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Usage

Uses

Used in Pharmaceutical Synthesis:
Methyl L-2-(4-fluorophenyl)glycinate HCl is used as a building block for the synthesis of various pharmaceuticals and organic compounds. Its structural components make it a versatile component in the creation of new molecules with potential therapeutic applications.
Used in Drug Development:
In the pharmaceutical industry, Methyl L-2-(4-fluorophenyl)glycinate HCl is utilized as a precursor in the development of new drugs and treatment methods. Methyl L-2-(4-fluorophenyl)glycinate HCl's unique structure, including the fluorophenyl group, suggests it may interact with specific biological targets, offering avenues for the discovery of novel therapeutic agents.
Used in Research and Development:
Methyl L-2-(4-fluorophenyl)glycinate HCl is also used in research settings to explore its potential interactions with biological systems. The presence of the fluorine atom in the phenyl ring can influence the compound's reactivity, selectivity, and binding affinity, making it a valuable tool for probing and understanding molecular interactions in drug discovery processes.

Upstream product

• 67-56-1 methanol 
• 19883-57-9 (S)-2-amino-2-(4-fluorophenyl)acetic acid 
• 185994-15-4 (S)-α-amino-α-(4-fluorophenyl)acetic acid hydrochloride 

Downstream Products

• 1587732-42-0 (S)-2-amino-2-(4-fluorophenyl)acetohydrazide 
• 888028-36-2 (1S)-1-amino-1-(4-fluorophenyl)-2-methylpropan-2-ol 
• 1456506-65-2 (S)-methyl 2-((4-((tert-butoxycarbonyl)amino)cyclohexyl)amino)-2-(4-fluorophenyl)acetate 

Relevant academic research and scientific papers

((S)-3-Mercapto-2-methylpropanamido)acetic acid derivatives as metallo-β-lactamase inhibitors: Synthesis, kinetic and crystallographic studies

The emergence and global spread of metallo-β-lactamase (MBL) mediated resistance to almost all β-lactam antibacterials poses a serious threat to public health. Since no clinically useful MBL inhibitors have been reported, there is an urgent need to develop new potent broad-spectrum MBL inhibitors effective against antibacterial resistance. Herein, we synthesized a set of 2-substituted ((S)-3-mercapto-2-methylpropanamido) acetic acid derivatives, some of which displayed potent inhibition with high ligand efficiency to the clinically relevant MBL subtypes, Verona Integron-encoded MBL (VIM)-2 and New Delhi MBL (NDM)-1. Kinetic studies revealed that the inhibitors are not strong zinc chelators in solution, and they bind reversibly to VIM-2 but dissociate very slowly. Crystallographic analyses revealed that they inhibit VIM-2 via chelating the active site zinc ions and interacting with catalytically important residues. Further cell- and zebrafish-based assays revealed that the inhibitors slightly increase susceptibility of E. coli cells expressing VIM-2 to meropenem, and they have no apparent toxicity to the viability of HEK293T cells and the zebrafish embryogenesis.

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.