70702-47-5

Basic information

• Product Name: 3-(3-Pyridyl)-D-alanine
• Synonyms: (R)-2-AMINO-3-(3'-PYRIDYL)PROPANOIC ACID;(R)-2-AMINO-3-PYRIDIN-3-YL-PROPIONIC ACID;RARECHEM AK ML 0090;H-BETA-(3-PYRIDYL)-D-ALA-OH 2 HCL;H-D-ALA(3'-PYRIDYL)-OH;H-D-ALA(3-PYRIDYL)-OH;H-D-ALA(3-PYRI)-OH;H-D-ALA(3-PYRI)-OH HCL
• CAS NO: 70702-47-5
• Molecular Formula: C₈H₁₀N₂O₂
• Molecular Weight: 166.18
• Product Categories: GLYCINESCAFFOLD;Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Alanine [Ala, A];Unusual Amino Acids;Amino hydrochloride;a-amino
• Mol File: 70702-47-5.mol

Chemical Properties

• Melting Point: 167-168 °C
• Boiling Point: 344.4 °C at 760 mmHg
• Flash Point: 162.1 °C
• Appearance: Off-white/Powder
• Density: 1.271 g/cm³
• Vapor Pressure: 3.86E-06mmHg at 25°C
• Storage Temp.: 2-8°C
• Solubility: 1 M HCl: 10 mg/mL, clear, colorless
• PKA: 1.95±0.10(Predicted)
• CAS DataBase Reference: 3-(3-Pyridyl)-D-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: 3-(3-Pyridyl)-D-alanine(70702-47-5)
• EPA Substance Registry System: 3-(3-Pyridyl)-D-alanine(70702-47-5)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36
• WGK Germany: 3
• F: 10
• Hazardous Substances Data: 70702-47-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
3-(3-Pyridyl)-D-alanine is used as a precursor in the synthesis of potent and subtype-selective ligands derived from N-methylation of a somatostatin antagonist. These ligands have potential applications in the development of drugs targeting specific somatostatin receptor subtypes, which can be useful in treating various neurological and endocrine disorders.
Used in Neuropeptide Research:
3-(3-Pyridyl)-D-alanine is used as a key component in the synthesis of morphiceptin analogs, which are neuropeptides with significant μ-opioid receptor binding activities. These analogs are valuable tools in neurobiological research, particularly in the study of opioid receptors and their role in pain perception, addiction, and other related physiological processes.
Used in Oncology Research:
In the field of oncology, 3-(3-Pyridyl)-D-alanine is utilized for the synthesis of morphiceptin analogs that exhibit binding activities in brain and mammary adenocarcinoma. These analogs can be instrumental in understanding the molecular mechanisms underlying cancer progression and in the development of targeted therapies for the treatment of brain and mammary tumors.

InChI:InChI=1/C8H10N2O2.ClH/c9-7(8(11)12)4-6-2-1-3-10-5-6;/h1-3,5,7H,4,9H2,(H,11,12);1H/t7-;/m1./s1

Upstream product

• 132478-13-8 5-[3]pyridylmethylene-imidazolidine-2,4-dione 
• 33560-91-7 2-(benzoylamino)-3-(3-pyridinyl)-propanoic acid 
• 41668-18-2 3,6-bis-[3]pyridylmethylene-piperazine-2,5-dione 
• 108-24-7 acetic anhydride 
• 500-22-1 3-pyridinecarboxaldehyde 
• 553-53-7 Nicotinic acid hydrazide 
• 5433-39-6 N'-nicotinoylbenzenesulfonohydrazide 
• 5086-43-1 2-phenyl-4-(pyridin-3-ylmethylene)oxazol-5(4H)-one 
• 102913-22-4 (4Z)-2-methyl-4((pyridin-3-yl)methylene)oxazol-5(4H)-one 
• 170092-30-5 N-acetyl-(β-3-pyridyl)-DL-alanine 
• 64090-98-8 L-(3-Pyridyl)-Alanine 
• 19337-97-4 trans-3-(3-pyridyl)acrylic acid 
• 69966-55-8 3-picolyl bromide 
• 95200-93-4 d-methyl 2-acetamido-3-(3-pyridyl)propanoate 

