164172-95-6

Usage

Uses

Used in Pharmaceutical Development:
(R)-2-AMINO-3-BIPHENYL-3-YL-PROPIONIC ACID is used as a building block in the synthesis of various pharmaceuticals for its potential to contribute to the development of new drugs with anti-inflammatory and analgesic properties. Its unique structure allows it to be a key component in the creation of molecules that can target specific biological pathways.
Used in Agrochemical Synthesis:
In the agrochemical industry, (R)-2-AMINO-3-BIPHENYL-3-YL-PROPIONIC ACID is utilized as a reference standard and a synthetic precursor for the development of new agrochemicals, potentially enhancing crop protection and yield through targeted pest and disease control.
Used in Materials Science:
(R)-2-AMINO-3-BIPHENYL-3-YL-PROPIONIC ACID is employed in materials science for its potential to be integrated into the design and synthesis of new materials with specific properties, such as improved stability or reactivity, which can be beneficial in various industrial applications.
Used in Chemical Research:
As a reference standard, (R)-2-AMINO-3-BIPHENYL-3-YL-PROPIONIC ACID is used in chemical research to validate and calibrate analytical methods, ensuring the accuracy of experimental results and contributing to the advancement of chemical knowledge and techniques.

Upstream product

• 82311-69-1 (S)-2-amino-3-(3-bromophenyl)propanoic acid 
• 98-80-6 phenylboronic acid 
• 14704-31-5 3-(bromomethyl)-1,1'-biphenyl 
• 643-93-6 3-methylbiphenyl 
• 1027167-32-3 1,1-dimethylethyl (2S)-trans-5-(<1,1'-biphenyl>-3-ylmethyl)-2-(1,1-dimethylethyl)-3-methyl-4-oxo-1-imidazolidinecarboxylate 

Downstream Products

• 199110-64-0 (S)-3-biphenyl-4-yl-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionic acid 

Relevant academic research and scientific papers

Constraining the Side Chain of C-Terminal Amino Acids in Apelin-13 Greatly Increases Affinity, Modulates Signaling, and Improves the Pharmacokinetic Profile

Side-chain-constrained amino acids are useful tools to modulate the biological properties of peptides. In this study, we applied side-chain constraints to apelin-13 (Ape13) by substituting the Pro12 and Phe13 positions, affecting the binding affinity and signaling profile on the apelin receptor (APJ). The residues 1Nal, Trp, and Aia were found to be beneficial substitutions for Pro12, and the resulting analogues displayed high affinity for APJ (Ki 0.08-0.18 nM vs Ape13 Ki 0.7 nM). Besides, constrained (d-Tic) or α,α-disubstituted residues (Dbzg; d-α-Me-Tyr(OBn)) were favorable for the Phe13 position. Compounds 47 (Pro12-Phe13 replaced by Aia-Phe, Ki 0.08 nM) and 53 (Pro12-Phe13 replaced by 1Nal-Dbzg, Ki 0.08 nM) are the most potent Ape13 analogues activating the Gα12 pathways (53, EC50 Gα12 2.8 nM vs Ape13, EC50 43 nM) known to date, displaying high affinity, resistance to ACE2 cleavage as well as improved pharmacokinetics in vitro (t1/2 5.8-7.3 h in rat plasma) and in vivo.

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.

Potent, Orally Active, Competitive N-Methyl-D-aspartate (NMDA) Receptor Antagonists Are Substrates for a Neutral Amino Acid Uptake System in Chinese Hamster Ovary Cells

A series of enantiomerically pure (phosphonomethyl)-substituted phenylalanine derivatives related to SDZ EAB 515 (1) were prepared as competitive N-methyl-D-aspartate (NMDA) receptor antagonists.Unlike most known competitive NMDA antagonists, analogs in this series with the S-configuration are potent NMDA antagonists whereas analogs with the unnatural R-configuration are weak NMDA antagonists, as determined by receptor binding experiments and their anticonvulsant action in mice.Examination in a previously reported competitive NMDA pharmacophore model revealed that receptor affinity can be explained partially by a cavity that accommodates the biphenyl ring of 1, while the biphenyl ring of the R-enantiomer 2 extends into a disallowed steric region.We proposed that analogs with the natural S-configuration and a large hydrophobic moiety would have an advantage in vivo over analogs with an R-configuration by being able to use a neutral amino acid uptake system to enhance both peripheral adsorption and transport into the brain.Examination in a system L neutral amino acid transport carrier assay shows that 1 competes with L-Phe for transport in an apparent competitive and stereospecific manner (estimated Ki=50 μM).The 1- and 2-naphthyl derivatives 3a,3b were found to be among the most potent, competitive NMDA antagonists yet discovered, being ca. 15-fold more potent than 1 in vitro and in vivo, with a long duration of action.The title compound 3a had potent oral activity in MES (ED50=5.0 mg/kg). 3a also retains its ability to compete, albeit more weakly than 1 (estimated Ki=200 μM), for L-Phe uptake to CHO cells.In this series, analogs with the R-configuration are not substrates for the system L neutral amino acid transport carrier.These results provide evidence that central nervous system active agents can be designed as substrates of a neutral amino acid transporter as a means to enhance penetration of the blood-brain barrier.