185994-15-4

Usage

Uses

Used in Pharmaceutical Industry:
(S)-AMINO-(4-FLUORO-PHENYL)-ACETIC ACID HYDROCHLORIDE is used as an intermediate in the synthesis of pharmaceutical compounds for its unique structural features, including the 4-fluoro-phenyl group and the amino-acetic acid backbone.
Used in Organic Synthesis:
In the field of organic synthesis, (S)-AMINO-(4-FLUORO-PHENYL)-ACETIC ACID HYDROCHLORIDE serves as a building block for the creation of more complex organic molecules, taking advantage of its reactive functional groups and the presence of the fluorine atom for further chemical transformations.
Used in Research:
(S)-AMINO-(4-FLUORO-PHENYL)-ACETIC ACID HYDROCHLORIDE is utilized in research settings to study the effects of structural modifications on the properties and reactivity of chemical compounds, particularly in the context of medicinal chemistry and drug discovery.

Upstream product

• 1313219-23-6 (S,S)-α-(4-fluorophenyl)-α-[1-(4-methoxyphenyl)ethylamino]acetonitrile hydrochloride 
• 459-57-4 4-fluorobenzaldehyde 

Downstream Products

• 916602-09-0 (S)-methyl 2-amino-2-(4-fluorophenyl)acetate hydrochloride 
• 1587732-42-0 (S)-2-amino-2-(4-fluorophenyl)acetohydrazide 

Relevant academic research and scientific papers

Structure-based design of inhibitors of the aspartic protease endothiapepsin by exploiting dynamic combinatorial chemistry

Structure-based design (SBD) can be used for the design and/or optimization of new inhibitors for a biological target. Whereas de novo SBD is rarely used, most reports on SBD are dealing with the optimization of an initial hit. Dynamic combinatorial chemistry (DCC) has emerged as a powerful strategy to identify bioactive ligands given that it enables the target to direct the synthesis of its strongest binder. We have designed a library of potential inhibitors (acylhydrazones) generated from five aldehydes and five hydrazides and used DCC to identify the best binder(s). After addition of the aspartic protease endothiapepsin, we characterized the protein-bound library member(s) by saturation-transfer difference NMR spectroscopy. Cocrystallization experiments validated the predicted binding mode of the two most potent inhibitors, thus demonstrating that the combination of de novo SBD and DCC constitutes an efficient starting point for hit identification and optimization. The dynamic duo: The combination of de novo structure-based design and dynamic combinatorial chemistry has been applied to the identification of novel acylhydrazone-based inhibitors for the aspartic protease endothiapepsin. 1H-STD-NMR spectroscopy has been used to identify the binders from the dynamic combinatorial libraries. Proposed binding modes of the most potent inhibitors have been confirmed by X-ray crystallography.

Asymmetric strecker synthesis of α-arylglycines

A practically simple three-component Strecker reaction for the asymmetric synthesis of enantiopure α-arylglycines has been developed. Addition of a range of aryl-aldehydes to a solution of sodium cyanide and (S)-1-(4- methoxyphenyl)ethylamine affords highly crystalline (S,S)-α-aminonitriles that are easily obtained in diastereomerically pure form. Heating the resultant (S,S)-α-aminonitriles in 6 M aqueous HCl at reflux resulted in cleavage of their chiral auxiliary fragments and concomitant hydrolysis of their nitrile groups to afford enantiopure (S)-α-arylglycines. The enantiopurities of these (S)-α-arylglycines were determined via derivatization of their corresponding methyl esters with 2-formylphenylboronic acid and (S)-BINOL, followed by 1H NMR spectroscopic analysis of the resultant mixtures of diastereomeric iminoboronate esters.