164332-89-2

Basic information

• Product Name: Boc-4-Amino-D-phenylalanine
• Synonyms: RARECHEM BK PT 0174;(R)-2-(TERT-BUTOXYCARBONYLAMINO)-3-(4-AMINOPHENYL)PROPANOIC ACID;N-ALPHA-T-BUTOXYCARBONYL-4-AMINO-D-PHENYLALANINE;N-ALPHA-TBOC-P-AMINO-D-PHENYLALANINE;N-ALPHA-TERT-BUTYLOXYCARBONYL-D-4-AMINOPHENYLALANINE;N-ALPHA-BOC-D-4-(AMINO)-PHENYLALANINE;(R)-3-(4-aminophenyl)-2-(tert-butoxycarbonylamino)propanoic acid;N-ALPHA-T-BUTYLOXYCARBONYL-D-4-AMINOPHENYLALANINE
• CAS NO: 164332-89-2
• Molecular Formula: C14H20N2O4
• Molecular Weight: 280.32
• Product Categories: Phenylalanine analogs and other aromatic alpha amino acids;Amino Acids;Phenylalanine [Phe, F];Unusual Amino Acids;Boc-Amino acid series;a-amino
• Mol File: 164332-89-2.mol

Chemical Properties

• Melting Point: 130-132°C
• Boiling Point: 484.9 °C at 760 mmHg
• Flash Point: 247 °C
• Appearance: /
• Density: 1.213 g/cm³
• Vapor Pressure: 3.25E-10mmHg at 25°C
• Refractive Index: 1.56
• Storage Temp.: -15°C
• PKA: 3.74±0.10(Predicted)
• CAS DataBase Reference: Boc-4-Amino-D-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: Boc-4-Amino-D-phenylalanine(164332-89-2)
• EPA Substance Registry System: Boc-4-Amino-D-phenylalanine(164332-89-2)

Safety Data

• Statements: 36/37/38
• Safety Statements: 26-36/37/39
• HazardClass: IRRITANT
• Hazardous Substances Data: 164332-89-2(Hazardous Substances Data)

Usage

Chemical Properties

White to off-white powder

InChI:InChI=1/C14H20N2O4/c1-14(2,3)20-13(19)16-11(12(17)18)8-9-4-6-10(15)7-5-9/h4-7,11H,8,15H2,1-3H3,(H,16,19)(H,17,18)/t11-/m1/s1

Upstream product

• 33305-77-0 (2R)-2-{[(tert-butoxy)carbonyl]amino}-3-(4-nitrophenyl)propanoic acid 
• 56613-61-7 (R)-4-nitro-phenylalanine 
• 673-06-3 D-(R)-phenylalanine 
• 86937-80-6 2-tert-butoxycarbonylamino-3-(4-nitro-phenyl)-propionic acid 
• 80994-44-1 {[(tert-butoxycarbonyl)oxy]amino}(phenyl)acetonitrile 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 
• 33173-55-6 (S)-3-(4-azidophenyl)-2-((tert-butoxycarbonyl)amino)propanoic acid 
• 33305-77-0 Boc-Phe(p-NO₂)-OH 

Downstream Products

• 232594-43-3 (S)-3-[4-[[2-(3-benzyl-ureido)-thiazole-4-carbonyl]-amino]-phenyl]-2-tert-butoxy-carbonylamino-propionic acid 
• 232594-45-5 (R)-3-[4-[[2-(3-benzyl-ureido)-thiazole-4-carbonyl]-amino]-phenyl]-2-tert-butoxy-carbonylamino-propionic acid 
• 583870-09-1 (2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-[4-[(2-methylpropan-2-yl)oxycarbonylamino]phenyl]propanoic acid 

Relevant articles and documents

Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres

Hepsin is a type II transmembrane serine protease (TTSP) associated with cell proliferation and overexpressed in several types of cancer including prostate cancer (PCa). Because of its significant role in cancer progression and metastasis, hepsin is an attractive protein as a potential therapeutic and diagnostic biomarker for PCa. Based on the reported Leu-Arg dipeptide-based hepsin inhibitors, we performed structural modification and determined in vitro hepsin- and matriptase-inhibitory activities. Comprehensive structure-activity relationship studies identified that the p-guanidinophenylalanine-based dipeptide analog 22a exhibited a strong hepsin-inhibitory activity (Ki = 50.5 nM) and 22-fold hepsin selectivity over matriptase. Compound 22a could be a prototype molecule for structural optimization of dipeptide-based hepsin inhibitors.

Multistimuli-responsive supramolecular organogels formed by low-molecular-weight peptides bearing side-chain azobenzene moieties

This work demonstrates that the incorporation of azobenzene residues into the side chain of low-molecular-weight peptides can modulate their self-assembly process in organic solvents leading to the formation of stimuli responsive physical organogels. The major driving forces for the gelation process are hydrogen bonding and π-π interactions, which can be triggered either by thermal or ultrasound external stimuli, affording materials having virtually the same properties. In addition, a predictive model for gelation of polar protic solvent was developed by using Kamlet-Taft solvent parameters and experimental data. The obtained viscoelastic materials exhibited interconnected multistimuli responsive behaviors including thermal-, photo-, chemo- and mechanical responses. All of them displayed thermoreversability with gel-to-sol transition temperatures established between 33-80 °C and gelation times from minutes to several hours. Structure-property relationship studies of a designed peptide library have demonstrated that the presence and position of the azobenzene residue can be operated as a versatile regulator to reduce the critical gelation concentration and enhance both the thermal stability and mechanical strength of the gels, as demonstrated by comparative dynamic rheology. The presence of N-Boc protecting group in the peptides showed also a remarkable effect on the formation and properties of the gels. Despite numerous examples of peptide-based gelators known in the literature, this is the first time in which low-molecular-weight peptides bearing side chain azobenzene units are used for the synthesis of "intelligent" supramolecular organogels. Compared with other approaches, this strategy is advantageous in terms of structural flexibility since it is compatible with a free, unprotected amino terminus and allows placement of the chromophore at any position of the peptide sequence. Intelligent response: The incorporation of the azobenzene moiety into the side chain of low-molecular-weight peptides allows for the preparation of multistimuli-responsive supramolecular organogels. The presence and position of the azobenzene residue act as a versatile regulator to reduce the minimum gelation concentration and enhance both the thermal stability and mechanical strength of the materials (see figure). Copyright

