58438-03-2

Basic information

• Product Name: 3-(2-Naphthyl)-L-alanine
• Synonyms: 3-(2-NAPHTHYL)-L-ALANINE.HCL 98%;(R)-2-Amino-3-naphthalene-2-yl-propionic acid;3-(2-Naphthyl)-L-alanine;1-(S)-AMINO-2-NAPHTHALENEPROPANOIC ACID;3-Naphth-2-yl-L-alanine;(2S)-2-Amino-3-(2-naphthyl)propanoic acid;(2S)-2-Amino-3-(2-naphthyl)propionic acid;(S)-2-Amino-3-(2-naphthyl)propanoic acid
• CAS NO: 58438-03-2
• Molecular Formula: C₁₃H₁₃NO₂
• Molecular Weight: 215.25
• Product Categories: Alanine [Ala, A];Unusual Amino Acids;a-amino;Amino Acids
• Mol File: 58438-03-2.mol

Chemical Properties

• Melting Point: 240°C(dec.)(lit.)
• Boiling Point: 355.53°C (rough estimate)
• Flash Point: 203.2 °C
• Appearance: Off-white/Crystalline Powder
• Density: 1.1242 (rough estimate)
• Refractive Index: 1.5480 (estimate)
• Storage Temp.: 2-8°C
• Solubility: Soluble in 1mol/L NaOH.
• PKA: 2.21±0.30(Predicted)
• CAS DataBase Reference: 3-(2-Naphthyl)-L-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: 3-(2-Naphthyl)-L-alanine(58438-03-2)
• EPA Substance Registry System: 3-(2-Naphthyl)-L-alanine(58438-03-2)

Safety Data

• Hazard Codes: Xi
• Safety Statements: 24/25
• WGK Germany: 3
• Hazardous Substances Data: 58438-03-2(Hazardous Substances Data)

Usage

Uses

Used in Organic Synthesis:
3-(2-Naphthyl)-L-alanine is used as a key intermediate for the synthesis of complex organic molecules. Its unique structure allows for the creation of novel compounds with potential applications in various industries.
Used in Pharmaceuticals:
In the pharmaceutical industry, 3-(2-Naphthyl)-L-alanine is utilized as a crucial building block for the development of new drugs. Its chiral nature and naphthalene ring provide a versatile scaffold for the design of innovative therapeutic agents.
Used in Agrochemicals:
3-(2-Naphthyl)-L-alanine is employed as an important raw material in the synthesis of agrochemicals, such as pesticides and herbicides. Its unique structure contributes to the development of effective and targeted agricultural products.
Used in Dye Industry:
In the dye industry, 3-(2-Naphthyl)-L-alanine is used as a key intermediate for the production of various dyes and pigments. Its naphthalene ring imparts color and stability to the resulting dyes, making them suitable for a wide range of applications.

InChI:InChI=1/C13H13NO2/c14-12(13(15)16)8-9-5-6-10-3-1-2-4-11(10)7-9/h1-7,12H,8,14H2,(H,15,16)/t12-/m0/s1

Upstream product

• 56-40-6 glycine 
• 939-26-4 2-bromomethylnaphthyl bromide 
• 109063-69-6 (S)-methyl 2-amino-3-(naphthalen-2-yl)propanoate 
• 49711-14-0 (E)-3-(naphthalen-2-yl)acrylic acid 
• 138774-94-4 N-(9-fluorenylmethoxycarbonyl)-3-(β-naphthyl)-L-alanine 
• 111726-64-8 3-(naphthalene-2-yl)-2-oxopropanoic acid 
• 37439-99-9 (RS)-N-acetyl-2-naphthylalanine 
• 603944-76-9 (±)-ethyl 2-amino-3-(naphthalen-2-yl)propanoate 
• 172214-89-0 2-Acetylamino-3-naphthalen-2-yl-propionic acid ethyl ester 
• 37447-33-9 acetylamino-[2]naphthylmethyl-malonic acid diethyl ester 
• 139040-43-0 (R)-1,1,1-Trichloro-3-naphthalen-2-yl-propan-2-ol 
• 139040-38-3 1,1,1-Trichloro-3-naphthalen-2-yl-propan-2-one 
• 136015-50-4 2-Acetylamino-2-naphthalen-2-ylmethyl-malonic acid monoethyl ester 
• 14108-60-2 2-amino-3-(2-naphthyl)propanoic acid 