Downstream Products

• 20173-24-4 2-pyridin-3-ylethylamine 
• 123760-88-3 2-(4-Chloro-benzylamino)-3-pyridin-3-yl-propionic acid 
• 1397697-66-3 N-fluorenylmethyloxycarbonyl-3-pyridylalanine-methyl ester 
• 1397697-68-5 C₂₄H₂₂N₂O₄ 
• 175453-07-3 (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(pyridin-3-yl)propanoic acid 
• 746672-88-8 C₂₃H₂₀N₂O₄ 
• 105454-25-9 N-(tert-butoxycarbonyl)-3-(pyridin-3-yl)alanine 
• 15504-40-2 3-(pyridin-3-yl)pyruvic acid 
• 98266-33-2 Boc-DPal 
• 240428-64-2 N-<(1,1-dimethylethoxy)carbonyl>-2,2-dimethyl-β-alanyl-(2S)-2-hydroxy-4-(methylpentanoyl)-(2E,5S,6R,7E)-5-hydroxy-6-methyl-8-phenyl-2,7-octadienoyl-3-(3-pyridinyl)-D-alanine 
• 923015-03-6 1-(2-tert-butoxycarbonylamino-3-pyridin-3-yl-propionyl)-pyrrolidine-2-carboxylic acid methyl ester 
• 923015-04-7 1-[2-(2-tert-butoxycarbonylamino-4-methyl-pentanoylamino)-3-pyridin-3-yl-propionyl]-pyrrolidine-2-carboxylic acid methyl ester 
• 923015-05-8 1-{2-[2-(5-benzyloxycarbonylamino-2-tert-butoxycarbonylamino-pentanoylamino)-4-methyl-pentanoylamino]-3-pyridin-3-yl-propionyl}-pyrrolidine-2-carboxylic acid methyl ester 

Relevant articles and documents

SMALL MOLECULE VE-PTP INHIBITORS

The present disclosure relates to compounds capable of inhibiting vascular endothelial protein tyrosine phosphatase (VE-PTP). These compounds are also capable of activating Tie2 receptor-mediated signaling. The present disclosure also relates to pharmaceutically acceptable salts of said compounds, to pharmaceutical compositions comprising such compounds and/or pharmaceutically acceptable salts thereof, and to the use of such compounds, pharmaceutically acceptable salts thereof, and/or pharmaceutical compositions comprising the same in treating diseases and/or conditions mediated by VE-PTP signaling, such as those mediated by Angiopoietm/Tie2 signaling.

Deracemization and Stereoinversion of α-Amino Acids by l-Amino Acid Deaminase

Enantiomerically pure α-amino acids are compounds of primary interest for the fine chemical, pharmaceutical, and agrochemical sectors. Amino acid oxidases are used for resolving d,l-amino acids in biocatalysis. We recently demonstrated that l-amino acid deaminase from Proteus myxofaciens (PmaLAAD) shows peculiar features for biotechnological applications, such as a high production level as soluble protein in Escherichia coli and a stable binding with the flavin cofactor. Since l-amino acid deaminases are membrane-bound enzymes, previous applications were mainly based on the use of cell-based methods. Now, taking advantage of the broad substrate specificity of PmaLAAD, a number of natural and synthetic l-amino acids were fully converted by the purified enzyme into the corresponding α-keto acids: the fastest conversion was obtained for 4-nitrophenylalanine. Analogously, starting from racemic solutions, the full resolution (ee >99%) was also achieved. Notably, d,l-1-naphthylalanine was resolved either into the d- or the l-enantiomer by using PmaLAAD or the d-amino acid oxidase variant having a glycine at position 213, respectively, and was fully deracemized when the two enzymes were used jointly. Moreover, the complete stereoinversion of l-4-nitrophenylalanine was achieved using PmaLAAD and a small molar excess of borane tert-butylamine complex. Taken together, recombinant PmaLAAD represents an l-specific amino acid deaminase suitable for producing the pure enantiomers of several natural and synthetic amino acids or the corresponding keto acids, compounds of biotechnological or pharmaceutical relevance. (Figure presented.).

