57855-18-2

Basic information

• Product Name: 2-butyl-6-methoxycyclohexa-2,5-diene-1,4-dione
• Synonyms: 2,5-cyclohexadiene-1,4-dione, 2-butyl-6-methoxy-; 2-Butyl-6-methoxy-1,4-benzoquinone; 2-Butyl-6-methoxy-2,5-cyclohexadiene-1,4-dione
• CAS NO: 57855-18-2
• Molecular Formula: C₁₁H₁₄O₃
• Molecular Weight: 194.2271
• Mol File: 57855-18-2.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 301.5°C at 760 mmHg
• Flash Point: 130.8°C
• Density: 1.08g/cm³
• Vapor Pressure: 0.00105mmHg at 25°C
• Refractive Index: 1.497
• CAS DataBase Reference: 2-butyl-6-methoxycyclohexa-2,5-diene-1,4-dione(CAS DataBase Reference)
• NIST Chemistry Reference: 2-butyl-6-methoxycyclohexa-2,5-diene-1,4-dione(57855-18-2)
• EPA Substance Registry System: 2-butyl-6-methoxycyclohexa-2,5-diene-1,4-dione(57855-18-2)

Safety Data

• Hazardous Substances Data: 57855-18-2(Hazardous Substances Data)

Upstream product

• 148-53-8 3-methoxy-2-hydroxybenzaldehyde 
• 130223-24-4 6-butyl-2-methoxyphenol 

Relevant articles and documents

Development of natural product-derived receptor tyrosine kinase inhibitors based on conservation of protein domain fold

Receptor tyrosine kinases (RTKs) such as Tie-2, IGF1R, Her-2/Neu, EGFR, and VEGFR1-3 play crucial roles in the control of cell growth and differentiation. Inhibition of such RTKs has become a major focus of current anticancer drug development, and therefore the discovery of new classes of inhibitors for these signal-transducing proteins is of prime importance. We have recently proposed a novel concept for improving the hit-finding process by employing natural products as biologically validated starting points in structural space for compound library development. In this concept, natural products are regarded as evolutionary chosen ligands for protein domains which are structurally conserved yet genetically mobile. Here we report on the discovery of novel and highly selective VEGFR-2 and -3, Tie-2, and IGF1R inhibitors derived from the naturally occurring Her-2/Neu kinase inhibitor nakijiquinone C and developed on the basis of this concept. Based on the structure of the natural product, a small library (74 members) was synthesized and investigated for inhibition of kinases with highly similar ATP-binding domains. The library yielded inhibitors with IC50s in the low micromolar range with high frequency (7 out of 74). In particular, four inhibitors of Tie-2 were found, a kinase critically involved in the formation of new blood vessels from preexisting ones (angiogenesis) and believed to be a new promising target in antitumor therapy. These results support the "domain concept". To advance the development of improved inhibitors, extensive molecular modeling studies were undertaken, including the construction of new homology models for VEGFR-2 and Tie-2. These studies revealed residues in the kinase structure which are crucial to the development of tailor-made receptor tyrosine kinase inhibitors.