21582-41-2

Basic information

• Product Name: (-)(2S:3R)-2-bromo-3-methyl-valeric acid
• Synonyms: (-)(2S:3R)-2-bromo-3-methyl-valeric acid
• CAS NO: 21582-41-2
• Molecular Weight: 195.056
• Mol File: 21582-41-2.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: (-)(2S:3R)-2-bromo-3-methyl-valeric acid(CAS DataBase Reference)
• NIST Chemistry Reference: (-)(2S:3R)-2-bromo-3-methyl-valeric acid(21582-41-2)
• EPA Substance Registry System: (-)(2S:3R)-2-bromo-3-methyl-valeric acid(21582-41-2)

Safety Data

• Hazardous Substances Data: 21582-41-2(Hazardous Substances Data)

Upstream product

• 73-32-5 L-isoleucine 

Downstream Products

• 319-78-8 D-Isoleucine 
• 1254975-32-0 (2'S,5R)-5-sec-butyl-3-(1'-benzenesulfonylpyrrolidin-2'-yl)-4,5-dihydro-1,2,4-oxadiazin-6-one 
• 1255738-00-1 O-2'-bromo-3'-methylpentanoyl-1-benzenesulfonylpyrrolidine-2-carboxamidoxime 
• 1509-34-8 D-allo-isoleucine 
• 106753-67-7 (R)-3-Methyl-2-[1-phenyl-eth-(E)-ylideneaminooxy]-pentanoic acid 

Relevant articles and documents

α-Aminoxy Oligopeptides: Synthesis, Secondary Structure, and Cytotoxicity of a New Class of Anticancer Foldamers

α-Aminoxy peptides are peptidomimetic foldamers with high proteolytic and conformational stability. To gain an improved synthetic access to α-aminoxy oligopeptides we used a straightforward combination of solution- and solid-phase-supported methods and obtained oligomers that showed a remarkable anticancer activity against a panel of cancer cell lines. We solved the first X-ray crystal structure of an α-aminoxy peptide with multiple turns around the helical axis. The crystal structure revealed a right-handed 28-helical conformation with precisely two residues per turn and a helical pitch of 5.8 ?. By 2D ROESY experiments, molecular dynamics simulations, and CD spectroscopy we were able to identify the 28-helix as the predominant conformation in organic solvents. In aqueous solution, the α-aminoxy peptides exist in the 28-helical conformation at acidic pH, but exhibit remarkable changes in the secondary structure with increasing pH. The most cytotoxic α-aminoxy peptides have an increased propensity to take up a 28-helical conformation in the presence of a model membrane. This indicates a correlation between the 28-helical conformation and the membranolytic activity observed in mode of action studies, thereby providing novel insights in the folding properties and the biological activity of α-aminoxy peptides.

Asymmetric Reduction of Chiral Acetophenone Oxime Ethers to Optically Active Primary Amines

Chiral oxime ethers were synthesized from Na salt of acetophenone oxime and chiral halides, tosylates, or N-tosylaziridines which were derived from β-pinene or α-amino acids.Asymmetric reduction of the chiral oxime ether with LiAlH4 or BH3*THF gave the optically active primary amine.