118290-05-4

Basic information

• Product Name: DDAO
• Synonyms: 7-HYDROXY-9H-(1,3-DICHLORO-9,9-DIMETHYLACRIDIN-2-ONE);DDAO;1,3-Dichloro-7-hydroxy-9,9-dimethyl-2(9H)-acridinone;DDAO [9H-(1,3-dichloro-9,9-diMethylacridin-2-one)] *Reference Standard*;DDAO [7-hydroxy-9H-(1,3-dichloro-9,9-dimethylacridin-2-one)] *CAS 118290-05-4*
• CAS NO: 118290-05-4
• Molecular Formula: C₁₅H₁₁Cl₂NO₂
• Molecular Weight: 308.16
• Mol File: 118290-05-4.mol

Chemical Properties

• Boiling Point: 449℃
• Flash Point: 225℃
• Appearance: /
• Density: 1.46
• Vapor Pressure: 3.12E-12mmHg at 25°C
• PKA: 9.97±0.60(Predicted)
• CAS DataBase Reference: DDAO(CAS DataBase Reference)
• NIST Chemistry Reference: DDAO(118290-05-4)
• EPA Substance Registry System: DDAO(118290-05-4)

Safety Data

• Hazardous Substances Data: 118290-05-4(Hazardous Substances Data)

Usage

Uses

Used in Enzyme Substrates Preparation:
DDAO is used as a red fluorophore for the preparation of enzyme substrates, which are essential for studying enzyme activity and function in various biological processes.
Used in Spectrophotometric Determination:
DDAO is used as a reagent for the spectrophotometric determination of phenols and other aromatic compounds. This application is crucial in chemical analysis and quality control, as it helps in the accurate measurement and identification of these compounds in various samples.

InChI:InChI=1/C15(11)12/h4-5H,2-3,9H2,1H3,(H,10,13)(H,11,12)(H,14,15)/p-2

Upstream product

• 118290-04-3 1,3-Dichloro-9,9-dimethyl-9,10-dihydro-acridine-2,7-diol 
• 101-38-2 2,6-dichloroquinone-4-chloroimide 
• 7765-97-1 meta-hydroxy-α,α-dimethylbenzyl alcohol 
• 118290-03-2 2,6-Dichloro-4-[4-hydroxy-2-(1-hydroxy-1-methyl-ethyl)-phenylamino]-phenol 
• 64-17-5 ethanol 
• 1407499-96-0 C₄₅H₃₁Br₂Cl₂F₃N₂O₁₄ 
• 137041-53-3 2,6-Dichloro-4-[4-hydroxy-2-(1-hydroxy-1-methyl-ethyl)-phenylimino]-cyclohexa-2,5-dienone 

Downstream Products

• 1407499-95-9 C₅₀H₃₇Br₂Cl₄N₃O₁₃ 
• 1407499-96-0 C₄₅H₃₁Br₂Cl₂F₃N₂O₁₄ 
• 1453905-13-9 C₃₂H₂₅Cl₂N₃O₁₁ 
• 1453905-12-8 C₃₅H₃₂Cl₂N₂O₁₂ 
• 1453905-11-7 C₃₃H₂₈Cl₂N₂O₉ 
• 1453905-14-0 C₃₃H₂₆Br₂Cl₂N₂O₉ 

Relevant articles and documents

Synthesis of a far-red fluorophore and its use as an esterase probe in living cells

We report the synthesis of a new far-red fluorophore, 1,3-dichloro-7-hydroxy-2H-spiro[acridine-9,1′-cyclohexane]-2′,5′-diene-2,4′-dione (DSACO), which was modified to make two esterase probes: DSACO-2-AME and DSACO-7-AME. Both probes act as "turn-on" substrates for esterases and lipases. DSACO-2-AME exhibited efficient esterase-activated fluorescence inside living cells and is a stable, far-red alternative for the widely-used fluorescein diacetate.

A chemically encoded timer for dual molecular delivery at tailored ranges and concentrations

Spatiotemporal control of molecular distribution is much in demand in many fields of chemistry. To address this goal, we exploit a low molecular weight branched self-immolative architecture, which acts as a triggerable chemically encoded timer for autonomous sequential release of two chemicals. Using a light-activated model liberating two distinct fluorophores, we generated a tunable spatially contrasted molecular distribution.

