93413-05-9

Usage

Uses

Used in Pharmaceutical Industry:
Asperlicin E is used as a cholecystokinin antagonist for its potential role in treating conditions related to gastrointestinal motility and satiety regulation. Its antagonistic properties may help in managing obesity and other eating disorders by modulating the release of cholecystokinin, a hormone that signals feelings of fullness after eating.

Upstream product

• 93413-06-0 asperlicin C 
• 118-92-3 anthranilic acid 
• 13139-14-5 Boc-Trp-OH 
• 93413-06-0 (7S)-6,7-dihydro-7-(1H-indol-3-ylmethyl)quinazolino[3,2-a][1,4]benzodiazepine-5,13-dione 
• 73-22-3 L-Tryptophan 
• 118-48-9 isatoic anhydride 
• 101409-14-7 (S)-3-[(1H-indol-3-yl)methyl]-3,4-dihydro-1H-benzo[1,4]diazepine-2,5-dione 

Relevant academic research and scientific papers

Procedure - Economical enantioselective total syntheses of asperlicins C and e

We report a procedure - economical method for the highly enantioselective and protecting-group free total syntheses of nonpeptidal CCK antagonists asperlicins C and E. Starting from l-tryptophan, the synthesis of asperlicin C has been achieved in three steps, which features the low-valent titanium (LVT: TiCl4-Zn combination)-mediated reductive cyclization of o-nitrobenzamide to construct the (3H)-quinazolin-4-one moiety. This is the first employment of LVT for the synthesis of asperlicin C, which allowed accessing asperlicin C in >99% enantioselectivity. Asperlicin C was converted, in one-pot, into asperlicin E and 2,3-di-epi-asperlicin E by dimethyl dioxirane (DMDO)-mediated tandem reactions. The use of DMDO as a green, cheap, and easily available oxidant to replace the photochemical method renders the synthesis of asperlicin E experimentally convenient.

Assembly of asperlicin peptidyl alkaloids from anthranilate and tryptophan: A two-enzyme pathway generates heptacyclic scaffold complexity in asperlicin E

Members of the asperlicin family of fungal metabolites produced by Aspergillus alliaceus are known potent CCKA antagonists. Herein, we report the identification of the gene cluster responsible for directing their biosynthesis. We validate and probe the pathway by genetic manipulation, and provide the first biochemical characterization of the oxidative cyclization en route to the heptacyclic asperlicin E by reconstituting the activity of the FAD depend monooxygenase AspB. This report provides the first genetic characterization of a NRPS assembly line that efficiently activates two anthranilate building blocks and illustrates the remarkably efficient biosynthesis of the complex heptacyclic asperlicin E.