1098-50-6

Basic information

• Product Name: DANSYL-L-VALINE
• Synonyms: (S)-2-[[[5-(Dimethylamino)-1-naphthalenyl]sulfonyl]amino]-3-methylbutyric acid;N-[[5-(Dimethylamino)-1-naphthalenyl]sulfonyl]-L-valine;N-[5-(Dimethylamino)-1-naphtylsulfonyl]-L-valine;N-[5-(Dimethylamino)-1-naphtylsulfonyl]valine;N-Dns-L-Valine;5-Dimethylaminonaphthalene-1-sulfonyl-L-valine Dns-Val-OH;Dansyl-L-valine;DANSYL-L-VALINE
• CAS NO: 1098-50-6
• Molecular Formula: C₁₇H₂₂N₂O₄S
• Molecular Weight: 350.43
• Product Categories: Dansyl Amino Acids;Amino Acids;Amino Acids (N-Protected);Biochemistry
• Mol File: 1098-50-6.mol
• Article Data: 6

Chemical Properties

• Melting Point: 140 °C
• Boiling Point: 536.2±60.0 °C(Predicted)
• Appearance: /
• Density: 1.281±0.06 g/cm3(Predicted)
• Refractive Index: 19.5 ° (C=1, MeOH)
• PKA: 3.32±0.10(Predicted)
• CAS DataBase Reference: DANSYL-L-VALINE(CAS DataBase Reference)
• NIST Chemistry Reference: DANSYL-L-VALINE(1098-50-6)
• EPA Substance Registry System: DANSYL-L-VALINE(1098-50-6)

Safety Data

• Hazardous Substances Data: 1098-50-6(Hazardous Substances Data)

Usage

General Description

DANSYL-L-VALINE is a fluorescent amino acid derivative that is commonly used in biochemistry and chemical biology research. It is a synthetic compound that consists of a dansyl fluorophore attached to the amino acid L-valine. The fluorescent properties of DANSYL-L-VALINE make it useful for studying protein structure, dynamics, and interactions, as well as for monitoring enzymatic reactions and peptide synthesis. Its unique structure allows for easy detection and quantification using fluorescence spectroscopy, making it a valuable tool in a variety of biological and chemical applications.

Upstream product

• 42808-05-9 dansyl-valine 
• 72-18-4 L-valine 
• 605-65-2 5-(dimethylamino)naphth-1-ylsulfonyl chloride 
• 516-06-3 D,L-valine 

Downstream Products

• 270072-24-7 (S)-2-[Benzyl-(5-dimethylamino-naphthalene-1-sulfonyl)-amino]-3-methyl-butyric acid 

Relevant articles and documents

Yaku'amides A and B, cytotoxic linear peptides rich in dehydroamino acids from the marine sponge ceratopsion sp.

Two cytotoxic peptides, yaku'amides A (1) and B (2), were isolated from the marine sponge Ceratopsion sp. Their planar structures were elucidated on the basis of spectroscopic data, whereas the absolute configurations were determined by a combination of the Marfey's analysis and dansylation analysis of the total and partial acid hydrolysis products. The growth inhibitory profile of yaku'amide A against a panel of 39 human cancer cell lines was clearly unique and distinguished from other anticancer drugs.

A new chiral ligand exchange capillary electrophoresis system based on Zn(ii)-l-leucine complexes coordinating with β-cyclodextrin and its application in screening tyrosinase inhibitors

Tyrosinase plays a key role in melanin formation, and it is closely related to hyper pigmentation in animals and enzymatic browning in food. Thus, it is of great significance to screen inhibitors of tyrosinase. In this work, a new chiral ligand exchange-capillary electrophoresis (CLE-CE) system based on the coordination effect of Zn(ii)-l-leucine complexes and β-cyclodextrin (β-CD) was developed for screening the inhibitors of tyrosinase. The effects of the concentration of β-CD, buffer pH, the ratio of l-leucine to Zn(ii), and the complex concentration were investigated with Dns-d,l-tyrosine, Dns-d,l-valine and Dns-d,l-phenylalanine as the tested analytes. The optimum buffer conditions were composed of 100.0 mM boric acid, 5.0 mM ammonium acetate, 3.0 mM Zn(ii), 6.0 mM l-leucine and 4.0 mM β-CD at pH 8.2. It has been found that six pairs of Dns-d,l-AAs could be baseline-separated and five pairs of Dns-d,l-AAs were partly enantioseparated. Then the quantitative analysis of l-tyrosine was conducted and good linearity (r2 = 0.992) was obtained with a concentration ranging from 12.95 μM to 413.3 μM. A kinetics study of tyrosinase was realized, and the Km and Vmax were 636 μM and 312 μmol min-1 mg-1. Moreover, the proposed method was applied in screening the inhibitors of tyrosinase with four kinds of chalcones as the model inhibitors. The results demonstrated that the developed CLE-CE system was favorable for screening enzyme inhibitors, and showed great potential in related drugs discovery and clinical analysis in the future.

Chiral separation of enantiomers of amino acid derivatives by HPLC on vancomycin and teicoplanin chiral stationary phases

The chiral separation of α-amino acids by liquid chromatography using macrocyclic antibiotic bonded stationary phases were studied. Teicoplanin and vancomycin bonded stationary phases have been used to separate enantiomers of dansyl amino acids in the reversed - phase high performance liquid chromatography mode. By comparison of chromatographic parameters obtained by use of both chiral stationary phases it the mechanism of chiral separation could be suggested. The better separation - greater value of R(j,i) of enantiomers - was achieved by the teicoplanin column.