1036844-37-7Relevant academic research and scientific papers
Synthesis and Spectroscopic Properties of Fluorinated Coumarin Lysine Derivatives
Shukla, Lakshmi,Moodie, Lindon W. K.,Kindahl, Tomas,Hedberg, Christian
, p. 4792 - 4799 (2018/04/25)
The site-selective incorporation of fluorescent amino acids into proteins has emerged as a valuable alternative to expressible protein reporters. For successful application, a robust and scalable, yet flexible, route to non-natural amino acids is required. This work describes an improved synthesis of coumarin-conjugated lysine derivatives where fluorinated variants are accessed. These analogues can be utilized at low pH and should find application probing biological processes that operate under acidic conditions.
A HTS assay for the detection of organophosphorus nerve agent scavengers
Louise-Leriche, Ludivine,Paunescu, Emilia,Saint-Andre, Geraldine,Baati, Rachid,Romieu, Anthony,Wagner, Alain,Renard, Pierre-Yves
experimental part, p. 3510 - 3523 (2010/07/06)
A new pro-fluorescent probe aimed at a HTS assay of scavengers is able to selectively and efficiently cleave the P-S bond of organophosphorus nerve agents and by this provides non-toxic phosphonic acid has been designed and synthesised. The previously described pro-fluorescent probes were based on a conventional activated P-Oaryl bond cleavage, whereas our approach uses a self-immolative linker strategy that allows the detection of phosphonothioase activity with respect to a non-activated P-Salkyl bond. Further, we have also developed and optimised a high-throughput screening assay for the selection of decontaminants (chemical or biochemical scavengers) that could efficiently hydrolyse highly toxic V-type nerve agents. A preliminary screening, realised on a small α-nucleophile library, allowed us to identify some preliminary "hits", among which pyridinealdoximes, α-oxo oximes, hydroxamic acids and, less active but more original, amidoximes were the most promising. Their selective phosphonothioase activity has been further confirmed by using PhX as the substrate, and thus they offer new perspectives for the synthesis of more potent V nerve agent scavengers.
Designing better coumarin-based fluorogenic substrates for PTP1B
Holmes, Christopher P.,Macher, Natalie,Grove, J. Russell,Jang, Larry,Irvine, Jennifer D.
body text, p. 3382 - 3385 (2009/04/11)
As part of a program to develop better PTP1B fluorogenic substrates that more closely mimic the functionality found in the natural substrate, we have prepared and evaluated nine novel analogs of 4-methylumbelliferone phosphate (MUP) with a variety of additional groups occupying the second phosphate binding pocket.