Downstream Products

• 63024-26-0 methyl (S)-2-amino-3-(naphthalen-2-yl)propanoate hydrochloride 
• 56583-58-5 N-tert-butoxycarbonyl-3-(2-naphthyl)-L-alanine 
• 145232-09-3 3-{2-[2-tert-butoxycarbonylamino-3-(1H-indol-3-yl)-propionylamino]-3-naphthalen-2-yl-propionylamino}-N-(1-carbamoyl-2-phenyl-ethyl)-succinamic acid benzyl ester 

Relevant articles and documents

Drug Design Inspired by Nature: Crystallographic Detection of an Auto-Tailored Protease Inhibitor Template

De novo drug discovery is still a challenge in the search for potent and selective modulators of therapeutically relevant target proteins. Here, we disclose the unexpected discovery of a peptidic ligand 1 by X-ray crystallography, which was auto-tailored by the therapeutic target MMP-13 through partial self-degradation and subsequent structure-based optimization to a highly potent and selective β-sheet peptidomimetic inhibitor derived from the endogenous tissue inhibitors of metalloproteinases (TIMPs). The incorporation of non-proteinogenic amino acids in combination with a cyclization strategy proved to be key for the de novo design of TIMP peptidomimetics. The optimized cyclic peptide 4 (ZHAWOC7726) is membrane permeable with an IC50 of 21 nm for MMP-13 and an attractive selectivity profile with respect to a polypharmacology approach including the anticancer targets MMP-2 (IC50: 170 nm) and MMP-9 (IC50: 140 nm).

Tailored Mutants of Phenylalanine Ammonia-Lyase from Petroselinum crispum for the Synthesis of Bulky l- and d-Arylalanines

Tailored mutants of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) were created and tested in ammonia elimination from various sterically demanding, non-natural analogues of phenylalanine and in ammonia addition reactions into the corresponding (E)-arylacrylates. The wild-type PcPAL was inert or exhibited quite poor conversions in both reactions with all members of the substrate panel. Appropriate single mutations of residue F137 and the highly conserved residue I460 resulted in PcPAL variants that were active in ammonia elimination but still had a poor activity in ammonia addition onto bulky substrates. However, combined mutations that involve I460 besides the well-studied F137 led to mutants that exhibited activity in ammonia addition as well. The synergistic multiple mutations resulted in substantial substrate scope extension of PcPAL and opened up new biocatalytic routes for the synthesis of both enantiomers of valuable phenylalanine analogues, such as (4-methoxyphenyl)-, (napthalen-2-yl)-, ([1,1′-biphenyl]-4-yl)-, (4′-fluoro-[1,1′-biphenyl]-4-yl)-, and (5-phenylthiophene-2-yl)alanines.

Asymmetric Transamination of α-Keto Acids Catalyzed by Chiral Pyridoxamines

A new type of novel chiral pyridoxamines 3a-g containing a side chain has been developed. The pyridoxamines displayed catalytic activity and promising enantioselectivity in biomimetic asymmetric transamination of α-keto acids, to give various α-amino acids in 47-90% yields with up to 87% ee's under very mild conditions. An interesting effect of the side chain on enantioselectivity was observed in the reaction.

Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine

l-Aminoacylase from Aspergillus melleus was co-aggregated with polyethyleneimine and subsequently cross-linked with glutaraldehyde to obtain aminoacylase-polyethyleneimine cross-linked enzyme aggregates (termed as AP-CLEA). Under the optimum conditions, AP-CLEA expressed 74.9% activity recovery and 81.2% aggregation yield. The said method of co-aggregation and cross-linking significantly improved the catalytic stability of l-aminoacylase with respect to temperature and storage. AP-CLEA were employed for enantioselective synthesis of three unnatural amino acids (namely: phenylglycine, homophenylalanine and 2-naphthylalanine) via chiral resolution of their ester-, amide- and N-acetyl derivatives. The enantioselectivity of AP-CLEA was the highest for hydrolysis of amino acid amides; was moderate for hydrolysis of N-acetyl amino acids and was the least for hydrolysis of amino acid esters. Furthermore, AP-CLEA were found to retain more than 92% of the initial activity after five consecutive batches of (RS)-homophenylalanine hydrolysis suggesting an adequate operational stability of the biocatalyst.

Enzymatic conversion of unnatural amino acids by yeast D-amino acid oxidase

Unnatural amino acids, particularly synthetic α-amino acids, are becoming crucial tools for modern drug discovery research. In particular, this application requires enantiomerically pure isomers. In this work we report on the resolution of racemic mixtures of the amino acids D,L-naphthylalanine and D,L-naphthylglycine by using a natural enzyme, D-amino acid oxidase from the yeast Rhodotorula gracilis. A significant improvement of the bioconversion is obtained using a single-point mutant enzyme designed by a rational approach. With this D-amino acid oxidase variant the complete resolution of all the unnatural amino acids tested was obtained: in this case, the bioconversion requires a shorter time and a lower amount of biocatalyst compared to the wild-type enzyme. The simultaneous production of the corresponding α-keto acid, a possible precursor of the amino acid in the L-form, improves the significance of the procedure.

Substituted quinoxaline-2-ones as glutamate receptor antagonists

A novel series of substituted quinoxaline 2-ones useful as neuroprotective agents are taught. Novel intermediates, processes of preparation, and pharmaceutical compositions containing the compounds are also taught. The compounds are glutamate receptor antagonists and are useful in the treatment of stroke, cerebral ischemia, or cerebral infarction resulting from thromboembolic or hemorrhagic stroke, cerebral vasospasms, hypoglycemia, cardiac arrest, status epilepticus, perinatal asphyxia, anoxia, seizure disorders, pain, Alzheimer's, Parkinson's, and Huntington's Diseases.

Method for producing optically active amino acid of derivative thereof having high optical purity

A method for producing an optically active amino acid or derivative thereof having a high optical purity from an optically active amino acid comprising optical isomers or derivative thereof, which comprises any one of processes (A), (B), and (C), wherein the process (A) comprises the steps: (1) previously preparing an optically active amino acid or derivative thereof having an optical purity higher than a convergent value of a mutual solubility of the optical isomers and (2) crystallizing the optically active amino acid or the derivative thereof that exists in excess, said convergent value being a ratio of the desired optical isomer in the optical isomers dissolved in a mother liquor in which crystals of a racemate and an optically active compound coexist at equilibrium (the optical purity in a mother liquor). The processes (B) and (C) are described in the specification.

Asymmetric synthesis of α-amino acids via diastereoselective addition of (R)-pantolactone to their ketenes

The diastereoselective addition of (R)-pantolactone to various amino ketenes derived from phthalylamino acids is reported. The configuration of the newly-generated asymmetric center is dependent on alkyl or aryl C(x substitution. This method constitutes a novel and convenient way of amino acid deracemization.

Enzymatic peptide synthesis in frozen aqueous systems: Use of N(α)-unprotected unusual acyl donors

α-Chymotrypsin (EC 3.4.21.1) was used for catalyzing the reaction of various N(α)-unprotected non-coded phenylalanine ester derivatives with H-Leu-NH2 and H-Arg-NH2 in frozen aqueous solution at -15°C. Compared with reactions at room temperature, a significant yield increasing effect could be established. The kinetic parameters of ester hydrolysis show that most of the unusual acyl donors (compared with the coded phenylalanine methyl ester) are well accepted substrates for α-chymotrypsin.