25951-24-0Relevant academic research and scientific papers
Acceptorless dehydrogenation of primary alcohols to carboxylic acids by self-supported NHC-Ru single-site catalysts
Yin, Shenxiang,Zheng, Qingshu,Chen, Jie,Tu, Tao
, p. 165 - 172 (2022/03/23)
The acceptorless dehydrogenation of diverse aromatic and aliphatic primary alcohols to corresponding carboxylic acids has been accomplished by self-supported NHC-Ru single-site catalysts under mild reaction conditions. Besides broad substrates with excellent activity, selectivity and good tolerance to sensitive functional groups, the solid single-site catalyst could be recovered and reused for more than 20 runs without deactivation. Remarkably, up to 1.8 × 104 turnover numbers could be achieved by this newly developed sustainable protocol in gram scale at low catalyst loading, highlighting its potential in industry.
A Cleavable C2-Symmetric trans-Cyclooctene Enables Fast and Complete Bioorthogonal Disassembly of Molecular Probes
Carlson, Jonathan C. T.,Haider, Maximilian,Herrmann, Barbara,Klubnick, Jenna,Mikula, Hannes,Sohr, Barbara,Weissleder, Ralph,Wilkovitsch, Martin
supporting information, p. 19132 - 19141 (2020/11/13)
Bioorthogonal chemistry is bridging the divide between static chemical connectivity and the dynamic physiologic regulation of molecular state, enabling in situ transformations that drive multiple technologies. In spite of maturing mechanistic understanding and new bioorthogonal bond-cleavage reactions, the broader goal of molecular ON/OFF control has been limited by the inability of existing systems to achieve both fast (i.e., seconds to minutes, not hours) and complete (i.e., >99%) cleavage. To attain the stringent performance characteristics needed for high fidelity molecular inactivation, we have designed and synthesized a new C2-symmetric trans-cyclooctene linker (C2TCO) that exhibits excellent biological stability and can be rapidly and completely cleaved with functionalized alkyl-, aryl-, and H-tetrazines, irrespective of click orientation. By incorporation of C2TCO into fluorescent molecular probes, we demonstrate highly efficient extracellular and intracellular bioorthogonal disassembly via omnidirectional tetrazine-triggered cleavage.
D-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-D-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice
Shibata, Kimihiko,Imanishi, Daiki,Abe, Katsumasa,Suzuki, Masataka,Takahashi, Shouji,Kera, Yoshio
, (2020/09/04)
N-Methyl-D-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of D-aspartate N-methyltransferase (DDNMT), which produces NMDA from D-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for D-aspartate and is S-adenosyl-L-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).
Synthesis of Deuterated or Tritiated Glycine and Its Methyl Ester
Shevchenko,Andreeva,Nagaev, I. Yu.,Myasoedov
, p. 266 - 267 (2019/01/03)
Abstract: Heating glycine (Gly) and methyl glycinate (GlyOCH3) supported on 5% Pd/C or 5% Pt/C in a deuterium or tritium gas atmosphere gave the isotope-labeled products. The experiments were carried out at 180°C for 10 min. The deuterium atom inclusion under these conditions averaged up to 1.8 atoms per molecule for Gly and up to 1.0 atom per molecule for GlyOCH3. The reaction with tritium gas gave labeled products with a specific radioactivity of 27–31 Ci/mmol for Gly and 18 Ci/mmol for GlyOCH3.
Unraveling Tetrazine-Triggered Bioorthogonal Elimination Enables Chemical Tools for Ultrafast Release and Universal Cleavage
Carlson, Jonathan C.T.,Mikula, Hannes,Weissleder, Ralph
supporting information, p. 3603 - 3612 (2018/03/21)
Recent developments in bond cleavage reactions have expanded the scope of bioorthogonal chemistry beyond click ligation and enabled new strategies for probe activation and therapeutic delivery. These applications, however, remain in their infancy, with fu
Purification and characterization of carbon-phosphorus bond-cleavage enzyme from glyphosate degrading pseudomonas putida T5
Selvi, A. Arul,Manonmani
, p. 380 - 397 (2015/10/29)
An inducible, carbon-phosphorus bond-cleavage enzyme was purified from cells of Pseudomonas putida T5 grown on N-phosphonomethyl glycine. The native enzyme had a molecular mass of approximately 70 kD and upon sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), yielded a homogeneous protein band with an apparent molecular mass of about 70 kD. Activity of purified enzyme was increased by 627-fold compared to the crude extract and showed pH and temperature optima of approximately 7 and 30°C, respectively. The purified enzyme had an apparent Km and Vmax of 3.7 mM and 6.8 mM/min, respectively, for its sole substrate N-phosphonomethyl glycine. The enzyme was inhibited by phenylmethylsulfonyl fluoride (PMSF), indicating the presence of serine at the active site. The enzyme was not inhibited by SDS, suggesting the absence of disulfide linkage in the enzyme. The enzyme was found to be inhibited by most of the metals studied except Mg2+. Detergents studied also inhibited glyphosate acting as a carbon-phosphorus bond-cleavage enzyme. Thus initial characterization of the purified enzyme suggested that it could be used as a potential candidate for glyphosate bioremediation.
