1152-14-3Relevant academic research and scientific papers
Colorimetric and fluorescence analysis of percarbonate and oxygen bleach by perhydrolysis of resorufin ester
Ahn, Sangdoo,Chang, Suk-Kyu,Choi, Myung Gil,Kim, Na Young,Lee, Kang Min,Park, Ka Young,Yoo, Jae Hoon
, (2021)
Percarbonate is an important oxidant that is widely used in industrial applications and daily life. In this study, a simple colorimetric and fluorescence method for percarbonate determination using resorufin-based probe 1, carrying a pivaloyl protection group as a signaling switch, was developed. Probe 1 exhibited selective and sensitive signaling behavior for percarbonate via perhydrolysis of the pivaloyl group by hydrogen peroxide that was produced from percarbonate, in the presence of commonly encountered metal ions and anions. Among the esters tested as signaling switches, pivalate was optimal owing to its resistance to spontaneous hydrolysis and high signaling speed under the employed conditions. The detection limit for percarbonate was estimated to be 0.45 μM. The probe was applied to the analysis of percarbonate in domestic bleach using a scanner as a field-oriented signal-capturing device.
Set-up and validation of a high throughput screening method for human monoacylglycerol lipase (MAGL) based on a new red fluorescent probe
Miceli, Matteo,Casati, Silvana,Ottria, Roberta,Di Leo, Simone,Eberini, Ivano,Palazzolo, Luca,Parravicini, Chiara,Ciuffreda, Pierangela
supporting information, (2019/06/20)
Monoacylglycerol lipase (MAGL) is a serine hydrolase that has a key regulatory role in controlling the levels of 2-arachidonoylglycerol (2-AG), the main signaling molecule in the endocannabinoid system. Identification of selective modulators of MAGL enables both to provide new tools for investigating pathophysiological roles of 2-AG, and to discover new lead compounds for drug design. The development of sensitive and reliable methods is crucial to evaluate this modulatory activity. In the current study, we report readily synthesized long-wavelength putative fluorogenic substrates with different acylic side chains to find a new probe for MAGL activity. 7-Hydroxyresorufinyl octanoate proved to be the best substrate thanks to the highest rate of hydrolysis and the best Km and Vmax values. In addition, in silico evaluation of substrates interaction with the active site of MAGL confirms octanoate resorufine derivative as the molecule of choice. The well-known MAGL inhibitors URB602 and methyl arachidonylfluorophosphonate (MAFP) were used for the assay validation. The assay was highly reproducible with an overall average Z0 value of 0.86. The fast, sensitive and accurate method described in this study is suitable for low-cost high-throughput screening (HTS) of MAGL modulators and is a powerful new tool for studying MAGL activity.