Assessment of the inhibitory effects of pyrethroids against human carboxylesterases

Pyrethroids are broad-spectrum insecticides that widely used in many countries, while humans may be exposed to these toxins by drinking or eating pesticide-contaminated foods. This study aimed to investigate the inhibitory effects of six commonly used pyrethroids against two major human carboxylesterases (CES) including CES1 and CES2. Three optical probe substrates for CES1 (DME, BMBT and DMCB) and a fluorescent probe substrate for CES2 (DDAB) were used to characterize the inhibitory effects of these pyrethroids. The results demonstrated that most of the tested pyrethroids showed moderate to weak inhibitory effects against both CES1 and CES2, but deltamethrin displayed strong inhibition towards CES1. The IC50 values of deltamethrin against CES1-mediated BMBT, DME, and DMCB hydrolysis were determined as 1.58?μM, 2.39?μM, and 3.3?μM, respectively. Moreover, deltamethrin was cell membrane permeable and capable of inhibition endogenous CES1 in living cells. Further investigation revealed that deltamethrin inhibited CES1-mediated BMBT hydrolysis via competitive manner but noncompetitively inhibited DME or DMCB hydrolysis. The inhibition behaviors of deltamethrin against CES1 were also studied by molecular docking simulation. The results demonstrated that CES1 had at least two different ligand-binding sites, one was the DME site and another was the BMBT site which was identical to the binding site of deltamethrin. In summary, deltamethrin was a strong reversible inhibitor against CES1 and it could tightly bind on CES1 at the same ligand-binding site as BMBT. These findings are helpful for the deep understanding of the interactions between xenobiotics and CES1.

A far-red fluorescent probe for sensing laccase in fungi and its application in developing an effective biocatalyst for the biosynthesis of antituberculous dicoumarin

A far-red fluorescent probe has been developed for sensing fungal laccase. The probe was used to determine that Rhizopus oryzae had a high level endogenous laccase amongst 24 fungal strains. The Rhizopus oryzae was then used as a biocatalyst for the preparation of dicoumarin resulting in significant inhibition of Mycobacterium tuberculosis H37Ra.

Syntheses and kinetic studies of cyclisation-based self-immolative spacers

Kinetic analysis of the disassembly of self-immolative spacers based on cyclisation processes was performed. Five compounds were synthesized belonging to two different series, and their kinetic constants were determined. Electron-donating substituents gav

"Self-immolative" spacer for uncaging with fluorescence reporting

Dual photoliberation: A caged, branched, self-immolative spacer (see scheme, gray box) was designed to rapidly and simultaneously release a desired compound (green) and a fluorophore (red) upon photoactivation. Careful kinetic analysis of the disassembly of the spacer shows that it occurs on the shortest time scale reported to date.

A rapid method for preparing chromogenic alfa-amylase substrate compounds at high preparative yields

A method for preparing chromogenic α-amylase substrate compounds at substantially high preparative yields in a relatively short period of time by the transglucosylation of a chromogenic glucoside compound to a maltooligosaccharide chain. The concentration of the maltooligosaccharide compound is greater than about 3 times the concentration of the chromogenic glucoside compound to result in at least about 50% of the chromogenic glucoside compound being converted to the desired chromogenic α-amylase substrate compound.

Chromogenic acridinone enzyme substrates

Chromogenic acridinone enzyme substrate compounds comprising 7-hydroxy-9H-acridin-2-one chromogens derivatized at the 7-hydroxy-position with an enzymatically-cleavable group and disubstituted at the 9-position with alkyl or aryl groups, which can be the same or different, preferably lower alkyl or phenyl, respectively, or together form a cyclohexa-2,5-diene-4-one residue or a 4-hydroxycycloxhexyl residue, and 7-hydroxy-1,3-dihalo-9,9-dimethyl-acridin-2-one intermediates useful for the preparation of the novel chromogenic acridinone enzyme substrate compounds and methods therefor. The enzymatically-cleavable group is a radical of a compound Y-OH comprising an enzyme-specific moiety which is capable of being cleaved by a specific enzyme wherein a deprotonated form of the chromogen is liberated having an absorbance maximum in basic solution which is substantially greater than the absorbance maximum of the chromogenic acridinone enzyme substrate compound to provide a distinct change in absorbance which can be accurately measured and correlated to the amount of enzyme present in a liquid test sample.