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
• Article Data: 7

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

L-4,4''-Biphenylalanine is a useful reagent in the preparation of other biologically active small molecules.

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

• 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 
• 63024-30-6 (S)-2-amino-3-(biphenyl-4-yl)-propionic acid methyl ester hydrochloride 
• 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.

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.

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.