914465-85-3

Basic information

• Product Name: 3-FLUORO-5-METHOXYBENZYLAMINE
• Synonyms: 3-FLUORO-5-METHOXYBENZYLAMINE;(3-Fluoro-5-methoxyphenyl)methanamine;3-fluoro-5-methoxybenzenemethanamine
• CAS NO: 914465-85-3
• Molecular Formula: C8H10FNO
• Molecular Weight: 155.1695032
• Mol File: 914465-85-3.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 3-FLUORO-5-METHOXYBENZYLAMINE(CAS DataBase Reference)
• NIST Chemistry Reference: 3-FLUORO-5-METHOXYBENZYLAMINE(914465-85-3)
• EPA Substance Registry System: 3-FLUORO-5-METHOXYBENZYLAMINE(914465-85-3)

Safety Data

• Hazardous Substances Data: 914465-85-3(Hazardous Substances Data)

Usage

General Description

3-Fluoro-5-methoxybenzylamine is a chemical compound with the molecular formula C8H10FNO. It is a benzylamine derivative with a fluorine atom at the 3 position and a methoxy group at the 5 position of the benzene ring. 3-FLUORO-5-METHOXYBENZYLAMINE is commonly used in organic synthesis and pharmaceutical research as a building block for the synthesis of various biologically active molecules. It has potential applications in the development of new drugs and pharmaceutical products. Additionally, it may also be used as a reagent in chemical reactions to introduce specific functional groups into organic molecules.

Upstream product

• 439280-18-9 3-Fluoro-5-methoxybenzonitrile 
• 699016-24-5 3-fluoro-5-methoxybenzaldehyde 

Relevant articles and documents

MONO AND BICYCLIC RING BORONIC ACID, ESTER AND SALT COMPOUNDS AS INHIBITORS OF P97 COMPLEX

Monocyclic or bicyclic ring boronic acid or ester compounds having an arylalkyi amine substituent at the 4 position and a substituted 5:6 bicyclic group at the 2 position of the mono or bicyclic ring boronic acid or ester as well as optional aliphatic, functional and/or aromatic components substituted at other positions of the mono or bicyclic boronic acid or ester compounds are disclosed. These compounds are inhibitors of the AAA proteasome complex containing p97 and are effective medicinal agents for treatment of diseases associated with the Valosin containing protein and p97 bioactivity such as cancer. Formula (I).

New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: Analysis by SARs and computational docking

Structure activity relationships for semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1) were studied using a library of arylalkylamine substrates, with the aim of contributing to the discovery of more efficient SSAO substrates. Experimental data were contrasted with computational docking studies, thereby allowing us to examine the mechanism and substrate-binding affinity of SSAO and thus contribute to the discovery of more efficient SSAO substrates and provide a structural basis for their interactions. We also built a model of the mouse SSAO structure, which provides several structural rationales for interspecies differences in SSAO substrate selectivity and reveals new trends in SSAO substrate recognition. In this context, we identified novel efficient substrates for human SSAO that can be used as a lead for the discovery of antidiabetic agents.