805201-62-1

Basic information

• Product Name: 3-METHOXY-4-(3-PIPERIDIN-1-YLPROPOXY)ANILINE
• Synonyms: 3-METHOXY-4-(3-PIPERIDIN-1-YLPROPOXY)ANILINE
• CAS NO: 805201-62-1
• Molecular Formula: C15H24N2O2
• Molecular Weight: 264.36
• Mol File: 805201-62-1.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 3-METHOXY-4-(3-PIPERIDIN-1-YLPROPOXY)ANILINE(CAS DataBase Reference)
• NIST Chemistry Reference: 3-METHOXY-4-(3-PIPERIDIN-1-YLPROPOXY)ANILINE(805201-62-1)
• EPA Substance Registry System: 3-METHOXY-4-(3-PIPERIDIN-1-YLPROPOXY)ANILINE(805201-62-1)

Safety Data

• Hazardous Substances Data: 805201-62-1(Hazardous Substances Data)

Upstream product

• 136616-34-7 1-piperidino-3-(2-methoxy-4-nitrophenoxy)propane 
• 2287-09-4 α-Bromo-ω-(2-methoxy-4-nitrophenoxy)propane 
• 3251-56-7 2-methoxy-4-nitrophenol 

Relevant articles and documents

Discovery of novel anti-breast cancer agents derived from deguelin as inhibitors of heat shock protein 90 (HSP90)

A series of O-substituted analogues of the B,C-ring truncated scaffold of deguelin were designed as C-terminal inhibitors of heat shock protein 90 (HSP90) and investigated as novel antiproliferative agents against HER2-positive breast cancer. Among the synthesized compounds, compound 80 exhibited significant inhibition in both trastuzumab-sensitive and trastuzumab-resistant breast cancer cells, whereas compound 80 did not show any cytotoxicity in normal cells. Compound 80 markedly downregulated the expression of the major client proteins of HSP90 in both cell types, indicating that the cytotoxicity of 80 in breast cancer cells is attributed to the destabilization and inactivation of HSP90 client proteins and that HSP90 inhibition represents a promising strategy to overcome trastuzumab resistance. A molecular docking study of 80 with the homology model of a HSP90 homodimer showed that 80 fit nicely in the C-terminal domain with a higher electrostatic complementary score than that of ATP.

Discovery of Potent Human Glutaminyl Cyclase Inhibitors as Anti-Alzheimer’s Agents Based on Rational Design

Glutaminyl cyclase (QC) has been implicated in the formation of toxic amyloid plaques by generating the N-terminal pyroglutamate of β-amyloid peptides (pGlu-Aβ) and thus may participate in the pathogenesis of Alzheimer’s disease (AD). We designed a library of glutamyl cyclase (QC) inhibitors based on the proposed binding mode of the preferred substrate, Aβ3E?42. An in vitro structure-activity relationship study identified several excellent QC inhibitors demonstrating 5- to 40-fold increases in potency compared to a known QC inhibitor. When tested in mouse models of AD, compound 212 significantly reduced the brain concentrations of pyroform Aβ and total Aβ and restored cognitive functions. This potent Aβ-lowering effect was achieved by incorporating an additional binding region into our previously established pharmacophoric model, resulting in strong interactions with the carboxylate group of Glu327 in the QC binding site. Our study offers useful insights in designing novel QC inhibitors as a potential treatment option for AD.

THIA-TETRAAZAACENAPHTHYLENE KINASE INHIBITORS

The present invention is directed to novel thia-tetraazaacenaphthylene compounds of Formula (I): and pharmaceutically acceptable forms thereof and their synthesis and use as inhibitors of ATP-protein kinase interactions.