95753-56-3

Basic information

• Product Name: Fmoc-4-Amino-L-phenylalanine
• Synonyms: FMOC-L-PHE(4-NH2)-OH;FMOC-PHE(4-NH2)-OH;FMOC-P-AMINO-L-PHE-OH;FMOC-P-AMINO-PHENYLALANINE;FMOC-P-AMINO-PHE-OH;FMOC-PHE(P-NH2)-OH;FMOC-S-PHE(4-NH2)-OH;FMOC-L-4-AMINOPHENYLALANINE
• CAS NO: 95753-56-3
• Molecular Formula: C₂₄H₂₂N₂O₄
• Molecular Weight: 402.44
• EINECS: 1806241-263-5
• Product Categories: Phenylalanine [Phe, F];Unusual Amino Acids;Fmoc-Amino acid series
• Mol File: 95753-56-3.mol

Chemical Properties

• Boiling Point: 671.5 °C at 760 mmHg
• Flash Point: 359.9 °C
• Appearance: /
• Density: 1.316 g/cm³
• Storage Temp.: -15°C
• PKA: 3.63±0.10(Predicted)
• CAS DataBase Reference: Fmoc-4-Amino-L-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-4-Amino-L-phenylalanine(95753-56-3)
• EPA Substance Registry System: Fmoc-4-Amino-L-phenylalanine(95753-56-3)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 95753-56-3(Hazardous Substances Data)

Usage

InChI:InChI=1/C24H22N2O4/c25-16-11-9-15(10-12-16)13-22(23(27)28)26-24(29)30-14-21-19-7-3-1-5-17(19)18-6-2-4-8-20(18)21/h1-12,21-22H,13-14,25H2,(H,26,29)(H,27,28)/t22-/m0/s1

Upstream product

• 95753-55-2 N-α-FMOC-4-nitro-L-phenylalanine 
• 943-80-6 4-amino-L-phenylalanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 63-91-2 L-phenylalanine 

Downstream Products

• 1141050-60-3 4-[[(2,4,6-trimethylphenyl)sulfonyl]amino]-L-phenylalanine 

Relevant articles and documents

Synthesis of new tetrazolyl derivatives of L- and D-phenylalanine

New tetrazolyl derivatives of L- and D-phenylalanine were synthesized by azidation of n-propyl esters of (2S)- and (2R)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(4-aminophenyl)propionic acids and by a series of subsequent chemical transformations. The structure and individuality of the compounds obtained were confirmed by using a complex of spectral and chromatographic methods.

Incorporation of non-natural amino acids improves cell permeability and potency of specific inhibitors of proteasome trypsin-like sites

Proteasomes degrade the majority of proteins in mammalian cells by a concerted action of three distinct pairs of active sites. The chymotrypsin-like sites are targets of antimyeloma agents bortezomib and carfilzomib. Inhibitors of the trypsin-like site se

N-alkanoylphenylalanine derivatives

Compounds of the formula: are disclosed which have activity as inhibitors of binding between VCAM-1 and cells expressing VLA-4. Such compounds are useful for treating diseases whose symptoms and/or damage are related to the binding of VCAM-1 to cells expressing VLA-4.

N-aroylphenylalanine derivative VCAM-1 inhibitors

Compounds of the formula: are disclosed which have activity as inhibitors of binding between VCAM-1 and cells expressing VLA-4. Such compounds are useful for treating diseases whose symptoms and/or damage are related to the binding of VCAM-1 to cells expr

α,α-difluorophosphonomethyl azobenzene derivatives as photoregulated phosphoamino acid analogs. 1. Design and synthesis

A series of novel, photoregulated phosphoamino acid analogs based on an azobenzene core bearing an α,α-difluoromethylphosphonate as a hydrolytically stable phosphate isostere have been prepared with N-Fmoc protection for use in peptide synthesis. Classes of reagents analogous to both phosphotyrosine and phosphoserine/threonine were prepared by a common route employing a nitrosoarene/aniline condensation to form the azo linkage and the Cu(I)-promoted coupling of an iodoarene with (diethylphosphono)difluoromethyl cadmium bromide (Burton's method) to introduce the phosphonate moiety.

Two novel amino acid derivatives containing side-chain thioamides for the synthesis of photoactivatable peptides

The highly efficient preparation of two optically pure phenylalanine analogues containing p-N-aryl thiobenzamide moieties are described. These amino acids are readily incorporated into peptides via standard solid-phase strategies.

Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

Syntheses of S-peptide analogues bearing phenylazophenylalanine (Pap) residues at positions 4, 8, and 11 are described. Noncovalent reassociation of the Pap-4 and Pap-11 peptides with S-protein reconstitutes ribonuclease activity. Photoisomerization of the Pap-4 peptide is found to modulate the enzyme activity.

CHIRAL ANALYSIS OF THE REACTION STAGES IN THE EDMAN METHOD FOR SEQUENCING PEPTIDES

Chiral isothiocyanate reagents suitable for 'Edman sequencing' have been synthesised and used to assess the chiral features of individual stages in the Edman method.Using h.p.l.c. analysis of the diastereoisomeric thiohydantoins obtained, it has been deduced that the cyclisation and cleavage of thiazolinone step is the likely source of racemisation of the chiral centre derived from the N-terminal amino acid.