81-87-8Relevant academic research and scientific papers
Oxidation pathways for the intracellular probe 2',7'-dichlorofluorescin
Zhu, Huan,Bannenberg, Gerard L.,Moldeus, Peter,Shertzer, Howard G.
, p. 582 - 587 (1994)
The oxidation of 2',7'-dichlorofluorescin (DCFH) to a fluorescent product is currently used to evaluate oxidant stress in cells. However, there is considerable uncertainty as to the enzymatic and nonenzymatic pathways that may result in DCFH oxidation. Iron/hydrogen peroxide-induced DCFH oxidation was inhibited by catalase or by the hydroxyl radical scavenger dimethyl sulfoxide; however, superoxide dismutase (SOD) had no effect on DCFH oxidation. The formation of hydroxyl radical (indicated by the oxidation of salicylic acid to 2,3-dihydroxybenzoic acid) was proportional to DCFH oxidation, suggesting that the hydroxyl radical is responsible for the iron/peroxide-mediated oxidation of DCFH. Utilizing a superoxide generating system consisting of hypoxanthine/xanthine oxidase, oxidation of DCFH was unaffected by SOD, catalase or desferoxamine, and stimulated by removing hypoxanthine from the reaction mixture. In contrast, SOD or elimination of hypoxanthine abolished superoxide formation. In addition, potassium superoxide did not support the oxidation of DCFH. Thus, superoxide is not involved in DCFH oxidation. Boiling xanthine oxidase eliminated its concentration-dependent oxidation of 1 μM DCFH, indicating that xanthine oxidase can enzymatically utilize DCFH as a highly affinity substrate. Kinetic studies of the oxidation of DCFH by xanthine oxidase indicated a Km(app) of 0.62 μM. Hypoxanthine competed with DCFH with a Ki(app) of 1.03 mM. These studies suggest that DCFH oxidation may be a useful indicator of oxidative stress. However, other types of cellular damage may produce DCFH oxidation. For example, conditions or chemicals that damage intracellular membranes may release to the cytoplasm oxidases or peroxidases that might use DCFH as a substrate, similar to xanthine oxidase. - Keywords: Dichlorofluorescein; Iron; Hydrogen peroxide; Hydroxyl radical; Oxidative stress; Superoxide anion; Xanthine oxidase
Fat mass and obesity-associated protein (FTO) inhibitors prepared from 9-(2-carboxyphenyl) xanthene compounds and therapeutic effects thereof
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Paragraph 0055-0058; 0059-0061, (2020/07/13)
The invention relates to usage of the following general formula I as a drug for diseases targeting fat mass and obesity-associated protein (FTO), and provides usage of 9-(2-carboxyphenyl) xanthene compounds in preparation of FTO inhibitors. Specifically, the invention discloses usage of the 9-(2-carboxyphenyl) xanthene compounds as shown in the formula (I), as well as derivatives and pharmaceutically acceptable salts thereof, in preparation of the FTO inhibitors or pharmaceutical compositions for treating FTO-related diseases.
Synthetic molecules for labeling histidine-rich proteins
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Page 9, (2008/06/13)
The invention provides Zn-chelating compounds that are molecularly engineered to bind to a specific target sequence in a protein of interest. The Zn2+0 ion is far less toxic and promiscuous than nickel and therefore provides an attractive alternative to Ni-based labeling systems. Invention Zn-chelating compounds also do not require oxidizable thiols and therefore can be used in non-reducing environments such as the surface of living cells. In addition, the target sequence is genetically encodable and requires incorporation of only a few amino acids, unlike fusions to fluorescent proteins such as GFP.
