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Usage

Uses

Used in Pharmaceutical Industry:
(S)-1-(2-aminoacetyl)-4,4-difluoropyrrolidine-2-carbonitrile 4-methylbenzenesulfonic acid is used as a potential drug candidate for its ability to interact with biological systems due to the presence of the aminoacetyl group. This interaction may lead to the development of pharmaceutical agents targeting specific diseases or conditions.
Used in Chemical Research:
In the field of chemical research, (S)-1-(2-aminoacetyl)-4,4-difluoropyrrolidine-2-carbonitrile 4-methylbenzenesulfonic acid is used as a subject of study for its unique difluoropyrrolidine moiety. This component may provide interesting chemical and biological properties that could inspire further research and potential applications in various scientific fields.

Upstream product

• 74844-91-0 1-tert-butyl 2-methyl (2S,4R)-4-hydroxy-1,2-pyrrolidinedicarboxylate 
• 203866-17-5 1-tert-butyl 2-methyl (2S)-4,4-difluoropyrrolidine-1,2-dicarboxylate 
• 203866-15-3 1-(tert-butoxycarbonyl)-4,4-difluoro-L-proline 
• 102195-80-2 (S)-1-tert-butyl 2-methyl 4-oxopyrrolidine-1,2-dicarboxylate 
• 1448440-50-3 tert-butyl (S)-(2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)carbamate 
• 104-15-4 toluene-4-sulfonic acid 
• 1448440-48-9 (S)-tert-butyl 2-(2-carbamoyl-4,4-difluoropyrrolidin-1-yl)-2-oxoethylcarbamate 
• 1448440-46-7 (S)-4,4-difluoropyrrolidine-2-carboxamide trifluoroacetic acid 
• 426844-50-0 (S)-2-carbamoyl-4,4-difluoropyrrolidine-1-carboxylic acid tert-butyl ester 

Relevant academic research and scientific papers

Extended structure-activity relationship and pharmacokinetic investigation of (4-quinolinoyl)glycyl-2-cyanopyrrolidine inhibitors of fibroblast activation protein (FAP)

Fibroblast activation protein (FAP) is a serine protease related to dipeptidyl peptidase IV (DPPIV). It has been convincingly linked to multiple disease states involving remodeling of the extracellular matrix. FAP inhibition is investigated as a therapeutic option for several of these diseases, with most attention so far devoted to oncology applications. We previously discovered the N-4-quinolinoyl-Gly-(2S)-cyanoPro scaffold as a possible entry to highly potent and selective FAP inhibitors. In the present study, we explore in detail the structure-activity relationship around this core scaffold. We report extensively optimized compounds that display low nanomolar inhibitory potency and high selectivity against the related dipeptidyl peptidases (DPPs) DPPIV, DPP9, DPPII, and prolyl oligopeptidase (PREP) the log D values, plasma stabilities, and microsomal stabilities of selected compounds were found to be highly satisfactory. Pharmacokinetic evaluation in mice of selected inhibitors demonstrated high oral bioavailability, plasma half-life, and the potential to selectively and completely inhibit FAP in vivo.