80091-07-2

Upstream product

• 105-53-3 diethyl malonate 
• 103-63-9 1-phenyl-2-bromoethane 

Downstream Products

• 27356-87-2 ethyl 2-phenethylpropenoate 
• 1316742-39-8 2-(RS)-{2-[(1H-indole-2-carbonyl)-amino]phenylcarbamoyl}-4-phenylbutyric acid ethyl ester 
• 1316742-01-4 2-(RS)-{2-[(1H-indole-2-carbonyl)amino]phenylcarbamoyl}-4-phenylbutyric acid 

Relevant academic research and scientific papers

New anthranilic acid based antagonists with high affinity and selectivity for the human cholecystokinin receptor 1 (hCCK1-R)

The anthranilic acid diamides represent the most recent class of nonpeptide CCK1 receptor (CCK1-R) antagonists. Herein we describe the second phase of the anthranilic acid C-terminal optimization using nonproteinogenic amino acids containing a phenyl ring in their side chain. The Homo-Phe derivative 2 (VL-0797) enhanced 12-fold the affinity for the rat CCK1-R affinity and 15-fold for the human CCK1-R relative to the reference compound 12 (VL-0395). The eutomer of 2 (6) exhibited a nanomolar range affinity toward the human CCK1-R and was at least 400-fold selective for the CCK1-R over the CCK2-R. Molecular docking in the modeled CCK1-R and its validation by site-directed mutagenesis experiments showed that the 6 binding site overlaps that occupied by the C-terminal bioactive region of the natural agonist CCK. Owing to their interesting properties, new compounds provided by this study represent a solid basis for further advances aimed at synthesis of clinically valuable CCK1-R antagonists.

Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: A structure-activity study

Several phosphinic pseudo-tripeptides of general formula R-XaaΨ(PO2- CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.

BENZAZEPINE-, BENZOXAZEPINE- AND BENZOTHIAZEPINE-N-ACETIC ACID DERIVATIVES, PROCESS FOR THEIR PREPARATION AND PHARMACEUTICAL COMPOSITIONS CONTAINING THEM

Compounds with neutral endopeptidase (NEP) inhibitory activity corresponding to the formula I STR1 in which R 1 is a lower alkoxy-lower-alkyl group whose lower alkoxy radical is substituted by a lower alkoxy group, or a phenyl-lower-alkyl or phenyloxy-lower-alkyl group which can optionally be substituted in the phenyl ring by lower alkyl, lower alkoxy or halogen, or a naphthyl-lower-alkyl group, A is CH 2, O or S,R 2 is hydrogen or halogen,R. sup.3 is hydrogen or halogen,R 4 is hydrogen or a group forming a biolabile ester, andR 5 is hydrogen or a group forming a biolabile ester, and the physiologically acceptable acid addition salts thereof.