Category: 115144-35-9

Sudhaharan, T.; Reddy, A. Ram published the artcile< Metal ion-mediated inhibition of firefly bioluminescence: a possibility via a quaternary complex>, Quality Control of 115144-35-9, the main research area is ATP luciferase luciferin metal ion complex firefly bioluminescence; Photinus bioluminescence ATP luciferase luciferin metal ion complex; conformation luciferase metal ion bioluminescence firefly.

D(-)-Luciferin, interacts with different metal ions to produce colorless soluble salts with absorption spectra broader, intense and red shifted as compared to those of the parent compound The equilibrium constants for the luciferin-metal ion system vary in the order, depository divalent transition metal ions > alkali metal ions. The equilibrium constants for the ternary complexes formed between metal ions and a mixture of luciferin and luciferase are larger than that of binary complexes but vary in the same order. Steady state fluorometric titration’s of luciferin further confirmed its complexation with metal ions. The single absorption maximum of firefly luciferase at 278 nm originating from tyrosine was split into a doublet in presence of transition metal ions. The absorption maximum at lower wavelength is attributed to the H-bond ruptured free tyrosine denatured conformation of the luciferase while the longer wavelength band to tyrosine-transition metal ion complex. Difference spectra of luciferase metal ion complex yielded change in the molar extinction coefficients from which the number of tyrosine mols. exposed to aqueous solution by the perturbant metal ions are evaluated following the Donovan model. The number of tyrosine mols. exposed to the aqueous medium as a result of conformational change in the enzyme are 4, 3, 3, 2 and 3 by Hg2+, Mn2+, Co2+, Cd2+ and Cs+, resp. The denaturation constants calculated for the luciferase-metal ion complexes vary between 0.152 and 0.570 and follow the order of Hg2+ > Cs+ > Cd2+ > Co2+ > Mn2+. Steady state fluorescence data reveal that the metal ions quench the fluorescence of enzyme by complexation with the side chain residues of the excited state tyrosine. Profound change in the UV CD spectrum of luciferin and luciferase in presence of metal ions was attributed to the conformational change in the substrate and enzyme. Thus the inhibition of luciferase activity in the firefly bioluminescence by metal ions is attributed to the quaternary complex formed between metal ion-luciferin-luciferase and ATP near or around the active site of the enzyme.

Indian Journal of Biochemistry & Biophysics published new progress about Bioluminescence. 115144-35-9 belongs to class thiazole, and the molecular formula is C11H7KN2O3S2, Quality Control of 115144-35-9.

Referemce:
Thiazole | C3H3NS – PubChem,
Thiazole | chemical compound | Britannica

Wilkinson, Isabel V. L.; Reynolds, Jessica K.; Galan, Sebastien R. G.; Vuorinen, Aini; Sills, Adam J.; Pires, Elisabete; Wynne, Graham M.; Wilson, Francis X.; Russell, Angela J. published the artcile< Characterisation of utrophin modulator SMT C1100 as a non-competitive inhibitor of firefly luciferase>, Safety of Potassium (S)-2-(6-hydroxybenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylate, the main research area is firefly luciferase bioluminescence enzyme kinetics inhibitor duchenne muscular dystrophy; Assay interference; Bioluminescence; Duchenne muscular dystrophy; Enzyme inhibitor; Enzyme kinetics; Enzyme mechanism; Firefly luciferase; Inhibition mechanism; Photoaffinity probe.

Firefly luciferase (FLuc) is a powerful tool for mol. and cellular biol., and popular in high-throughput screening and drug discovery. However, FLuc assays have been plagued with pos. and neg. artifacts due to stabilization and inhibition by small mols. from a range of chem. classes. Here we disclose Phase II clin. compound SMT C1100 for the treatment of Duchenne muscular dystrophy as an FLuc inhibitor (KD of 0.40 ± 0.15μM). Enzyme kinetic studies using SMT C1100 and other non-competitive inhibitors including resveratrol and NFκBAI4 identified previously undescribed modes of inhibition with respect to FLuc’s luciferyl adenylate intermediate. Employing a photoaffinity strategy to identify SMT C1100’s binding site, a photolabeled SMT C1100 probe instead underwent FLuc-dependent photooxidation Our findings support novel binding sites on FLuc for non-competitive inhibitors.

Bioorganic Chemistry published new progress about Chemiluminescent probes. 115144-35-9 belongs to class thiazole, and the molecular formula is C11H7KN2O3S2, Safety of Potassium (S)-2-(6-hydroxybenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylate.

Referemce:
Thiazole | C3H3NS – PubChem,
Thiazole | chemical compound | Britannica

Wilkinson, Isabel V. L.; Reynolds, Jessica K.; Galan, Sebastien R. G.; Vuorinen, Aini; Sills, Adam J.; Pires, Elisabete; Wynne, Graham M.; Wilson, Francis X.; Russell, Angela J. published the artcile< Characterisation of utrophin modulator SMT C1100 as a non-competitive inhibitor of firefly luciferase>, HPLC of Formula: 115144-35-9, the main research area is firefly luciferase bioluminescence enzyme kinetics inhibitor duchenne muscular dystrophy; Assay interference; Bioluminescence; Duchenne muscular dystrophy; Enzyme inhibitor; Enzyme kinetics; Enzyme mechanism; Firefly luciferase; Inhibition mechanism; Photoaffinity probe.

