758685-64-2

Usage

Uses

Used in Pharmaceutical Industry:
L-2-AMINO-3-(3'-METHYL-BIPHENYL-4-YL)-PROPIONIC ACID is used as a key intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows for the development of drugs with specific therapeutic properties, making it a valuable asset in drug discovery and design.
Used in Biotechnology Industry:
In the biotechnology sector, L-2-AMINO-3-(3'-METHYL-BIPHENYL-4-YL)-PROPIONIC ACID serves as a potential starting material for the production of bioactive peptides and proteins. Its incorporation into these biomolecules can lead to the creation of novel therapeutic agents with targeted functions.
Used in Neurotransmitter Function Research:
L-2-AMINO-3-(3'-METHYL-BIPHENYL-4-YL)-PROPIONIC ACID is used as a research tool in the study of neurotransmitter function. Its structural similarity to phenylalanine allows scientists to investigate its interactions with neurotransmitter systems and explore its potential role in modulating neurotransmission.
Used in Neurodegenerative Disease Treatment:
Due to its potential impact on neurotransmitter function, L-2-AMINO-3-(3'-METHYL-BIPHENYL-4-YL)-PROPIONIC ACID is being studied for its potential therapeutic applications in the treatment of neurodegenerative diseases. Its ability to modulate neurotransmitter systems may offer new avenues for the development of treatments for conditions such as Alzheimer's disease, Parkinson's disease, and other related disorders.

Upstream product

• 24250-84-8 H-p-BrPhe-OH 
• 16419-60-6 2-Methylphenylboronic acid 
• 1432516-24-9 C₃₀H₃₆N₄O₄ 

Relevant academic research and scientific papers

Suzuki-Miyaura Diversification of Amino Acids and Dipeptides in Aqueous Media

The Suzuki-Miyaura derivatisation of free amino acids, peptides and proteins is an attractive area with considerable potential utility for medicinal chemistry and chemical biology. Here we report the modification of unprotected and Boc-protected aromatic amino acids and dipeptides in aqueous media, enabling heteroarylation and vinylation. We systematically investigate the impact of the peptide backbone and adjacent amino acid residues upon the reaction. Our studies reveal that although asparagine and histidine hinder the reaction, by utilising dppf, a ferrocene-based bidentate phosphine ligand, cross coupling of halophenylalanine or halotryptophan adjacent to such a residue could be enabled. Our studies reveal dppf to have good compatibility with all unprotected, proteinogenic amino acid side chains.

Identification of new peptide amides as selective cathepsin L inhibitors: The first step towards selective irreversible inhibitors?

A small library of peptide amides was designed to profile the cathepsin L active site. Within the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L and cathepsin B, and then selected hits were further evaluated for binding to cathepsin K and cathepsin S. Five highly selective sequences with submicromolar affinities towards cathepsin L were identified. An acyloxymethyl ketone warhead was then attached to these sequences. Although these original irreversible inhibitors inactivate cathepsin L, it appears that the nature of the warhead drastically impact the selectivity profile of the resulting covalent inhibitors.