1609690-73-4

Upstream product

• 70-70-2 4-hydroxypropiophenone 
• 121-97-1 4-Methoxypropiophenone 
• 1056899-49-0 5-chloro-2-(4-methoxyphenyl)-3-methylbenzofuran 
• 695-96-5 2-bromo-4-chlorophenol 

Downstream Products

• 1609690-76-7 C₁₇H₁₃ClO₃ 
• 1609690-74-5 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tetra-O-acetyl-β-D-glucopyranoside 
• 1609690-80-3 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tetra-O-acetyl-β-D-galactopyranoside 
• 1609690-82-5 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tri-O-acetyl-β-L-fucopyranoside 
• 1609690-81-4 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tetra-O-acetyl-β-L-galactopyranoside 
• 1609690-90-5 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tri-O-benzoyl-α-L-rhamnopyranoside 
• 1609690-91-6 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl-α-L-rhamnopyranoside 
• 1609690-78-9 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl-β-D-glucopyranoside 
• 1609690-83-6 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl-β-L-glucopyranoside 
• 1609690-84-7 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl-β-D-galactopyranoside 
• 1609690-85-8 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl-β-L-galactopyranoside 
• 1609690-75-6 4-[5-chloro-3-methylbenzofuran-2-yl]phenyl tetra-O-acetyl-α-D-glucopyranoside 

Relevant academic research and scientific papers

Synthesis of Functionalized 2-(4-Hydroxyphenyl)-3-methylbenzofuran Allosteric Modulators of Hsp90 Activity

Hsp90 is a molecular chaperone that plays a pivotal role in the cell life cycle. ATP-regulated internal dynamics are critical to Hsp90 function and we recently demonstrated that these dynamics can be modulated in an allosteric fashion; the protein C-terminal domain (CTD) can be effectively targeted with a family of 2-phenyl-benzofuran derivatives. Here we describe the expansion of the initial library, reporting 28 new derivatives that explore the chemical space at opposite ends of the benzofuran scaffold. Interactions of the compounds with a full-length protein homolog were explored by Saturation Transfer Difference (STD) NMR spectroscopy. In this context we also report the interaction epitope of Novobiocin, a known CTD inhibitor.

Synthesis of potential allosteric modulators of Hsp90 by chemical glycosylation of Eupomatenoid-6

Hsp90 (Heat shock protein-90) is a chaperone protein and an established anti-apoptotic target in cancer therapy. Most of the known small-molecule inhibitors that have shown potent antitumor activity target the Hsp90 N-terminal domain and directly inhibit its ATP-ase activity. Many of these molecules display important secondary effects. A different approach to Hsp90 inhibition consists of targeting the protein C-terminal domain (CTD) and modulating its chaperone activity through allosteric effects. Using an original computational approach, allosteric hot-spots in the CTD have been recently identified that control interdomain communication. A combination of virtual and experimental screening enabled identification of a rhamnosylated benzofuran (Eupomatenoid-2) as a lead for further development. In this paper we describe glycodiversification of Eupomatenoid-2 using chemical glycosylation of the 2-(4′-hydroxyphenyl)benzofuran aglycon (a.k.a. Eupomatenoid-6). Glycosylation of the phenol by glycosyl bromides under basic conditions afforded the desired products in the gluco-, galacto-, and fuco-series. This approach failed in the manno- and rhamno-series. However, mannosylation and rhamnosylation of Eupomatenoid-6 could be obtained under carefully controlled acidic conditions, using O-benzoxazolyl imidate (OBox) donors. The glycosides obtained are currently under investigation as modulators of Hsp90 chaperone activity.