Firefly luciferase (FLuc) is a powerful tool for mol. and cellular biol., and popular in high-throughput screening and drug discovery. However, FLuc assays have been plagued with pos. and neg. artifacts due to stabilization and inhibition by small mols. from a range of chem. classes. Here we disclose Phase II clin. compound SMT C1100 for the treatment of Duchenne muscular dystrophy as an FLuc inhibitor (KD of 0.40 ± 0.15μM). Enzyme kinetic studies using SMT C1100 and other non-competitive inhibitors including resveratrol and NFκBAI4 identified previously undescribed modes of inhibition with respect to FLuc’s luciferyl adenylate intermediate. Employing a photoaffinity strategy to identify SMT C1100’s binding site, a photolabeled SMT C1100 probe instead underwent FLuc-dependent photooxidation Our findings support novel binding sites on FLuc for non-competitive inhibitors.

Bioorganic Chemistry published new progress about Chemiluminescent probes. 115144-35-9 belongs to class thiazole, and the molecular formula is C11H7KN2O3S2, HPLC of Formula: 115144-35-9.

Referemce:
Thiazole | C3H3NS – PubChem,
Thiazole | chemical compound | Britannica

Cheng, Lin; Su, Lantian; Tian, Xiaowen; Xia, Fan; Zhao, Chang; Yan, Wei; Shao, Zhenhua published the artcile< A pipeline to investigate the structures and signaling pathways of sphingosine 1-phosphate receptors>, Related Products of 115144-35-9, the main research area is sphingosine 1 phosphate receptor structure signaling pathway investigation.

Lysophospholipids (LPLs) are bioactive lipids that include sphingosine 1-phosphate (S1P), lysophosphatidic acid, etc. S1P, a metabolic product of sphingolipids in the cell membrane, is one of the best-characterized LPLs that regulates a variety of cellular physiol. responses via signaling pathways mediated by sphingosine 1-phosphate receptors (S1PRs). This implicated that the S1P-S1PRs signaling system is a remarkable potential therapeutic target for disorders, including multiple sclerosis (MS), autoimmune disorders, cancer, inflammation, and even COVID-19. S1PRs, a small subset of the class A G-protein coupled receptor (GPCR) family, are composed of five subtypes: S1PR1, S1PR2, S1PR3, S1PR4, and S1PR5. The lack of detailed structural information, however, impedes the drug discovery targeting S1PRs. Here, we applied the cryo-electron microscopy method to solve the structure of the S1P-S1PRs complex, and elucidated the mechanism of activation, selective drug recognition, and G-protein coupling by using cell-based functional assays. Other lysophospholipid receptors (LPLRs) and GPCRs can also be studied using this strategy.

Journal of Visualized Experimentspublished new progress about Autoimmune disease. 115144-35-9 belongs to class thiazole, and the molecular formula is C11H7KN2O3S2, Related Products of 115144-35-9.

Referemce:
Thiazole | C3H3NS – PubChem,
Thiazole | chemical compound | Britannica

Chemistry is an experimental science, and the best way to enjoy it and learn about it is performing experiments.Introducing a new discovery about 115144-35-9, Name is Potassium (S)-2-(6-hydroxybenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylate, name: Potassium (S)-2-(6-hydroxybenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylate.

Peroxy-caged luciferin (PCL-1) probe was first used to image hydrogen peroxide in living systems (Van de Bittner et al., 2010 [9]). Recently this probe was shown to react with peroxynitrite more potently than with hydrogen peroxide (Sieracki et al., 2013 [11]) and was suggested to be a more suitable probe for detecting peroxynitrite under in vivo conditions. In this work, we investigated in detail the products formed from the reaction between PCL-1 and hydrogen peroxide, hypochlorite, and peroxynitrite. HPLC analysis showed that hydrogen peroxide reacts slowly with PCL-1, forming luciferin as the only product. Hypochlorite reaction with PCL-1 yielded significantly less luciferin, as hypochlorite oxidized luciferin to form a chlorinated luciferin. Reaction between PCL-1 and peroxynitrite consists of a major and minor pathway. The major pathway results in luciferin and the minor pathway produces a radical-mediated nitrated luciferin. Radical intermediate was characterized by spin trapping. We conclude that monitoring of chlorinated and nitrated products in addition to bioluminescence in vivo will help identify the nature of oxidant responsible for bioluminescence derived from PCL-1.

Peroxy-caged luciferin (PCL-1) probe was first used to image hydrogen peroxide in living systems (Van de Bittner et al., 2010 [9]). Recently this probe was shown to react with peroxynitrite more potently than with hydrogen peroxide (Sieracki et al., 2013 [11]) and was suggested to be a more suitable probe for detecting peroxynitrite under in vivo conditions. In this work, we investigated in detail the products formed from the reaction between PCL-1 and hydrogen peroxide, hypochlorite, and peroxynitrite. HPLC analysis showed that hydrogen peroxide reacts slowly with PCL-1, forming luciferin as the only product. Hypochlorite reaction with PCL-1 yielded significantly less luciferin, as hypochlorite oxidized luciferin to form a chlorinated luciferin. Reaction between PCL-1 and peroxynitrite consists of a major and minor pathway. The major pathway results in luciferin and the minor pathway produces a radical-mediated nitrated luciferin. Radical intermediate was characterized by spin trapping. We conclude that monitoring of chlorinated and nitrated products in addition to bioluminescence in vivo will help identify the nature of oxidant responsible for bioluminescence derived from PCL-1.

Balanced chemical reaction does not necessarily reveal either the individual elementary reactions by which a reaction occurs or its rate law.name: Potassium (S)-2-(6-hydroxybenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylate. In my other articles, you can also check out more blogs about 115144-35-9

Reference£º
Thiazole | C3H9021NS – PubChem,
Thiazole | chemical compound | Britannica