Chemically reactive supramolecular hydrogel coupled with a signal amplification system for enhanced analyte sensitivity
Yoshii, Tatsuyuki,Onogi, Shoji,Shigemitsu, Hajime,Hamachi, Itaru
, p. 3360 - 3365 (2015/03/30)
Multicomponent supramolecular hydrogels are constructed for sensitive, naked-eye detection of small-molecule biomarkers. A dendritic self-immolative molecule and the corresponding enzyme as a signal amplification system were stably embedded in a hydrogen peroxide (H2O2)-responsive supramolecular hydrogel (BPmoc-F3), together with other enzymes. The nanostructure and mechanical strength of the hybrid BPmoc-F3 gel were not substantially diminished by incorporation of these multiple components in the absence of target biomarkers, but could be destroyed by addition of the biomarker through the multiple enzymatic and chemical cascade reactions operating in combination within the gel matrix. The sensitivity to biomarkers such as H2O2, glucose, and uric acid, detected by gel-sol transition, was significantly enhanced by the signal amplification system. An array chip consisting of these multicomponent hydrogels enabled the detection of the level of hyperuricemia disease in human plasma samples.
POTENT AND SELECTIVE INHIBITORS OF NAV1.7
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Page/Page column, (2015/02/18)
Disclosed is a composition of matter comprising an isolated polypeptide, which is a peripherally-restricted Nav1.7 inhibitor. In some disclosed embodiments, the isolated polypeptide is an inhibitor of Nav1.7. Other embodiments are conjugated embodiments of the inventive composition of matter and pharmaceutical compositions containing the inventive composition of matter. Isolated nucleic acids encoding some embodiments of inventive polypeptides and expression vectors, and recombinant host cells containing them are disclosed. A method of treating or preventing pain is also disclosed.
FUNCTIONALIZED FLUORINE CONTAINING PHTHALOCYANINE MOLECULES
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, (2015/03/16)
Functionalized fluorine containing phthalocyanine molecules, methods of making, and methods of use in diagnostic applications and disease treatment are disclosed herein. In some embodiments, the fluorine containing phthalocyanine molecules are functionalized with a reactive functional group or at least one cancer-targeting ligand (CTL). The CTL can facilitate more efficient binding and/or internalization to a cancer cell than to a healthy cell. The CTL can inhibit expression of oncoprotein in some embodiments. The pthalocyanine moiety can be used in diagnostic applications, such as fluorescence labeling of a cancer cell, and/or treatment applications, such as catalyzing formation of a reactive oxygen species (ROS) which can contribute to cell death of a cancer cell.
Folate in demethylation: The crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate
Luka, Zigmund,Pakhomova, Svetlana,Loukachevitch, Lioudmila V.,Newcomer, Marcia E.,Wagner, Conrad
, p. 392 - 398 (2014/07/07)
Dimethylglycine dehydrogenase (DMGDH) is a mammalian mitochondrial enzyme which plays an important role in the utilization of methyl groups derived from choline. DMGDH is a flavin containing enzyme which catalyzes the oxidative demethylation of dimethylglycine in vitro with the formation of sarcosine (N-methylglycine), hydrogen peroxide and formaldehyde. DMGDH binds tetrahydrofolate (THF) in vivo, which serves as an acceptor of formaldehyde and in the cell the product of the reaction is 5,10-methylenetetrahydrofolate instead of formaldehyde. To gain insight into the mechanism of the reaction we solved the crystal structures of the recombinant mature and precursor forms of rat DMGDH and DMGDH-THF complexes. Both forms of DMGDH reveal similar kinetic parameters and have the same tertiary structure fold with two domains formed by N- and C-terminal halves of the protein. The active center is located in the N-terminal domain while the THF binding site is located in the C-terminal domain about 40 ? from the isoalloxazine ring of FAD. The folate binding site is connected with the enzyme active center via an intramolecular channel. This suggests the possible transfer of the intermediate imine of dimethylglycine from the active center to the bound THF where they could react producing a 5,10- methylenetetrahydrofolate. Based on the homology of the rat and human DMGDH the structural basis for the mechanism of inactivation of the human DMGDH by naturally occurring His109Arg mutation is proposed. 2014 Elsevier Inc. All rights reserved.
