Tag: 400-500

Nishihara, Ryo; Kurita, Ryoji published an article in 2021, the title of the article was Mix-and-read bioluminescent copper detection platform using a caged coelenterazine analogue.Name: 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one And the article contains the following content:

Serum copper levels are biomarkers for copper-related diseases. Quantification of levels of free copper (not bound to proteins) in serum is important for diagnosing Wilson’s disease, in which the free copper concentration is elevated. Bioluminescence is commonly used in point-of-care diagnostics, but these assays require genetically engineered luciferase. Here, we developed a luciferase-independent copper detection platform. A luminogenic caged coelenterazine analog (TPA-H1) was designed and synthesized to detect copper ions in human serum. TPA-H1 was developed by introducing a tris[(2-pyridyl)-methyl]amine (TPA) ligand, which is a Cu+ cleavable caging group, to the carbonyl group at the C-3 position of the imidazopyrazinone scaffold. The luciferin, named HuLumino1, is the product of the cleavage reaction of TPA-H1 with a copper ion and displays “turn-on” bioluminescence signals specifically with human serum albumin, which can be used to quant. analyze copper ions. TPA-H1 exhibited a fast cleavage of the protective group, high specificity, and high sensitivity for copper over other metal ions. This novel caged coelenterazine derivative, TPA-H1, can detect free copper ions in serum in a simple “mix-and-read” manner. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Name: 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas:55779-48-1) belongs to pyrazines. Pyrazines were the focus of several computational modeling studies to explore regioselectivity and reactivity. And=pyrazines have found utility as part of metal complexes.Name: 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On September 21, 2022, Inouye, Satoshi; Sato, Jun-Ichi; Sahara-Miura, Yuiko; Tomabechi, Yuri; Sumida, Yuto; Sekine, Shun-Ichi; Shirouzu, Mikako; Hosoya, Takamitsu published an article.HPLC of Formula: 55779-48-1 The title of the article was Reverse mutants of the catalytic 19 kDa mutant protein (nanoKAZ/nanoLuc) from Oplophorus luciferase with coelenterazine as preferred substrate.. And the article contained the following:

Native Oplophorus luciferase (OpLase) and its catalytic 19 kDa protein (wild KAZ) show highest luminescence activity with coelenterazine (CTZ) among CTZ analogs. Mutated wild KAZ with 16 amino acid substitutions (nanoKAZ/nanoLuc) utilizes bis-coelenterazine (bis-CTZ) as the preferred substrate and exhibits over 10-fold higher maximum intensity than CTZ. To understand the substrate selectivity of nanoKAZ between CTZ and bis-CTZ, we prepared the reverse mutants of nanoKAZ by amino acid replacements with the original amino acid residue of wild KAZ. The reverse mutant with L18Q and V27L substitutions (QL-nanoKAZ) exhibited 2.6-fold higher maximum intensity with CTZ than that of nanoKAZ with bis-CTZ. The catalytic properties of QL-nanoKAZ including substrate specificity, luminescence spectrum, luminescence kinetics, luminescence products of CTZ, and luminescence inhibition by deaza-CTZ analogs were characterized and were compared with other CTZ-utilizing luciferases such as Gaussia and Renilla luciferases. Thus, QL-nanoKAZ with CTZ could be used as a potential reporter protein for various luminescence assay systems. Furthermore, the crystal structure of QL-nanoKAZ was determined at 1.70 Å resolution. The reverse mutation at the L18Q and V27L positions of α2-helix in nanoKAZ led to changes in the local structures of the α4-helix and the β6- and β7-sheets, and might enhance its binding affinity and oxidation efficiency with CTZ to emit light. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).HPLC of Formula: 55779-48-1

8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas:55779-48-1) belongs to pyrazines. Pyrazines were the focus of several computational modeling studies to explore regioselectivity and reactivity. And=pyrazines have found utility as part of metal complexes.HPLC of Formula: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Jiang, Tianyu; Li, Minyong published an article in 2022, the title of the article was Synthetic Coelenterazine Derivatives and Their Application for Bioluminescence Imaging..HPLC of Formula: 55779-48-1 And the article contains the following content:

