6331-95-9

Usage

Uses

Used in Organic Synthesis:
(1,3-dioxo-3,3a,7,7a-tetrahydro-4,7-epoxy-2-benzofuran-4(1H)-yl)methyl acetate is used as a building block in organic synthesis for the creation of complex organic molecules. Its structural components, including the tetrahydrofuran ring and epoxy group, allow for further reactions and modifications, making it a versatile component in the synthesis of various organic compounds.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, (1,3-dioxo-3,3a,7,7a-tetrahydro-4,7-epoxy-2-benzofuran-4(1H)-yl)methyl acetate is used as a starting material or intermediate in the development of new pharmaceuticals. Its potential biological and pharmacological activities, combined with its reactivity, make it a candidate for the synthesis of bioactive molecules with therapeutic applications.
Used in Drug Discovery and Development:
(1,3-dioxo-3,3a,7,7a-tetrahydro-4,7-epoxy-2-benzofuran-4(1H)-yl)methyl acetate is utilized in drug discovery and development processes to explore its potential as a lead compound or to enhance the properties of existing drug candidates. Its unique structure may offer novel mechanisms of action or improved pharmacokinetic profiles, contributing to the advancement of new therapeutic agents.
Used in the Production of Specialty Chemicals:
(1,3-dioxo-3,3a,7,7a-tetrahydro-4,7-epoxy-2-benzofuran-4(1H)-yl)methyl acetate also finds application in the production of specialty chemicals, where its specific structural features are exploited to create high-value chemical products for various industries, such as agriculture, materials science, and fragrances.

Upstream product

• 108-31-6 maleic anhydride 
• 623-17-6 furfurylacetate 
• 98-00-0 (2-furyl)methyl alcohol 

Downstream Products

• 15573-98-5 1-acetoxymethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic anhydride 

Relevant academic research and scientific papers

7-Oxanorbornane and norbornane mimics of a distorted β-D- mannopyranoside: Synthesis and evaluation as β-mannosidase inhibitors

The racemic 7-oxanorbornanyl and norbornanyl aminoalcohols 3, 4, 42, 45, and 46 were synthesized and tested as snail β-mannosidase inhibitors. The amino tetraol 3 was obtained from the known sulfonyl acrylate 9 and furan 10. Esterification provided 11 tha

Structure-based design of a highly selective catalytic site-directed inhibitor of Ser/Thr protein phosphatase 2B (calcineurin)

Protein serine/threonine phosphatases (PP1, PP2A and PP2B) play important roles in intracellular signal transductions. The immunosuppressant drugs FK506 and cyclosporin A (CsA) bind to immunophilins, and these complexes selectively inhibit PP2B (calcineurin), leading to the suppression of T-cell proliferation. Both FK506 and CsA must, however, form complexes with immunophilins to exert their inhibitory action on PP2B. Thus, it is of interest to find a direct and selective inhibitor of PP2B that does not involve the immunophilins as a biological tool for studies of PP2B and also as a candidate therapeutic agent. We selected the simple natural product cantharidin, a known PP2A-selective inhibitor, as a lead compound for this project. Primary SAR indicated that norcantharidin (7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic anhydride) inhibits not only PP1 and PP2A but also PP2B, and a binding model of norcantharidin carboxylate to the PP2B catalytic site was computationally constructed. Based on this binding model, we designed and synthesized several cantharidin derivatives. Among these compounds, 1,5-dibenzoyloxymethyl-substituted norcantharidin was found to inhibit PP2B without inhibiting PP1 or PP2A. To our knowledge, this is the first highly selective catalytic site-directed inhibitor of PP2B.

Structure-activity relationship of cantharidin derivatives to protein phosphatases 1, 2A1, and 2B

The effects of structural modification of cantharidin on the inhibition of protein Ser/Thr phosphatases are described. Removal of the methyl substituents at C2 and C3 in cantharidin improved the inhibition of PP2B. In contrast, introduction of a substituent to C1/C4-position drastically decreased inhibition of PP1 and PP2A1. PP2B was found to be quite tolerant to modifications at the C5 position.