5362-00-5

Basic information

• Product Name: 2-AcetaMido-2-Methylpropanoic acid
• Synonyms: 2-AcetaMido-2-Methylpropanoic acid;2-acetamido-2-methyl-propionic acid
• CAS NO: 5362-00-5
• Molecular Formula: C₆H₁₁NO₃
• Molecular Weight: 145.15644
• Mol File: 5362-00-5.mol
• Article Data: 9

Chemical Properties

• Melting Point: 195-196 °C
• Boiling Point: 357.4°C at 760 mmHg
• Flash Point: 169.9°C
• Appearance: /
• Density: 1.132g/cm³
• Vapor Pressure: 4.51E-06mmHg at 25°C
• Refractive Index: 1.458
• Storage Temp.: 2-8°C
• PKA: 3.78±0.10(Predicted)
• CAS DataBase Reference: 2-AcetaMido-2-Methylpropanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-AcetaMido-2-Methylpropanoic acid(5362-00-5)
• EPA Substance Registry System: 2-AcetaMido-2-Methylpropanoic acid(5362-00-5)

Safety Data

• Hazardous Substances Data: 5362-00-5(Hazardous Substances Data)

Usage

General Description

2-Acetamido-2-methylpropanoic acid is a synthetic compound that belongs to the class of organic compounds known as alpha amino acids. It is derived from the amino acid valine and is commonly used in the pharmaceutical and biotechnology industries. This chemical compound is also known as N-acetylvaline and is used as a building block in the synthesis of various drugs, such as the anti-inflammatory and analgesic drug nimesulide. Additionally, it has been studied for its potential antitumor and anti-metastatic properties, making it a subject of interest for researchers in the field of cancer treatment.

InChI:InChI=1/C6H11NO3/c1-4(8)7-6(2,3)5(9)10/h1-3H3,(H,7,8)(H,9,10)

Upstream product

• 75-05-8 acetonitrile 
• 595-46-0 2,2-dimethylmalonic acid 
• 118724-99-5 α-<(acetyl-α-aminoisobutanoyl)amino>-isobutanoic acid 
• 7732-18-5 water 
• 114983-62-9 N-Formyl-N-acetyl-α-methylalanin-essigsaeure-anhydrid 
• 64-19-7 acetic acid 
• 62-57-7 2-Aminoisobutyric acid 
• 108-24-7 acetic anhydride 
• 40652-06-0 N-(1-cyano-1-methyl-ethyl)acetamide 

Downstream Products

• 17582-78-4 N-(2-methyl-1-oxo-1-phenylpropan-2-yl)acetamide 
• 43135-06-4 Ac-Aib-OMe 
• 76718-72-4 2-[4-(alpha-acetamidoisobutyrylamino)phenyl]-4-hydroxy-5-pyrimidine carboxylic acid 

Relevant articles and documents

AZETIDIN-3-YLMETHANOL DERIVATIVES AS CCR6 RECEPTOR MODULATORS

The present invention relates to compounds of Formula (I), their synthesis and use as CCR6 receptor modulators for the treatment or prevention of various diseases, conditions or disorders.

Bio- And Medicinally Compatible α-Amino-Acid Modification via Merging Photoredox and N-Heterocyclic Carbene Catalysis

An N-heterocyclic carbene and photoredox cocatalyzed α-amino-acid decarboxylative carbonylation reaction is presented. This method displays good scope generality, providing a direct pathway to access various downstream α-amino ketones under bio- and medicinally compatible conditions. Moreover, this strategy is appealing to chemical biology because it has great potential for the chemical modification of peptides or the late-stage synthesis of keto-peptides.

Conformational manifold of α-aminoisobutyric acid (Aib) containing alanine-based tripeptides in aqueous solution explored by vibrational spectroscopy, electronic circular dichroism spectroscopy, and molecular dynamics simulations

Replacement of the α-proton of an alanine residue to generate α-aminoisobutyric acid (Aib) in alanine-based oligopeptides favors the formation of a 310 helix when the length of the oligopeptide is about four to six residues. This research was aimed at experimentally identifying the structural impact of an individual Aib residue in an alanine context of short peptides in water and Aib's influence on the conformation of nearest-neighbor residues. The amide I band profile of the IR, isotropic and anisotropic Raman, and vibrational circular dichroism (VCD) spectra of Ac-Ala-Ala-Aib-OMe, Ac-Ala-Aib-Ala-OMe, and Ac-Aib-Ala-Ala-OMe were measured and analyzed in terms of different structural models by utilizing an algorithm that exploits the excitonic coupling between amide I′ modes. The conformational search was guided by the respective 1H NMR and electronic circular dichroism spectra of the respective peptides, which were also recorded. From these analyses, all peptides adopted multiple conformations. Aib predominantly sampled the right-handed and left-handed 310-helix region and to a minor extent the bridge region between the polyproline (PPII) and the helical regions of the Ramachandran plot. Generally, alanine showed the anticipated PPII propensity, but its conformational equilibrium was shifted towards helical conformations in Ac-Aib-Ala-Ala-OMe, indicating that Aib can induce helical conformations of neighboring residues positioned towards the C-terminal direction of the peptide. An energy landscape exploration by molecular dynamics simulations corroborated the results of the spectroscopic studies. They also revealed the dynamics and pathways of potential conformational transitions of the corresponding Aib residues.