Large amino acid transporter 1 (LAT1) prodrugs of valproic acid: New prodrug design ideas for central nervous system delivery

Central nervous system (CNS) drug delivery is a major challenge in drug development because the blood-brain barrier (BBB) efficiently restricts the entry of drug molecules into the CNS at sufficient amounts. The brain uptake of poorly penetrating drugs could be improved by utilizing the transporters at the BBB with a prodrug approach. In this study, we designed four phenylalanine derivatives of valproic acid and studied their ability to utilize a large amino acid transporter 1 (LAT1) in CNS delivery with an aim to show that the meta-substituted phenylalanine prodrugs bind to LAT1 with a higher affinity compared with the affinity of the para-substituted derivatives. All of the prodrugs crossed the BBB carrier mediatedly via LAT1 in in situ rat brain perfusion. For the first time, we introduced a novel meta-substituted phenylalanine analogue promoiety which improved the LAT1 affinity 10-fold and more importantly the rat brain uptake of the prodrug 2-fold compared with those of the para-substituted derivatives. Therefore, we have characterized a new prodrug design idea for CNS drug delivery utilizing a transporter-mediated prodrug approach.

Synthesis and?antiproliferative activities of?indolin-2-one?derivatives bearing amino acid moieties

A convenient synthesis of indolin-2-ones substituted in the 3 position by an aminomethylene group bearing different amino acid moieties is described. Their antiproliferative activities were evaluated toward a panel of human solid tumor cell lines (PC 3, DLD-1, MCF-7, M4 Beu, A549, PA 1) and healthy cell lines (a murine fibroblast L929 and a human fibroblast primary culture).

Melphalan derivatives and their use as cancer chemotherapeutic drugs

The invention refers to new alkylating di- and tripeptides based on a melphalan unit, and one or two additional amino acids or amino acid derivatives, which can be used in the treatment of carcinogenic diseases. Further, the invention refers to a a pharmaceutical composition comprising the alkylating peptides of the invention.

A general Staudinger protocol for solution-phase parallel synthesis

The Staudinger reaction has been adapted for parallel synthesis by the application of fluorous-tethered triphenyl phosphine. The fluorous-tethered triphenylphosphine is expediently removed in parallel by FluoroFlash SPE columns to afford functionalized amines in high yields and purities.

Selective protein tyrosine phosphatatase inhibitors

Compounds of formula (I) or therapeutically acceptable salts thereof, are selective protein tyrosine kinase-B (PTP1B) inhibitors. Preparation of the compounds, compositions containing the compounds, and treatment of disorders using the compounds are disclosed.

Asymmetric synthesis of conformationally restricted L-arginine analogues as active site probes of nitric oxide synthase

Using the catalytic asymmetric sharpless carbamate aminohydroxylation, conformationally restricted L-arginine and L-homoarginine derivatives (5-8) were prepared in good enantiomeric excess to investigate the binding requirements of L-arginine-based compounds with nitric oxide synthase. The L- arginine derivatives (5 and 6) inhibited both the inducible and neuronal isoforms of nitric oxide synthase with little isoform selectivity (5, IC50 = 42 and 144 μM, 6, 8 and 12 μM, respectively). The guanidine-containing compound (5) did not act as a nitric oxide producing substrate for nitric oxide synthase. The ability of these compounds to interact with the enzyme supports the idea that L-arginine-based inhibitors bind to the enzyme in a folded conformation. The L-homoarginine derivatives (7 and 8) did not interact with the enzyme as either substrates or inhibitors. The two-carbon L-arginine homologue (9), prepared from L-phenylalanine, demonstrated the greatest isoform selective inhibition of the compounds examined (IC50(iNOS) = 19 and IC50(nNOS) = 147 μM, IC50(nNOS)/IC50i(NOS) = 7.7). These results suggest isoform selective inhibition may be related to the folded conformations required for binding of these higher L-arginine homologues.

Development of active center-directed plasmin and plasma kallikrein inhibitors and studies on the structure-inhibitory activity relationship

The molecule of trans-4-aminomethylcyclohexanecarbonylphenylalanine 4- carboxymethylanilide (8), which is a potent and selective inhibitor of plasma kallikrein, can be divided into three parts (P1, P1 and P2), each of which contains one of the rings. In order to study the role of each part in the manifestation of potent and selective inhibitory activity and the relationship between the structure and inhibitory activities toward plasmin, plasma kallikrein, urokinase and thrombin, each part was substituted with various other moieties to give many kinds of analogs and their inhibitory activities against the above enzymes were examined. Among them, trans-4- aminomethylcyclohexanecarbonyl-O-2-bromobenzyloxycarbonyltyrosine 4- acetylanilide (12) inhibited plasmin and plasma kallikrein with IC50 values of 2.3 x 10-7 M and 3.7 x 10-7 M, and K(i) values of 1.2 x 10-7 M and 1.3 x 10-7 M, respectively.