17243-26-4

Basic information

• Product Name: 4-(acetylamino)phenyl ethyl carbonate
• CAS NO: 17243-26-4
• Molecular Formula: C₁₁H₁₃NO₄
• Molecular Weight: 223.2252
• Mol File: 17243-26-4.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 408.4°C at 760 mmHg
• Flash Point: 200.8°C
• Density: 1.219g/cm³
• Vapor Pressure: 7.02E-07mmHg at 25°C
• Refractive Index: 1.549
• CAS DataBase Reference: 4-(acetylamino)phenyl ethyl carbonate(CAS DataBase Reference)
• NIST Chemistry Reference: 4-(acetylamino)phenyl ethyl carbonate(17243-26-4)
• EPA Substance Registry System: 4-(acetylamino)phenyl ethyl carbonate(17243-26-4)

Safety Data

• Hazardous Substances Data: 17243-26-4(Hazardous Substances Data)

Upstream product

• 108-95-2 phenol 
• 103-90-2 4-acetaminophenol 
• 82619-14-5 ethoxycarbonyloxymethyl iodide 
• 35179-98-7 chloromethyl ethyl carbonate 
• 541-41-3 chloroformic acid ethyl ester 

Relevant articles and documents

Overcoming steric effects in the coupling reaction of alkyloxycarbonyloxymethyl (AOCOM) halides with phenols: an efficient synthesis of AOCOM phenolic prodrugs

Steric hindrance is a key factor in the coupling reaction of AOCOM halides with phenols. Sterically unhindered alkoxy groups favor the formation of acylated phenol. Under phase-transfer conditions, alkylated phenol is favored regardless of steric hindrance.

Specificity of esterases and structure of prodrug esters: Reactivity of various acylated acetaminophen compounds and acetylaminobenzoated compounds

The relative rates of enzymatically catalyzed hydrolysis of various esters of p-acetylaminobenzoic acid (APAB) and variously acylated acetaminophen (APAP) derivatives were measured. Neutral, anionic, and cationic esters were examined. The enzyme sources adopted were rat intestinal homogenate, rat liver homogenate, rat plasma, and a partly purified commercial enzyme. In both APAB and APAP esters, neutral esters were the most sensitive of the enzyme sources examined, and the sensitivity was due to the carbon chain length. The APAP esters were enzymatically more stable than the APAP esters. The relative rates of hydrolysis of these esters varied depending on the enzyme source. The ability of structure recognition was good in rat intestinal homogenate, but weak in rat plasma. These results suggest that ester prodrugs can be designed to cleave preferentially at selected sites along the pathway between absorption and disposition in the body.