112052-43-4

Upstream product

• 14565-11-8 methyl 7-hydroxyheptanoate 
• 98-59-9 p-toluenesulfonyl chloride 
• 502-42-1 cycloheptanone 
• 539-87-7 oxocan-2-one 
• 20257-95-8 8-hydroxyoctanoic acid methyl ester 

Downstream Products

• 89790-31-8 8-(4-Cyanomethyl-phenoxy)-octanoic acid methyl ester 
• 89790-19-2 p-(7-carbamoylheptamethylenoxy)phenylacetamide 
• 89790-21-6 8-(4-Carbamoylmethyl-phenoxy)-octanoic acid amide 
• 89790-20-5 8-(4-Carbamoylmethyl-phenoxy)-octanoic acid methyl ester 

Relevant academic research and scientific papers

PEGylated Poly-HDACi: A Designer Polyprodrug from Optimized Drug Units**

We designed, synthesized, and characterized a tri-block copolymer. Its hydrophobic part, a chain of histone deacetylase inhibitor (HDACi) prodrug, was symmetrically flanked by two identical PEG blocks, whereas the built-in HDACi was a linear molecule, terminated with a thiol at one end, and a hydroxyl group at the other. Such a feature facilitated end-to-end linkage of prodrugs through alternatively aligned disulfides and carbonates. The disulfides served dual roles: redox sensors of smart nanomedicine, and warheads of masked HDACi drugs. This approach, carefully designed to benefit both control-release and efficacy, is conceptually novel for optimizing drug units in nanomedicine. Micelles from this designer polyprodrug released only PEG, CO2 and HDACi, and synergized with DOX against HCT116 cells, demonstrating its widespread potential in combination therapy. Our work highlights, for the first time, the unique advantage of thiol-based drug molecules in nanomedicine design.

Design of Inhibitors from the Three-Dimensional Structure of Alcohol Dehydrogenase. Chemical Synthesis and Enzymatic Properties

Inhibitors of liver alcohol dehydrogenase were designed from the three-dimensional structure of the enzyme.The ligand to the catalytic zinc ion is an amide group or, better, a formamide group.With the latter function, a hydrogen bond between the NH group and the hydroxyl group of Ser-48 may be formed.The hydrophobic substrate binding site brings structural restraints. α-ω bifunctional molecules show good inhibitory properties possibly due to the interactions with polar residues at the entrance of the substrate binding site.