Bioluminescence (BL), the emission light resulting from the enzyme-catalyzed oxidative reaction, is a powerful imaging modality for monitoring biological phenomena both in vitro and in vivo. Coelenterazine (CTZ), the known widespread luciferin found in bioluminescent organisms, develops bioluminescence imaging (BLI). Here, we describe an approach to synthesize a series of novel CTZ derivatives for diversifying the toolbox of the BL substrates. Furthermore, we exemplify some of them display excellent BL signals in vitro and in vivo, and thus should be noted as one of the ideal substrates for in vivo BLI compared with a well-known conventional substrate, DeepBlueC. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).HPLC of Formula: 55779-48-1

The Article related to bioluminescence, coelenterazine (ctz), derivatives, luciferin, renilla luciferase (rluc), diagnostic imaging, imidazoles: chemistry, luminescent measurements: methods, pyrazines: chemistry and other aspects.HPLC of Formula: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On February 18, 2020, Mallefet, Jerome; Duchatelet, Laurent; Coubris, Constance published an article.SDS of cas: 55779-48-1 The title of the article was Bioluminescence induction in the ophiuroid Amphiura filiformis (Echinodermata).. And the article contained the following:

Bioluminescence is a widespread phenomenon in the marine environment. Among luminous substrates, coelenterazine is the most widespread luciferin, found in eight phyla. The wide phylogenetic coverage of this light-emitting molecule has led to the hypothesis of its dietary acquisition, which has so far been demonstrated in one cnidarian and one lophogastrid shrimp species. Within Ophiuroidea, the dominant class of luminous echinoderms, Amphiura filiformis is a model species known to use coelenterazine as substrate of a luciferin/luciferase luminous system. The aim of this study was to perform long-term monitoring of A. filiformis luminescent capabilities during captivity. Our results show (i) depletion of luminescent capabilities within 5 months when the ophiuroid was fed a coelenterazine-free diet and (ii) a quick recovery of luminescent capabilities when the ophiuroid was fed coelenterazine-supplemented food. The present work demonstrates for the first time a trophic acquisition of coelenterazine in A. filiformis to maintain light emission capabilities. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).SDS of cas: 55779-48-1

The Article related to brittle star, coelenterazine, luciferase, trophic acquisition, animals, diet, echinodermata: physiology, imidazoles: administration & dosage, luminescent measurements, potassium chloride: pharmacology, pyrazines: administration & dosage and other aspects.SDS of cas: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Abe, Masahiro; Nishihara, Ryo; Ikeda, Yuma; Nakajima, Takahiro; Sato, Moritoshi; Iwasawa, Naoko; Nishiyama, Shigeru; Paulmurugan, Ramasamy; Citterio, Daniel; Kim, Sung Bae; Suzuki, Koji published an article in 2019, the title of the article was Near-Infrared Bioluminescence Imaging with a through-Bond Energy Transfer Cassette.Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one And the article contains the following content:

A coelenterazine (CTZ) analogue emitting near-infrared (NIR) bioluminescence was synthesized for through-bond energy transfer (TBET)-based imaging modalities. The analogue, named Cy5-CTZ, was prepared by conjugating cyanine-5 (Cy5) dye to CTZ through an acetylene linker. This novel derivative is intrinsically fluorescent and emits NIR-shifted luminescence upon reacting with an appropriate luciferase, the Renilla luciferase. This Cy5-CTZ substrate is optically stable in physiological samples and rapidly permeabilize through the plasma membrane into the cytosolic compartment of live cells. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to bioluminescence, dyes/pigments, energy transfer, fluorescence, imaging agents, carbocyanines: chemistry, energy transfer, imidazoles: chemistry, infrared rays, luminescent agents: chemistry, luminescent measurements, molecular structure, pyrazines: chemistry and other aspects.Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On December 31, 2020, Wu, Nan; Kobayashi, Naohiro; Tsuda, Kengo; Unzai, Satoru; Saotome, Tomonori; Kuroda, Yutaka; Yamazaki, Toshio published an article.HPLC of Formula: 55779-48-1 The title of the article was Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. And the article contained the following:

