104538-82-1

Basic information

• Product Name: C₃₂H₄₆O₄
• Synonyms: C₃₂H₄₆O₄
• CAS NO: 104538-82-1
• Molecular Weight: 494.715
• Mol File: 104538-82-1.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₃₂H₄₆O₄(CAS DataBase Reference)
• NIST Chemistry Reference: C₃₂H₄₆O₄(104538-82-1)
• EPA Substance Registry System: C₃₂H₄₆O₄(104538-82-1)

Safety Data

• Hazardous Substances Data: 104538-82-1(Hazardous Substances Data)

Upstream product

• 1249-75-8 methyl lithocholate 
• 65-85-0 benzoic acid 

Downstream Products

• 434-13-9 Isolithocholic acid 

Relevant articles and documents

Structure-Activity Relationships and Mechanism of Action of Eph-ephrin Antagonists: Interaction of Cholanic Acid with the EphA2 Receptor

The Eph-ephrin system, including the EphA2 receptor and the ephrinA1 ligand, plays a critical role in tumor and vascular functions during carcinogenesis. We previously identified (3α,5β)-3-hydroxycholan-24-oic acid (lithocholic acid) as an Eph-ephrin antagonist that is able to inhibit EphA2 receptor activation; it is therefore potentially useful as a novel EphA2 receptor-targeting agent. Herein we explore the structure-activity relationships of a focused set of lithocholic acid derivatives based on molecular modeling investigations and displacement binding assays. Our exploration shows that while the 3-α-hydroxy group of lithocholic acid has a negligible role in recognition of the EphA2 receptor, its carboxylate group is critical for disrupting the binding of ephrinA1 to EphA2. As a result of our investigation, we identified (5β)-cholan-24-oic acid (cholanic acid) as a novel compound that competitively inhibits the EphA2-ephrinA1 interaction with higher potency than lithocholic acid. Surface plasmon resonance analysis indicates that cholanic acid binds specifically and reversibly to the ligand binding domain of EphA2, with a steady-state dissociation constant (KD) in the low micromolar range. Furthermore, cholanic acid blocks the phosphorylation of EphA2 as well as cell retraction and rounding in PC3 prostate cancer cells, two effects that depend on EphA2 activation by the ephrinA1 ligand. These findings suggest that cholanic acid can be used as a template structure for the design of effective EphA2 antagonists, and may have potential impact in the elucidation of the role played by this receptor in pathological conditions.