1155356-49-2Relevant articles and documents
Resin bead micro-UV-visible absorption spectroscopy
Lu, Shin Wong,Birembaut, Fabrice,Brocklesby, William S.,Frey, Jeremy G.,Bradley, Mark
, p. 2247 - 2251 (2005)
The construction and design of a microscope coupled with a miniature UV-vis spectrometer is described. This was applied to the study of dyes linked to solid supports and displayed good correlation in spectral shape and λmax values when compared
Synthetic Fluorogenic Peptides Reveal Dynamic Substrate Specificity of Depalmitoylases
Amara, Neri,Foe, Ian T.,Onguka, Ouma,Garland, Megan,Bogyo, Matthew
, p. 35 - 7,47 (2019)
Palmitoylation is a post-translational modification involving the thioesterification of cysteine residues with a 16-carbon-saturated fatty acid. Little is known about rates of depalmitoylation or the parameters that dictate these rates. Here we report a modular strategy to synthesize quenched fluorogenic substrates for the specific detection of depalmitoylase activity and for mapping the substrate specificity of individual depalmitoylases. We demonstrate that human depalmitoylases APT1 and APT2, and TgPPT1 from the parasite Toxoplasma gondii, have distinct specificities that depend on amino acid residues distal to the palmitoyl cysteine. This information informs the design of optimal and non-optimal substrates as well as isoform-selective substrates to detect the activity of a specific depalmitoylase in complex proteomes. In addition to providing tools for studying depalmitoylases, our findings identify a previously unrecognized mechanism for regulating steady-state levels of distinct palmitoylation sites by sequence-dependent control of depalmitoylation rates. Amara et al. describe a method for preparing positional scanning libraries of fluorogenic palmitoylated peptide substrates. This allowed identification of residues that are distal to the palmitoylation site that impact turnover. This information allowed the design of substrates that are selective for a specific depalmitoylating enzyme.
ENZYME DETECTION COMPOUND AND MANUFACTURING METHOD OF THE COMPOUND
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Paragraph 0039, (2018/02/27)
PROBLEM TO BE SOLVED: To obtain a noel compound for detecting enzyme and a detection method of enzyme using the same and a compound having following structure, R1 and R2 are each independently H, an alkyl group having 1 to 2 carbon atoms, an alkenyl group having 2 carbon atoms or an alkynyl group or a phenyl group having 2 carbon atoms, n is 2 to 12 and X is an amino acid residue. SELECTED DRAWING: Figure 2 COPYRIGHT: (C)2018,JPOandINPIT
FRET-based imaging of transbilayer movement of pepducin in living cells by novel intracellular bioreductively activatable fluorescent probes
Tsuji, Mieko,Ueda, Satoshi,Hirayama, Tasuku,Okuda, Kensuke,Sakaguchi, Yoshiaki,Isono, Aoi,Nagasawa, Hideko
supporting information, p. 3030 - 3037 (2013/07/26)
To elucidate the mechanisms of direct transmembrane penetration of pepducins, which are artificial lipopeptide G protein-coupled receptor (GPCR) modulators, we developed two types of FRET-based probes, Pep13-FL-SS-Dab (13) targeting the inner leaflet of the lipid bilayer and Pep13-Dab-SS-FL (14) targeting the cytosol, respectively. They are composed of a pepducin moiety and a fluorescent switch component consisting of 5(6)-carboxyfluorescein (FAM) as a fluorophore and dabcyl as a quencher connected through disulfide bond linkage. When they are internalized into the cytosol, intracellular glutathione can cleave the disulfide bond to release the quencher, which results in a turn-on fluorescence signal. Using these probes, we performed live cell imaging of transbilayer movements of pepducins on MCF-7 cells for the first time. The results suggested that the lipid moiety of the probes facilitated pepducin flipping across and tethering to the membrane. The present study raises the possibility of applying the probe architecture for direct intracellular drug delivery. The Royal Society of Chemistry 2013.