324017-21-2

Usage

Uses

Used in Peptide Synthesis:
FMOC-4-Amino-D-phenylalanine is used as a building block for the creation of peptide chains, playing a crucial role in the synthesis of various biologically active peptides. The FMOC protecting group ensures that the amino group remains protected during the initial stages of peptide synthesis, facilitating the controlled assembly of peptide sequences.
Used in Biochemistry Research:
In the realm of biochemistry, FMOC-4-Amino-D-phenylalanine is utilized for the study and development of novel peptide-based compounds. Its unique structure and the presence of the FMOC group make it an ideal candidate for exploring the properties and functions of peptides in biological systems.
Used in Pharmaceutical Research:
FMOC-4-Amino-D-phenylalanine is employed as a key component in the synthesis of pharmaceutically relevant peptides and peptidomimetics. Its versatility in peptide synthesis allows for the development of new drug candidates with potential therapeutic applications in various diseases and conditions.
Used in the Synthesis of Peptidomimetics:
FMOC-4-Amino-D-phenylalanine is also used in the design and synthesis of peptidomimetics, which are peptide-like compounds that mimic the structure and function of natural peptides. These peptidomimetics can offer improved stability and bioavailability compared to their natural peptide counterparts, making them attractive candidates for drug development.

Upstream product

• 943-80-6 4-amino-L-phenylalanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 177966-63-1 (2R)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(4-nitrophenyl)propionic acid 
• 673-06-3 D-(R)-phenylalanine 
• 56613-61-7 (R)-4-nitro-phenylalanine 
• 95753-55-2 N-α-FMOC-4-nitro-L-phenylalanine 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 63-91-2 L-phenylalanine 

Downstream Products

• 95753-57-4 N-Fmoc-L-p-aminophenylalanine methyl ester hydrochloride 
• 214750-77-3 N-α-(9-fluoromethoxycarbonyl)-L-4-tert-butoxycarbonylaminophenylalanine 
• 1421639-82-8 (S)-tert-butyl (4-(2-amino-3-(methoxy(methyl)amino)-3-oxopropyl)phenyl)carbamate 
• 1421639-83-9 (S)-tert-butyl (4-(3-(methoxy(methyl)amino)-3-oxo-2-(tritylamino)propyl)phenyl)carbamate 
• 1421639-84-0 (S,E)-tert-butyl (4-(4-(methylsulfonyl)-2-(tritylamino)but-3-en-1-yl)phenyl)carbamate 
• 1431297-95-8 (S,E)-tert-butyl (4-(4-(methylsulfonyl)-2-aminobut-3-en-1-yl)phenyl)carbamate 
• 1421639-85-1 (S)-benzyl (3-(4-(tert-butyloxycarbonylamino)phenyl)-1-(methoxy(methyl)amino)-1-oxopropan-2-yl)carbamate 
• 1421639-86-2 (S)-benzyl (1-(4-(tert-butyloxycarbonylamino)phenyl)-4-methyl-3-oxopent-4-en-2-yl)carbamate 
• 1421639-87-3 benzyl ((2S,3R)-1-(4-(tert-butyloxycarbonylamino)phenyl)-3-hydroxy-4-methylpent-4-en-2-yl)carbamate 
• 1421639-88-4 benzyl ((S)-3-(4-(tert-butyloxycarbonylamino)phenyl)-1-((R)-2-methyloxiran-2-yl)-1-oxopropan-2-yl)carbamate 

Relevant academic research and scientific papers

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.

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.

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.

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.