97611-60-4

Usage

Uses

Used in Pharmaceutical Synthesis:
AMINO-NAPHTHALEN-1-YL-ACETIC ACID is used as a building block for the synthesis of novel drugs, leveraging its chemical properties to create new therapeutic agents that could address various medical conditions.
Used in Research and Development:
In the field of medicinal chemistry, AMINO-NAPHTHALEN-1-YL-ACETIC ACID is used as a research tool for understanding the structure-activity relationships of bioactive compounds, aiding in the design and optimization of more effective pharmaceuticals.
Used in Anti-inflammatory and Analgesic Applications:
Due to its demonstrated potential anti-inflammatory and analgesic effects, AMINO-NAPHTHALEN-1-YL-ACETIC ACID is considered a promising candidate for the development of new therapeutic agents to treat conditions that involve inflammation and pain.
Used in Medical Field Development:
With further research and development, AMINO-NAPHTHALEN-1-YL-ACETIC ACID could lead to the creation of new treatments for a variety of medical conditions, particularly those that benefit from its anti-inflammatory and analgesic properties.

InChI:InChI=1/C12H11NO2/c13-11(12(14)15)10-7-3-5-8-4-1-2-6-9(8)10/h1-7,11H,13H2,(H,14,15)

Upstream product

• 70946-42-8 α-Amino-<1>napthyl-essigsaeure-methylester 
• 37059-68-0 hydroxyimino-[1]naphthyl-acetic acid 
• 95048-05-8 1-naphthaldimine 
• 132-75-2 naphthalen-1-ylacetonitrile 
• 90-11-9 1-Bromonaphthalene 
• 66-77-3 1-naphthaldehyde 
• 113543-62-7 (+/-)-α-Amino-1-naphthaleneacetonitrile 
• 111652-13-2 t-butyl 2-(t-butoxycarbonylamino)-2-(naphth-1-yl)acetate 
• 101004-87-9 (Benzhydrylidene-amino)-naphthalen-1-yl-acetic acid ethyl ester 

Downstream Products

• 146621-91-2 2-(tert-butoxycarbonylamino)-2-(naphthalen-1-yl)acetic acid 
• 95426-07-6 D,L-Benzyloxycarbonylamino--essigsaeure 
• 86217-42-7 2-hydroxy-1-naphthalidene-monoethanolamine 
• 26153-26-4 1-naphthylglyoxylic acid 
• 111820-05-4 (S)-amino(naphthalen-1-yl)acetic acid 
• 1415026-51-5 C₂₁H₁₆N₄OS 

Relevant academic research and scientific papers

TOLL-LIKE RECEPTOR 4 (TLR4) INHIBITORS AND USE THEREOF

Peptides, peptidomimetics and small molecules, collectively referred to as "decoy peptides", are provided, which interfere with binding to a TIR domain of a toll-like receptor 4 (TLR4), and inhibit a TLR4-induced signaling pathway. These decoy peptides may be useful for treating diseases associated with induction of TLR4 signaling pathway such as a disease or disorder secondary to a cardiovascular disease, sepsis or an inflammatory disease.

Structure-based bioisosterism design, synthesis and biological evaluation of novel 1,2,4-triazin-6-ylthioacetamides as potent HIV-1 NNRTIs

The development of new HIV-1 non-nucleoside reverse transcriptase inhibitors (NNRTIs) offers the possibility of generating novel chemical entities of increased potency. Previous investigations in our laboratory resulted in the discovery of several novel series of arylazolylthioacetanilides as potent NNRTIs. In this study, based on the structure-based bioisosterism strategy, novel 1,2,4-triazin-6-yl thioacetamide derivatives were designed, synthesized and evaluated for their anti-HIV activity in MT-4 cells. Among them, the most promising compound was 8b15 with double-digit nanomolar activity against wild-type HIV-1 (EC50 = 0.018 ± 0.007 μM) and moderate activity against the double mutant strain RES056 (EC50 = 3.3 ± 0.1 μM), which indicated that 1,2,4-triazin-6-yl thioacetamide can be used as a novel scaffold to develop a new class of potent NNRTIs active against both wild-type and drug-resistant HIV-1 strains. In addition, preliminary structure-activity relationship (SAR) and molecular modeling results are also briefly discussed, which provide some useful information for the further design of novel NNRTIs.

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.

Inhibitors of phenylalanine ammonialyase: 1-aminobenzylphosphonic acids substituted in the benzene ring

Dextrorotatory 1-amino-3′,4′-dichlorobenzylphosphonic acid was found to be a potent inhibitor of the plant enzyme phenylalanine ammonia-lyase both in vitro and in vivo from among the ring-substituted 1-aminobenzylphosphonic acids and other analogues of phenylglycine. A structure activity relationship analysis of the results obtained permits predictions on the geometry of the pocket of the enzyme and is a basis in the strategy of better inhibitor synthesis.

Highly selective tripeptide thrombin inhibitors

Tripeptide aldehydes such as Boc-D-Phe-Pro-Arg-H (5l) exhibit potent direct inhibition of thrombin. This distinction offers important insight for the design of more potent and selective serine protease inhibitors which may be useful pharmacological tools and hold promise for development of clinically useful agents. The structure-activity relationships (SAR) on a series of anticoagulant peptides with high selectivity for the enzyme thrombin are discussed. The SAR is centered on a series of di- and tripeptide arginine aldehydes based on the structure of 5l. The structural and conformational role of the amino acid residue in position 1 was investigated by substitution with conformationally restricted aromatic amino acids, aromatic acids, and a dipeptide isostere containing the ψ[CH2N] amide bond replacement. Many of these peptides demonstrate potent antithrombotic activity along with selectivity toward thrombin, determined by comparison of in vitro inhibitory effects on trypsin, plasmin, factor Xa, and tissue plasminogen activator. Compound 5f, D-1-Tiq-Pro-Arg-H · sulfate is highly active and the most selective tripeptide aldehyde inhibitor of thrombin reported to date.

NEW SYNTHESES OF α-AMINO ACIDS BASED ON N-ACYLIMINO ACETATES

The reaction of N-acylamino-2-bromoacetates 2 ( via N-acylimino acetates 3 ) with higher order mixed cuprates, trimethylsilyl enol ethers and β-dicarbonyl compounds leads to a variety of α-amino acid derivatives.Their conversion into the free amino acids can be conveniently carried out by the use of t-butyl protection.In case of the N-acetyl compounds cleavage of the protecting group and optical resolution can be achieved in one step hog renal acylase.

The Synthesis of Amino Acids via Organoboranes

The reaction of the acetate (1) with organoboranes provides a convenient, new route to amino acids.

THE SYNTHESIS OF AMINO ACIDS BY REACTION OF AN ELECTROPHILIC GLYCINE CATION EQUIVALENT WITH CARBON NUCLEOPHILES

Acetate 1, a glycine cation equivalent, is reacted with organocopper reagents to yield products 2 which can readily be converted to the higher amino acids.This method provides access to aryl-substituted amino acids as well as amino acids containing a β-tertiary carbon.