1202-41-1

Basic information

• Product Name: 3,4-Dihydroxycinnamamide
• Synonyms: 3,4-Dihydroxycinnamamide;2-PropenaMide, 3-(3,4-dihydroxyphenyl)-;3-(3,4-Dihydroxyphenyl)acrylaMide;3-(3,4-Dihydroxyphenyl)
• CAS NO: 1202-41-1
• Molecular Formula: C₉H₉NO₃
• Molecular Weight: 179
• Mol File: 1202-41-1.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 3,4-Dihydroxycinnamamide(CAS DataBase Reference)
• NIST Chemistry Reference: 3,4-Dihydroxycinnamamide(1202-41-1)
• EPA Substance Registry System: 3,4-Dihydroxycinnamamide(1202-41-1)

Safety Data

• Hazardous Substances Data: 1202-41-1(Hazardous Substances Data)

Usage

General Description

3,4-Dihydroxycinnamamide is a chemical compound with the molecular formula C9H9NO3. It is a derivative of cinnamic acid and is also known as 3,4-DHCA. 3,4-Dihydroxycinnamamide has two hydroxyl groups and an amide group attached to the aromatic ring, giving it antioxidant and potential anti-inflammatory properties. 3,4-Dihydroxycinnamamide has been studied for its potential in skin protection and repair, as well as its ability to protect against oxidative stress and inflammation. It is also being investigated for its potential therapeutic applications in conditions such as cancer, Parkinson's disease, and diabetes, although further research is needed to fully understand its biological effects and potential uses.

Upstream product

• 2345-56-4 Malonamic acid 
• 139-85-5 3,4-dihydroxybenzaldehyde 
• 1441337-89-8 C₂₈H₂₃NO₃ 
• 331-39-5 caffeic acid 
• 3843-74-1 Methyl caffeate 

Relevant articles and documents

Identification of cinnamic acid derivatives as novel antagonists of the prokaryotic proton-gated ion channel GLIC

Pentameric ligand gated ion channels (pLGICs) mediate signal transduction. The binding of an extracellular ligand is coupled to the transmembrane channel opening. So far, all known agonists bind at the interface between subunits in a topologically conserved "orthosteric site" whose amino acid composition defines the pharmacological specificity of pLGIC subtypes. A striking exception is the bacterial proton-activated GLIC protein, exhibiting an uncommon orthosteric binding site in terms of sequence and local architecture. Among a library of Gloeobacter violaceus metabolites, we identified a series of cinnamic acid derivatives, which antagonize the GLIC proton-elicited response. Structure-activity analysis shows a key contribution of the carboxylate moiety to GLIC inhibition. Molecular docking coupled to site-directed mutagenesis support that the binding pocket is located below the classical orthosteric site. These antagonists provide new tools to modulate conformation of GLIC, currently used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism.