155760-02-4

Basic information

• Product Name: L-4,4'-BIPHENYLALANINE
• Synonyms: (S)-4-BIPHENYL-ALANINE;(S)-4-BIPHENYLYL-ALANINE;(S)-2-AMINO-3-BIPHENYL-4-YL-PROPIONIC ACID;(S)-2-AMINO-3-(1,1'-BIPHENY-4-YL)PROPANOIC ACID;H-4-PHENYL-L-PHE-OH;H-4-PHENYL-PHE-OH;H-BIP(4,4')-OH;H-BIP-OH
• CAS NO: 155760-02-4
• Molecular Formula: C₁₅H₁₅NO₂
• Molecular Weight: 241.29
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Chiral Compound;a-amino
• Mol File: 155760-02-4.mol

Chemical Properties

• Boiling Point: 428.6 °C at 760 mmHg
• Flash Point: 213 °C
• Appearance: White fine crystals
• Density: 1.19 g/cm³
• Vapor Pressure: 8.52E-14mmHg at 25°C
• Refractive Index: 1.631
• Storage Temp.: Store at RT.
• Solubility: Acidic DMSO (Slightly)
• PKA: 2.21±0.10(Predicted)
• Stability: Hygroscopic
• CAS DataBase Reference: L-4,4'-BIPHENYLALANINE(CAS DataBase Reference)
• NIST Chemistry Reference: L-4,4'-BIPHENYLALANINE(155760-02-4)
• EPA Substance Registry System: L-4,4'-BIPHENYLALANINE(155760-02-4)

Safety Data

• Hazard Codes: Xi
• Hazardous Substances Data: 155760-02-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
L-4,4'-BIPHENYLALANINE is used as a building block for the synthesis of various biologically active small molecules, such as peptides, peptidomimetics, and other bioactive compounds. Its unique structural properties allow for the development of novel therapeutic agents with potential applications in the treatment of various diseases and conditions.
Used in Chemical Research:
L-4,4'-BIPHENYLALANINE serves as a valuable reagent in chemical research, particularly in the field of organic synthesis. Its distinct structural features make it an attractive candidate for the development of new synthetic methods and strategies, as well as for the exploration of its potential as a chiral auxiliary or ligand in asymmetric catalysis.
Used in Material Science:
The unique structural properties of L-4,4'-BIPHENYLALANINE also make it a promising candidate for the development of novel materials with specific properties, such as optoelectronic materials, sensors, or self-assembling systems. Its incorporation into polymers or other materials could lead to the creation of new materials with enhanced performance characteristics.

InChI:InChI=1/C18H20N2O4/c19-15(17(21)22)9-11-1-5-13(6-2-11)14-7-3-12(4-8-14)10-16(20)18(23)24/h1-8,15-16H,9-10,19-20H2,(H,21,22)(H,23,24)/t15-,16-/m0/s1

Upstream product

• 198561-04-5 Fmoc-4-bromo-L-phenylalanine 
• 199110-64-0 (S)-3-biphenyl-4-yl-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionic acid 
• 24250-84-8 H-p-BrPhe-OH 
• 76985-08-5 α-amino-(1,1'-biphenyl)-4-propanoic acid 
• 13026-23-8 (2E)-3-(1,1'-biphenyl-4-yl)acrylic acid 
• 98-80-6 phenylboronic acid 
• 119273-61-9 N-tert-butoxycarbonyl-p-phenyl-L-phenylalanine 
• 62129-39-9 4-bromo-N-{[(1,1-dimethylethyl)oxy]carbonyl}-L-phenylalanine 
• 1432516-20-5 C₂₉H₃₄N₄O₄ 

Downstream Products

• 63024-30-6 (S)-2-amino-3-(biphenyl-4-yl)-propionic acid methyl ester hydrochloride 
• 270568-72-4 2-benzyloxycarbonylamino-3-biphenyl-4-ylpropionic acid 
• 119273-61-9 N-tert-butoxycarbonyl-p-phenyl-L-phenylalanine 
• 225528-25-6 tert-butyl (2S)-2-amino-3-(4-phenylphenyl)propanoate 
• 139040-51-0 methyl (S)-2-amino-3-(biphenyl-4-yl)propanoate 

Relevant articles and documents

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.

