13325-14-9Relevant articles and documents
Trimethyl-substituted carbamate as a versatile self-immolative linker for fluorescence detection of enzyme reactions
Inoue, Kazuya,Nakamura, Noriaki,Ojida, Akio,Uchinomiya, Shohei
supporting information, (2020/05/25)
Self-immolative linker is a useful building block of molecular probes, with broad applications in the fields of enzyme activity analysis, stimuli-responsive material science, and drug delivery. This manuscript presents N-methyl dimethyl methyl (i.e., trimethyl) carbamate as a new class of self-immolative linker for the fluorescence detection of enzyme reactions. The trimethyl carbamate was shown to spontaneously undergo intramolecular cyclization upon formation of a carboxylate group, to liberate a fluorophore with the second time rapid reaction kinetics. Interestingly, the auto-cleavage reaction of trimethyl carbamate was also induced by the formation of hydroxyl and amino groups. Fluorescent probes with a trimethyl carbamate could be applicable for fluorescence monitoring of the enzyme reactions catalyzed by esterase, ketoreductase, and aminotransferase, and for fluorescence imaging of intracellular esterase activity in living cells, hence demonstrating the utility of this new class of self-immolative linker.
Specific Inhibitors in Vitamin Biosynthesis. Part 7. Syntheses of Blocked 7,8-Dihydropteridines via &α-Amino Ketones
Al-Hassan, Saiba S.,Cameron, Robert J.,Curran, Adrian W. C.,Lyall, William J. S.,Nicholson, Sydney H.,et al.
, p. 1645 - 1660 (2007/10/02)
The synthesis of 15 blocked 7,8-dihydropteridines is described in which the pyrazine ring is built from a derivative of an α-amino ketone.Three routes to the amino ketones based upon amino acids, nitrosyl chloride addition to alkenes, and nitro alcohols are discussed.The compounds synthesised are inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase , an enzyme in the pathway leading to dihydrofolate, and the inhibitory potencies of the compounds are discussed in the light of a hypothetical active site model for the enzyme.
