7758-42-1

Usage

Structure

A naphthalene molecule attached to an alanine amino acid residue.

Usage

Commonly used in the synthesis of peptides and proteins for research purposes.

Photophysical properties

Exhibits interesting photophysical properties, useful in the development of materials for organic electronics and photonics.

Therapeutic potential

Studied for its potential therapeutic applications, particularly in the treatment of metabolic disorders and neurodegenerative diseases.

Scientific value

Serves as a valuable tool for scientists and researchers in various fields, contributing to advancements in both fundamental science and practical applications.

Upstream product

• 102241-41-8 5-[1]naphthylmethylene-3-p-tolyl-imidazolidine-2,4-dione 
• 143218-06-8 2-acetylamino-2-cyano-3-[1]naphthyl-propionic acid ethyl ester 
• 86-52-2 1-Chloromethylnaphthalene 
• 125700-36-9 2-Amino-3-naphthalen-1-yl-propionic acid ethyl ester; hydrochloride 
• 66-77-3 1-naphthaldehyde 
• 59759-78-3 2-benzoylamino-3-naphthalen-1-yl-propionic acid 
• 28095-56-9 2-amino-3-(1-naphthyl)propanoic acid 
• 5440-57-3 diethyl (N-acetylamino)[(1-naphthyl)methyl]malonate 
• 939-26-4 2-bromomethylnaphthyl bromide 
• 59759-53-4 DL-N-Benzoyl-η-1-naphthyl-alaninamid 
• 157521-32-9 acetylamino-[1]naphthylmethyl-malonic acid 
• 57427-83-5 4-naphthalen-1-ylmethylene-2-phenyl-4H-oxazol-5-one 
• 3163-27-7 2-(bromomethyl)naphthalene 
• 125761-75-3 2-Acetylamino-3-naphthalen-1-yl-propionic acid ethyl ester 

Downstream Products

• 108327-31-7 α-(((Phenylmethoxy)carbonyl)amino)-1-naphthalenepropanoic acid 
• 62741-58-6 3-(naphthalene-1-yl)-2-oxopropanoic acid 
• 55516-54-6 L-1-naphthylalanine 
• 136375-70-7 naphythylalanine methylester 
• 223771-37-7 D-3-(1-naphthyl)alanine methylester 
• 1562416-37-8 N-benzoyl-L-β-(1-napthyl)alanine methyl ester 
• 1562416-38-9 C₂₁H₁₉NO₃ 
• 123760-85-0 2-(4-Chloro-benzylamino)-3-naphthalen-1-yl-propionic acid 
• 119357-91-4 (S)-1-naphthylalanine methyl ester 

Relevant academic research and scientific papers

In vitro evolution of an l-amino acid deaminase active on l-1-naphthylalanine

l-Amino acid deaminase from Proteus myxofaciens (PmaLAAD) is a promising biocatalyst for enantioselective biocatalysis that can be exploited to produce optically pure d-amino acids or α-keto acids. In this study, we improved the catalytic efficiency of PmaLAAD on l-1-naphthylalanine (l-1-Nal), a synthetic amino acid of biotechnological interest. Eight evolvable positions were identified by a molecular docking and evolutionary conservation analysis. These positions were subjected to site-saturation mutagenesis, producing smaller but smarter libraries of variants. The best variant (F318A/V412A/V438P PmaLAAD) possesses a ～5-fold lower Km (0.17 mM) and a ～7-fold higher catalytic efficiency (9.2 s-1 mM-1) on l-1-Nal than the wild-type enzyme. Molecular docking analysis suggests that the substitutions increase the active site volume, allowing better binding of the bulky l-1-Nal substrate. Bioconversion reactions showed that the F318A/V412A/V438P PmaLAAD variant outperforms the wild-type enzyme in the deracemization of d,l-1-Nal: the complete conversion of 0.6 mM of the l-enantiomer was achieved in about 15 min, which is ～7.5-fold faster than the wild-type enzyme. In addition, the F318A/V412A/V438P PmaLAAD is efficiently employed, together with the M213G d-amino acid oxidase variant, to produce 1-naphtylpyruvate from racemic d,l-1-Nal in one pot.

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.).

COMPOSITIONS AND METHODS FOR CYCLOFRUCTANS AS SEPARATION AGENTS

The present invention relates to derivatized cyclofructan compounds, compositions comprising derivatized cyclofructan compounds, and methods of using compositions comprising derivatized cyclofructan compounds for chromatographic separations of chemical species, including enantiomers. Said compositions may comprise a solid support and/or polymers comprising derivatized cyclofructan compounds.

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.

Asymmetric synthesis of (S)-2-amino-3-(1-naphthyl)propanoic acid via chiral nickel complex. Crystal structure, circular dichroism, 1H and 13C NMR spectra of the complex

The recently published environmentally friendly preparation of a glycine synthon 2 from regeneratable chiral auxiliary BPB ((S)-N-(2-benzoylphenyl)- N′-benzylprolinamide) was used for preparative asymmetric synthesis of the non-coded amino acid 3-(1-naphthyl)alanine (1). Full assignment of 1H and 13C NMR of both intermediate complex 3 and 1 and X-ray structure determination of complex 3 were made. Cotton effects observed in circular dichroism spectrum of complex 3 are consistent with published empirical rules.

Chiral salen-metal complexes as novel catalysts for the asymmetric synthesis of α-amino acids under phase transfer catalysis conditions

Chiral salen-metal complexes have been tested as catalysts for the C-alkylation of Schiff's bases of alanine and glycine esters with alkyl bromides under phase-transfer conditions (solid sodium hydroxide, toluene, ambient temperature, 1-10 mol% of the catalyst). The best catalyst, which was derived from a Cu(II) complex of (1R, 2R or 1S,2S)-[N,N′-bis(2′-hydroxybenzylidene)]-1,2-diaminocyclohexane, gave α-amino and α-methyl-α-amino acids with enantiomeric excesses of 70-96%.

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.

Benzo-fused lactams

Compounds of the formula STR1 wherein A is STR2 are useful as ACE and NEP inhibitors and those wherein A is STR3 are useful as ACE inhibitors. Methods of preparation and intermediates are also disclosed.

SUBSTITUTED AZEPINONE DUAL INHIBITORS OF ANGIOTENSIN CONVERTING ENZYME AND NEUTRAL EXDOPEPTIDASE

Compounds of the formula STR1 are disclosed as possessing inhibitory activity against angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) and thus being useful as cardiovascular agents. Processes for preparing these compounds are also disclosed.

COMPOUNDS CONTAINING A FUSED BICYCLE RING AND PROCESSES THEREFOR

Compounds of the formula STR1 wherein X is O or S--(O) t ; n is one or two; m is zero or one; Y is CH 2, O, or S--(O) t provided that Y is O or S--(O) t only when m is one; and A is STR2 are dual inhibitors of NEP and ACE. Compounds wherein A is STR3 are selective ACE inhibitors. Also disclosed are methods of preparation and intermediates.