5241-58-7

Basic information

• Product Name: H-PHE-NH2
• Synonyms: H-PHE-NH2;H-L-PHE-NH2;L-PHENYLALANINE AMIDE;L-PHENYLALANINAMIDE;PHENYLALANINE-NH2;L-phenylalaninamide free base;H-Phe-Nh;2-Amino-3-phenylpropanamide
• CAS NO: 5241-58-7
• Molecular Formula: C₉H₁₂N₂O
• Molecular Weight: 164.2
• Product Categories: Phenylalanine [Phe, F];Amino Acids and Derivatives;Amino Acid Derivatives;Peptide Synthesis;Phenylalanine;Amino Acids;I - Z;Modified Amino Acids;Amino Acids & Derivatives;Aromatics;Chiral Reagents
• Mol File: 5241-58-7.mol

Chemical Properties

• Melting Point: 93-95°C
• Boiling Point: 356.9 °C at 760 mmHg
• Flash Point: 169.7 °C
• Appearance: White/Powder
• Density: 1.143 g/cm³
• Storage Temp.: −20°C
• PKA: 15.85±0.50(Predicted)
• BRN: 6270941
• CAS DataBase Reference: H-PHE-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-NH2(5241-58-7)
• EPA Substance Registry System: H-PHE-NH2(5241-58-7)

Safety Data

• WGK Germany: 3
• HazardClass: IRRITANT
• Hazardous Substances Data: 5241-58-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-PHE-NH2 is used as an active pharmaceutical ingredient for its potential therapeutic applications. It plays a crucial role in the synthesis of various drugs and is involved in the treatment of several medical conditions.
Used in Food Industry:
H-PHE-NH2 is used as a flavor enhancer and additive in the food industry. Its unique taste and properties contribute to the enhancement of flavors in various food products.
Used in Cosmetic Industry:
H-PHE-NH2 is used as a key ingredient in the cosmetic industry, where it is utilized for its potential benefits in skincare and hair care products.
Used in Research and Development:
H-PHE-NH2 is used as a research compound in the field of biochemistry and molecular biology. It is essential for understanding the structure and function of proteins and other biological molecules.

InChI:InChI=1/C9H12N2O/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H2,11,12)/t8-/m0/s1

Upstream product

• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 3081-24-1 H-Phe-OEt 
• 5241-56-5 benzyl [(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]carbamate 
• 73148-50-2 Z(OMe)-Phe-NH₂ 
• 24730-33-4 (S)-2-amino-3-phenylpropanamide hydrobromide 
• 155385-83-4 (-)-1-<(1-cyano-2-phenylethyl)amino>-2R-methyl-5R-(1-methylethenyl)cyclohexane-1R,3R-dicarbonitrile 
• 35661-40-6 N-Fmoc L-Phe 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 47091-50-9 Asp-Phe-NH₂ 
• 15028-44-1 DL-phenylalanine methyl ester 
• 88463-18-7 (S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropionamide 
• 17193-31-6 (R,S)-2-amino-3-phenylpropionamide 
• 33662-25-8 (S)-N-Boc-phenylalanine benzylamide 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 

Downstream Products

• 33900-05-9 tert-butyl (S)-N-{2-[(2-amino-1-benzyl-2-oxoethyl)amino]-2-oxoethyl}carbamate 
• 17337-67-6 L--Phe-amid 
• 5241-68-9 Z-Asp(OBzl)-Phe-NH₂ 
• 81092-90-2 benzyloxycarbonyl-α-tert-butyl-L-aspartyl-β-L-phenylalanine amide 
• 17337-66-5 N-Benzyloxycarbonyl-γ-O-tert.-butyl-Glu-Phe-amid 
• 17471-89-5 carbobenzoxy-β-alanyl-L-phenylalanine amide 
• 17337-71-2 N-Benzyloxycarbonyl-L-norvalyl-Phe-amid 
• 129095-57-4 Z-Asn-Phe-NH₂ 
• 17327-61-6 N-Benzyloxycarbonyl-L-α-aminobuttersaeure-Phe-amid 
• 33900-18-4 Cam-3508 
• 38678-60-3 leucylphenylalanylamide 
• 27220-69-5 Boc-Ala-Phe-NH₂ 
• 33900-15-1 (2S)-N-[(1S)-2-amino-1-benzyl-2-oxoethyl]-2-[(tert-butoxycarbonyl)amino]-4-methylpentanamide 
• 17337-74-5 [(1S,2R)-1-((S)-1-Carbamoyl-2-phenyl-ethylcarbamoyl)-2-hydroxy-propyl]-carbamic acid benzyl ester 

Relevant articles and documents

Mechanism of fluorescence quenching of tyrosine derivatives by amide group

The difference between fluorescence lifetimes of the following amino acids: phenylalanine (Phe), tyrosine (Tyr), (O-methyl)tyrosine (Tyr(Me)), (3-hydroxy)tyrosine (Dopa), (3,4-dimethoxy)phenylalanine (Dopa(Me)2) and their amides was used to tes

Mechanochemical Synthesis of Primary Amides

Ball milling of aromatic, heteroaromatic, vinylic, and aliphatic esters with ethanol and calcium nitride afforded the corresponding primary amides in a transformation that was compatible with a variety of functional groups and maintained the integrity of a stereocenter α to carbonyl. This methodology was applied to α-amino esters and N-BOC dipeptide esters and also to the synthesis of rufinamide, an antiepileptic drug.

Guanidine-containing compound as well as preparation method and application thereof

The invention discloses a cyanoguanidine-containing compound as well as a preparation method and application thereof. The invention also discloses a composition containing the cyanoguanidine-structured compound (I) or a pharmaceutically acceptable salt thereof and a pharmaceutically acceptable carrier. The invention also discloses application thereof in preparation of analgesic drugs. The compounds of the invention are useful in the treatment of various pain.

