1100-23-8 Usage
Description
Dansyl-L-asparagine is a fluorescently labeled amino acid that is commonly used in the study of proteins and peptides. It is derived from asparagine, an essential amino acid, and is modified with a dansyl group, which imparts fluorescent properties to the molecule. This modification allows for the tracking and analysis of proteins and peptides in various experimental settings.
Uses
Used in Biochemistry Research:
Dansyl-L-asparagine is used as a fluorescent probe for studying protein structure, function, and interactions. The fluorescent properties of the dansyl group enable researchers to monitor protein folding, conformational changes, and binding events in real-time, providing valuable insights into protein behavior and mechanisms.
Used in Peptide Synthesis:
Dansyl-L-asparagine is used as a building block in the synthesis of fluorescent peptides. The incorporation of this labeled amino acid into peptide sequences allows for the tracking and analysis of peptide behavior in biological systems, including their stability, localization, and interactions with other molecules.
Used in Drug Discovery:
Dansyl-L-asparagine is used as a tool in the development of new drugs targeting specific proteins or peptides. The fluorescent properties of the dansyl group facilitate the screening of potential drug candidates for their ability to bind to and modulate the activity of target proteins or peptides, accelerating the drug discovery process.
Used in Analytical Techniques:
Dansyl-L-asparagine is used in various analytical techniques, such as high-performance liquid chromatography (HPLC) and capillary electrophoresis (CE), for the separation and detection of proteins and peptides. The fluorescent signal provided by the dansyl group enhances the sensitivity and selectivity of these methods, allowing for the accurate quantification and identification of protein and peptide samples.
Check Digit Verification of cas no
The CAS Registry Mumber 1100-23-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,1,0 and 0 respectively; the second part has 2 digits, 2 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 1100-23:
(6*1)+(5*1)+(4*0)+(3*0)+(2*2)+(1*3)=18
18 % 10 = 8
So 1100-23-8 is a valid CAS Registry Number.
InChI:InChI=1/C16H19N3O5S/c1-19(2)13-7-3-6-11-10(13)5-4-8-14(11)25(23,24)18-12(16(21)22)9-15(17)20/h3-8,12,18H,9H2,1-2H3,(H2,17,20)(H,21,22)
1100-23-8Relevant articles and documents
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
Su, Yuan,Mu, Xiaoyu,Qi, Li
, p. 55280 - 55285 (2015/02/05)
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.
