMS group, leading to a new temporary urethane protection readily hydrolyzed.
Synthesis and Evaluation of a Stable Isostere of Malonyllysine**
Jing, Yihang,Bergholtz, Sarah E.,Omole, Anthony,Kulkarni, Rhushi A.,Zengeya, Thomas T.,Yoo, Euna,Meier, Jordan L.
, (2021/11/09)
Lysine malonylation is a recently characterized post-translational modification involved in the regulation of energy metabolism and gene expression. One unique feature of this post-translational modification is its potential susceptibility to decarboxylation, which poses possible challenges to its study. As a step towards addressing these challenges, we report the synthesis and evaluation of a stable isostere of malonyllysine. First, we find that synthetic substitution of the malonyl group with a tetrazole isostere results in amino acid's resistant to thermal decarboxylation. Next, we demonstrate that protected variants of this amino acid are readily incorporated into peptides. Finally, we show that tetrazole isosteres of malonyllysine can be recognized by anti-malonyllysine antibodies and histone deacylases, validating their ability to mimic features of the endogenous lysine modification. Overall, this study establishes a new chemical strategy for stably mimicking a metabolite-derived post-translational modification, providing a foothold for tool development and functional analyses.
Random-coil:α-helix equilibria as a reporter for the Lewis X-LewisX interaction
Altamore, Timothy M.,Fernandez-Garcia, Christian,Gordon, Andrew H.,Huebscher, Tina,Promsawan, Netnapa,Ryadnov, Maxim G.,Doig, Andrew J.,Woolfson, Derek N.,Gallagher, Timothy
, p. 11167 - 11171 (2012/02/02)
Probing weak interactions: A peptide random-coil:α-helix equilibrium has been used to identify a weak carbohydrate-carbohydrate interaction (CCI). Glucose and lactose destabilized the helical conformer while LewisX trisaccharide led to increased helicity. Though small, the trend observed indicates that this peptide reporter can detect a single CCI in isolation. Copyright