Drug Design Inspired by Nature: Crystallographic Detection of an Auto-Tailored Protease Inhibitor Template

De novo drug discovery is still a challenge in the search for potent and selective modulators of therapeutically relevant target proteins. Here, we disclose the unexpected discovery of a peptidic ligand 1 by X-ray crystallography, which was auto-tailored by the therapeutic target MMP-13 through partial self-degradation and subsequent structure-based optimization to a highly potent and selective β-sheet peptidomimetic inhibitor derived from the endogenous tissue inhibitors of metalloproteinases (TIMPs). The incorporation of non-proteinogenic amino acids in combination with a cyclization strategy proved to be key for the de novo design of TIMP peptidomimetics. The optimized cyclic peptide 4 (ZHAWOC7726) is membrane permeable with an IC50 of 21 nm for MMP-13 and an attractive selectivity profile with respect to a polypharmacology approach including the anticancer targets MMP-2 (IC50: 170 nm) and MMP-9 (IC50: 140 nm).

Tailored Mutants of Phenylalanine Ammonia-Lyase from Petroselinum crispum for the Synthesis of Bulky l- and d-Arylalanines

Tailored mutants of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) were created and tested in ammonia elimination from various sterically demanding, non-natural analogues of phenylalanine and in ammonia addition reactions into the corresponding (E)-arylacrylates. The wild-type PcPAL was inert or exhibited quite poor conversions in both reactions with all members of the substrate panel. Appropriate single mutations of residue F137 and the highly conserved residue I460 resulted in PcPAL variants that were active in ammonia elimination but still had a poor activity in ammonia addition onto bulky substrates. However, combined mutations that involve I460 besides the well-studied F137 led to mutants that exhibited activity in ammonia addition as well. The synergistic multiple mutations resulted in substantial substrate scope extension of PcPAL and opened up new biocatalytic routes for the synthesis of both enantiomers of valuable phenylalanine analogues, such as (4-methoxyphenyl)-, (napthalen-2-yl)-, ([1,1′-biphenyl]-4-yl)-, (4′-fluoro-[1,1′-biphenyl]-4-yl)-, and (5-phenylthiophene-2-yl)alanines.

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.

Design, synthesis, and bioevaluation of viral 3C and 3C-like protease inhibitors

A class of tripeptidyl transition state inhibitors containing a P1 glutamine surrogate, a P2 leucine, and a P3 arylalanines, was found to potently inhibit Norwalk virus replication in enzyme and cell based assays. An array of warheads, including aldehyde, α-ketoamide, bisulfite adduct, and α-hydroxyphosphonate transition state mimic, was also investigated. Tripeptidyls 2 and 6 possess antiviral activities against noroviruses, human rhinovirus, severe acute respiratory syndrome coronavirus, and coronavirus 229E, suggesting a broad range of antiviral activities.

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.

Nonapeptide and decapeptide analogs of LHRH, useful as LHRH antagonists

Nonapeptide and decapeptide analogs of LHRH which have the formula: STR1 and the pharmaceutically acceptable salts thereof, wherein: X is a D-alanyl residue wherein one hydrogen on C-3 is replaced by:(a) a carbocyclic aryl-containing radical selected from the group consisting of phenyl substituted with three or more straight chain lower alkyl groups, naphthyl, anthryl, fluorenyl, phenanthryl, biphenylyl and benzhydryl; or(b) a saturated carbocyclic radical selected from the group consisting of cyclohexyl substituted with three or more straight chain lower alkyl groups, perhydronaphthyl, perhydrobiphenylyl, perhydro-2,2-diphenylmethyl, and adamantyl; or(c) a heterocyclic aryl containing radical selected from the group consisting of radicals represented by the following structural formulas: STR2 wherein A"" and A'' are independently selected from the group consisting of hydrogen, lower alkyl, chlorine, and bromine, and G is selected from the group consisting of oxygen, nitrogen, and sulfur;A is an aminoacyl residue selected from the group consisting of L-pyroglutamyl, D-pyroglutamyl, N-acyl-L-prolyl, N-acyl-D-prolyl, N-acyl-D-tryptophanyl, N-acyl-D-phenylalanyl, N-acyl-D-p-halophenylalanyl, and N-acyl-X wherein X is as defined previously;B is an amino acyl residue selected from the group consisting of D-phenylalanyl, D-p-halophenylalanyl, 2,2-diphenylglycyl, and X wherein X is as defined previously;C is an amino acyl residue selected from the group consisting of L-tryptophanyl, D-tryptophanyl, D-phenylalanyl and X wherein X is as defined above;E is glycinamide or --NH--R 1, wherein R 1 is lower alkyl, cycloalkyl, fluoro lower alkyl or STR3 wherein R 2 is hydrogen or lower alkyl; are disclosed. These compounds are LHRH antagonists.