Hybrid catalysis of 8-quinolinecarboxaldehyde and br?nsted acid for efficient racemization of α-amino amides and its application in chemoenzymatic dynamic kinetic resolution

The combination of 8-quinolinecarboxaldehyde and benzoic acid proved to be an effective catalyst system for the racemization of N-unprotected α-aryl- or α-alkyl-substituted α-amino amides. Application of this system to chemoenzymatic dynamic kinetic resolution provided an efficient access to enantiomerically pure N-acetyl-α-amino amides in good to high yields.

Mapping the s1 and s1’ subsites of cysteine proteases with new dipeptidyl nitrile inhibitors as trypanocidal agents

The cysteine protease cruzipain is considered to be a validated target for therapeutic intervention in the treatment of Chagas disease. A series of 26 new compounds were designed, synthesized, and tested against the recombinant cruzain (Cz) to map its S1/S1′ subsites. The same series was evaluated on a panel of four human cysteine proteases (CatB, CatK, CatL, CatS) and Leishmania mexicana CPB, which is a potential target for the treatment of cutaneous leishmaniasis. The synthesized compounds are dipeptidyl nitriles designed based on the most promising combinations of different moieties in P1 (ten), P2 (six), and P3 (four different building blocks). Eight compounds exhibited a Ki smaller than 20.0 nM for Cz, whereas three compounds met these criteria for LmCPB. Three inhibitors had an EC50 value of ca. 4.0 μM, thus being equipotent to benznidazole according to the antitrypanosomal effects. Our mapping approach and the respective structure-activity relationships provide insights into the specific ligand-target interactions for therapeutically relevant cysteine proteases.

ANALOGS THAT TARGET MITOCHONDRIAL DISEASES

Disclosed are analogs of elamipretide (MTP-131). The compounds are useful for the treatment and prevention of ischemia-reperfusion injury (e.g., cardiac ischemia-reperfusion injury) or myocardial infarction.

HEMIAMINAL-TAG FOR PROTEIN LABELING AND PURIFICATION

The invention pertains to the synthesis, isolation, and characterization of hemiaminal for selective labeling of peptides, proteins, antibodies, and organic fragments with -C(=0) CH2NH2 and derivatives with -CH2NH2 group over -C(=0) CHRNH2 group (where R≠H). The invention also pertains to the method of single-site immobilization of proteins through N-terminus Gly on solid phase. The invention includes late-stage tagging of N-terminus Gly with an affinity tag, 19F NMR probe, and a fluorophore and a method for metal-free protein purification and isolation of analytically pure proteins.

3, 5-disubstituted hydantoin compound as well as preparation method and application thereof

The invention provides a 3, 5-disubstituted hydantoin compound as well as a preparation method and an application thereof. The structure of the compound is shown in formula I in the description. The application of the 3, 5-disubstituted hydantoin compound shown in the formula I or solvates, hydrates or salts of the compound in preparation of medicines for treating Alzheimer's disease, vascular dementia and other dementia diseases with memory impairment also belongs to the protection scope. Animal experiments prove that the compound has the effect of saving memory of animal models, has high safety, does not have mutagenicity, can stay in blood for several hours after oral administration and intravenous injection, and can enter the brain.

Synthetic method for chiral alpha-aminoamide compounds

The invention provides a synthetic method for chiral alpha-aminoamide compounds, belongs to the technical field of organic synthetic methodology, and concretely relates to a synthetic method for chiral alpha-aminoamide compounds, wherein the method has a simple process, low costs and good economy. The method comprises the following steps: 1, performing ammonolysis: adding substituted chiral alpha-aminocarboxylate hydrochloride into concentrated ammonia water, performing stirring for 4-12h under a room temperature, wherein each 1mmol substituted chiral alpha-aminocarboxylate hydrochloride is corresponding to 2-8mL the concentrated ammonia water; 2, after a reaction is finished, performing distillation for removing ammonia water after the reaction to obtain crude products chiral alpha-aminoamide compounds; and 3, performing filtration on the obtained crude products chiral alpha-aminoamide compounds by adopting a manner of adding a solvent or performing purification on the obtained crude products chiral alpha-aminoamide compounds through a manner of column chromatography which uses ammonia water as a mobile phase to obtain the products chiral alpha-aminoamide compounds. Compared with the prior art, a large number of an ammonia gas for ammonolysis is not needed in the method, the process and post-treatment are simple, costs are low and reaction time is short.

Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (ThP-MP) Inhibitors of the Human Farnesyl Pyrophosphate Synthase

The human farnesyl pyrophosphate synthase (hFPPS), a key regulatory enzyme in the mevalonate pathway, catalyzes the biosynthesis of the C-15 isoprenoid farnesyl pyrophosphate (FPP). FPP plays a crucial role in the post-translational prenylation of small GTPases that perform a plethora of cellular functions. Although hFPPS is a well-established therapeutic target for lytic bone diseases, the currently available bisphosphonate drugs exhibit poor cellular uptake and distribution into nonskeletal tissues. Recent drug discovery efforts have focused primarily on allosteric inhibition of hFPPS and the discovery of non-bisphosphonate drugs for potentially treating nonskeletal diseases. Hit-to-lead optimization of a new series of thienopyrimidine-based monosphosphonates (ThP-MPs) led to the identification of analogs with nanomolar potency in inhibiting hFPPS. Their interactions with the allosteric pocket of the enzyme were characterized by crystallography, and the results provide further insight into the pharmacophore requirements for allosteric inhibition.