METHOD FOR SYNTHESIZING OPTICALLY ACTIVE a-AMINO ACID USING CHIRAL METAL COMPLEX COMPRISING AXIALLY CHIRAL N-(2-ACYLARYL)-2-[5,7-DIHYDRO-6H-DIBENZO[c,e]AZEPIN-6-YL] ACETAMIDE COMPOUND AND AMINO ACID

Objects of the present invention are to provide an industrially applicable method for producing an optically active α-amino acid in high yield and in a highly enantioselective manner, to provide a simple production method of an optically active α,α-disubstituted α-amino acid, and to provide an intermediate useful for the above production methods of an optically active α-amino acid and an optically active α,α-disubstituted α-amino acid. The present invention provides a production method of an optically active α-amino acid or a salt thereof, the production method comprising introducing a substituent into the α carbon in the α-amino acid moiety of a metal complex represented by the following Formula (1): by an alkylation reaction, an aldol reaction, the Michael reaction, or the Mannich reaction, and releasing an optically pure α-amino acid enantiomer or a salt thereof by acid decomposition of the metal complex.

METHOD FOR SYNTHESIZING OPTICALLY ACTIVE α-AMINO ACID USING CHIRAL METAL COMPLEX COMPRISING AXIALLY CHIRAL N-(2-ACYLARYL)-2-[5,7-DIHYDRO-6H-DIBENZO[c,e]AZEPIN-6-YL]ACETAMIDE COMPOUND AND AMINO ACID

Objects of the present invention are to provide an industrially applicable method for producing an optically active ±-amino acid in high yield and in a highly enantioselective manner, to provide a simple production method of an optically active ±,±-disubstituted ±-amino acid, and to provide an intermediate useful for the above production methods of an optically active ±-amino acid and an optically active ±,±-disubstituted ±-amino acid. The present invention provides a production method of an optically active ±-amino acid or a salt thereof, the production method comprising introducing a substituent into the ± carbon in the ±-amino acid moiety of a metal complex represented by the following Formula (1): by an alkylation reaction, an aldol reaction, the Michael reaction, or the Mannich reaction, and releasing an optically pure ±-amino acid enantiomer or a salt thereof by acid decomposition of the metal complex.

Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway

Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.

Chemoenzymatic routes to enantiomerically pure 2-azatyrosine and 2-, 3- and 4-pyridylalanine derivatives

Enantiomerically pure 2-, 3- or 4-pyridylalanine (pya) and 2-azatyrosine (azatyr) are known to present various biological activities. After incorporation into appropriate peptide sequences, these heterocyclic non natural α-amino acids could behave as new substrates or inhibitors of elastase from Pseudomonas aeruginosa. This enzyme is known to be involved in nosocomial infections and infections related to the cystic fibrosis disease. New efficient chemoenzymatic preparations of those compounds using α-chymotrypsin (α-CT) are presented. Springer-Verlag 2011.

Synthesis of low-hemolytic antimicrobial dehydropeptides based on gramicidin S

The synthesis and biological activity of a novel cyclic β-sheet-type antimicrobial dehydropeptide based on gramicidin S (GS) is described. The GS analogue, containing two (Z)-(β-3-pyridyl)-α,β-dehydroalanine (ΔZ3Pal) residues at the 4 and 4′ positions (2), was synthesized by solution-phase methodologies using Boc-Leu-ΔZ3Pal azlactone. Analogue 2 exhibited high antimicrobial activity against Gram-positive bacteria and had much lower hemolytic activity than wild-type GS and the corresponding (Z)-α,β-dehydrophenylalanine (ΔZ-Phe) analogue (1).