Synthesis and Characterization of Luciferin Derivatives for Use in Bioluminescence Enhanced Enzyme Immunoassays. New Ultrasensitive Detection Systems for Enzyme Immunoassays, I.

Abstract

IntroductioD, .

Beyond D-luciferin: expanding the scope of bioluminescence imaging in vivo

“…Geiger, Miska and coworkers pioneered the concept of bioluminogenic substrates that release D-luciferin or 6′-aminoluciferin upon the action of a hydrolytic enzyme (e.g., phosphatase, esterase, protease, β-galactosidase, or sulfatase) [35–38]. Prior to enzyme activation, these molecules are not light-emitting substrates for luciferase.…”

“…However, in employing this strategy, care must be taken to ensure that the reporter is actually specific for the desired analyte and is generally bioavailable [44]. Furthermore, caged luciferins that do not emit light with luciferase could still potentially be inhibitors [35] or even non-luminogenic substrates, a possibility that has not been universally explored.…”

Synthesis and Characterization of a New Substrate of Photinus pyralis Luciferase: 4-Methyl-D-luciferin

“…All are characterized by substitution of the carboxyl group or the phenoxide ion. However, since these two chemical groups are essential for luciferin light emission properties (8), the synthesized derivatives are poor substrates or require post modifications (7,9).…”

Recent progress in luminescent proteins development

“…The first caged D-luciferins were developed in 1987 for the establishment of highly sensitive enzyme-based immunoassays, as alternatives to radioimmunoassays [31]. One of the well-established caged D-luciferin substrates is Lugal (1-O-galactopyranosyl-luciferin), which contains D-luciferin conjugated with b-galactose (b-gal) [32].…”