23635-30-5Relevant articles and documents
Synthesis and study of 2-acetyl amino-3-[4-(2-amino-5-sulfo-phenylazo)- phenyl]-propionic acid: A new class of inhibitor for hen egg white lysozyme amyloidogenesis
Maity, Sibaprasad,Kumar, Ravi,Maity, Suman Kumar,Jana, Poulami,Bera, Santu,Haldar, Debasish
, p. 530 - 536 (2013/05/22)
The compounds capable of blocking the aggregation of amyloidogenic proteins may have therapeutic potentials. We report on the synthesis of 2-acetyl amino-3-[4-(2-amino-5-sulfo-phenylazo)-phenyl]-propionic acid as an HEWL (hen egg white lysozyme) amyloid inhibitor starting from phenylalanine. The compounds arrest the monomers and exhibit anti-aggregating activity. Moreover, the acetyl derivative 1 served as a better inhibitor than the trifluoroacetyl derivative 2 against in vitro amyloid fibrillogenesis of the HEWL model system.
Biotransformations in low-boiling hydrofluorocarbon solvents
Saul, Simon,Corr, Stuart,Micklefield, Jason
, p. 5519 - 5523 (2007/10/03)
Solvent solutions: Low-boiling hydrofluorocarbons (see examples) are excellent solvents for lipase-catalyzed reactions and ideal replacements for conventional organic solvents and supercritical fluids as media for nonaqueous biotransformations. Notably increased rates, yields, and enantioselectivities were observed with the model kinetic resolution of (±)-1-phenylethanol and the desymmetrization of weso-2-cyclopentene-1 ,4-diol.
Use of N-trifluoroacetyl-protected amino acid chlorides in peptide coupling reactions with virtually complete preservation of stereochemistry
Jass, Paul A.,Rosso, Victor W.,Racha, Saibaba,Soundararajan, Nachimuthu,Venit, John J.,Rusowicz, Andrew,Swaminathan, Shankar,Livshitz, Julia,Delaney, Edward J.
, p. 9019 - 9029 (2007/10/03)
The use of protected amino acid chlorides for peptide coupling reactions has long been avoided due to the extensive racemization that commonly occurs during either the acid chloride formation or the coupling reaction itself. Conditions are described which