Abstract: Gaussia luciferase (GLuc) is a small luciferase (18.2 kDa; 168 residues) and is thus attracting much attention as a reporter protein, but the lack of structural information is hampering further application. Here, we report the first solution structure of a fully active, recombinant GLuc determined by heteronuclear multidimensional NMR. We obtained a natively folded GLuc by bacterial expression and efficient refolding using a Solubility Enhancement Petide (SEP) tag. Almost perfect assignments of GLuc′s 1H, 13C and 15N backbone signals were obtained. GLuc structure was determined using CYANA, which automatically identified over 2500 NOEs of which > 570 were long-range. GLuc is an all-alpha-helix protein made of nine helixes. The region spanning residues 10-18, 36-81, 96-145 and containing eight out of the nine helixes was determined with a Cα-atom RMSD of 1.39 Å ± 0.39 Å. The structure of GLuc is novel and unique. Two homologous sequential repeats form two anti-parallel bundles made by 4 helixes and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helixes. Further, we found a hydrophobic cavity where several residues responsible for bioluminescence were identified in previous mutational studies, and we thus hypothesize that this is a catalytic cavity, where the hydrophobic coelenterazine binds and the bioluminescence reaction takes place. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).HPLC of Formula: 55779-48-1

The Article related to amino acid sequence, animals, copepoda: enzymology, disulfides: chemistry, imidazoles: metabolism, luciferases: chemistry, luciferases: metabolism, nuclear magnetic resonance, biomolecular: methods, protein conformation, protein domains, protein folding, pyrazines: metabolism and other aspects.HPLC of Formula: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On January 8, 2022, Inouye, Satoshi; Nakamura, Mitsuhiro; Hosoya, Takamitsu published an article.COA of Formula: C26H21N3O3 The title of the article was Enzymatic conversion of dehydrocoelenterazine to coelenterazine using FMN-bound flavin reductase of NAD(P)H:FMN oxidoreductase. And the article contained the following:

Coelenterazine (CTZ) is known as luciferin (a substrate) for the luminescence reaction with luciferase (an enzyme) in marine organisms and is unstable in aqueous solutions The dehydrogenated form of CTZ (dehydrocoelenterazine, dCTZ) is stable and thought to be a storage form of CTZ and a recycling intermediate from the condensation reaction of coelenteramine and 4-hydroxyphenylpyruvic acid to CTZ. In this study, the enzymic conversion of dCTZ to CTZ was successfully achieved using NAD(P)H:FMN oxidoreductase from the bioluminescent bacterium Vibrio fischeri ATCC 7744 (FRase) in the presence of NADH (the FRase-NADH reaction). CTZ reduced from dCTZ in the FRase-NADH reaction was identified by HPLC and LC/ESI-TOF-MS analyses. Thus, dCTZ can be enzymically converted to CTZ in vitro. Furthermore, the concentration of dCTZ could be determined by the luminescence activity using the CTZ-utilizing luciferases (Gaussia luciferase or Renilla luciferase) coupled with the FRase-NADH reaction. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).COA of Formula: C26H21N3O3

The Article related to aliivibrio fischeri: enzymology, aliivibrio fischeri: genetics, animals, bacterial proteins: genetics, bacterial proteins: metabolism, biocatalysis, biotransformation, chromatography, high pressure liquid, flavin mononucleotide: metabolism, gene expression, imidazoles: metabolism, kinetics, luciferases: genetics and other aspects.COA of Formula: C26H21N3O3

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On March 31, 2021, Dijkema, Fenne Marjolein; Nordentoft, Matilde Knapkoeien; Didriksen, Anders Kroell; Corneliussen, Anders Svaerke; Willemoes, Martin; Winther, Jakob R. published an article.Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one The title of the article was Flash properties of Gaussia luciferase are the result of covalent inhibition after a limited number of cycles. And the article contained the following:

Luciferases are widely used as reporters for gene expression and for sensitive detection systems. The luciferase (GLuc) from the marine copepod Gaussia princeps, has gained popularity, primarily because it is secreted and displays a very high light intensity. While firefly luciferase is characterized by kinetic behavior which is consistent with conventional steady-state Michaelis-Menten kinetics, GLuc displays what has been termed “flash” kinetics, which signify a burst in light emission followed by a rapid decay. As the mechanistic background for this behavior was unclear, we decided to decipher this in more detail. We show that decay in light signal is not due to depletion of substrate, but rather is caused by the irreversible inactivation of the enzyme. Inactivation takes place after between 10 and 200 reaction cycles, depending on substrate concentration and can be described by the sum of two exponentials with associated rate constants The dominant of these increases linearly with substrate concentration while the minor is substrate-concentration independent. In terms of rate of initial luminescence reaction, this increases with the substrate concentration to the power of 1.5 and shows no signs of saturation up to 10 μM coelenterazine. Finally, we find that the inactivated form of the enzyme has a larger apparent size in both size exclusion chromatog. and SDS-PAGE anal. and shows a fluorescence peak at 410 nm when excited at 333 nm. These findings indicate that the “flash” kinetics in Gaussia luciferase are caused by an irreversible covalent binding to a substrate derivative during catalysis. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to animals, copepoda: enzymology, copepoda: genetics, escherichia coli: genetics, imidazoles: chemistry, imidazoles: metabolism, kinetics, luciferases: chemistry, luciferases: genetics, luciferases: metabolism, pyrazines: chemistry, pyrazines: metabolism, recombinant proteins: chemistry, recombinant proteins: genetics and other aspects.Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Nishihara, Ryo; Abe, Masahiro; Suzuki, Koji; Kim, Sung-Bae published an article in 2021, the title of the article was Luciferase-Specific Coelenterazine Analogues for Optical Cross Talk-Free Bioassays.Category: pyrazines And the article contains the following content:

Spectral overlaps in fluorescence (FL) and bioluminescence (BL) commonly cause optical cross talks. The present protocol introduces five different lineages of coelenterazine (CTZ) analogs, which have selectivity to a specific luciferase, and thus cross talk-free. For example, some CTZ analogs with ethynyl or styryl groups display dramatically biased BL to specific luciferases and pH by modifying the functional groups at the C-2 and C-6 positions of the imidazopyridinne backbone of CTZ. The optical cross talk-free feature is exemplified with the multiplex system, which simultaneously illuminated antiestrogenic and rapamycin activities without optical cross talks. This unique protocol contributes to specific and high-throughput BL imaging of multiple optical readouts in mammalian cells without optical contamination. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Category: pyrazines

The Article related to alkynes: chemistry, animals, chlorocebus aethiops, cos cells, estrogen receptor modulators: pharmacology, imidazoles: chemistry, immunosuppressive agents: pharmacology, luciferases: drug effects, luciferases: metabolism, luminescent agents: chemistry, luminescent measurements: methods, optical imaging: methods, pyrazines: chemistry and other aspects.Category: pyrazines

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A. published an article in 2020, the title of the article was Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications.Electric Literature of 55779-48-1 And the article contains the following content:

A review. The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogs with new unique properties has led to the development of new exptl. anal. methods based on them. The com. availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of anal. methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biol. research areas, which confirms them to be a powerful anal. tool. In this , we consider the main directions, results, and achievements in research involving these luciferases. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Electric Literature of 55779-48-1

The Article related to review coelenterazine luciferase bioluminescent system, ca2+-regulated photoprotein, analytical systems, bioluminescence, coelenterazine, luciferase, Pharmaceuticals: Reviews and other aspects.Electric Literature of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem