149832-22-4Relevant academic research and scientific papers
Phenylalanine and Phenylglycine Analogues as Arginine Mimetics in Dengue Protease Inhibitors
Weigel, Lena F.,Nitsche, Christoph,Graf, Dominik,Bartenschlager, Ralf,Klein, Christian D.
, p. 7719 - 7733 (2015/10/20)
Dengue virus is an increasingly global pathogen. One of the promising targets for antiviral drug discovery against dengue and related flaviviruses such as West Nile virus is the viral serine protease NS2B-NS3. We here report the synthesis and in vitro characterization of potent peptidic inhibitors of dengue virus protease that incorporate phenylalanine and phenylglycine derivatives as arginine-mimicking groups with modulated basicity. The most promising compounds were (4-amidino)-l-phenylalanine-containing inhibitors, which reached nanomolar affinities against dengue virus protease. The type and position of the substituents on the phenylglycine and phenylalanine side chains has a significant effect on the inhibitory activity against dengue virus protease and selectivity against other proteases. In addition, the non-natural, basic amino acids described here may have relevance for the development of other peptidic and peptidomimetic drugs such as inhibitors of the blood clotting cascade.
Genotoxic activity of halogenated phenylglycine derivatives
Boto, Alicia,Gallardo, Juan A.,Hernandez, Rosendo,Ledo, Francisco,Munoz, Ana,Murguia, Jose R.,Menacho-Marquez, Mauricio,Orjales, Aurelio,Saavedra, Carlos J.
, p. 6073 - 6077 (2008/12/22)
The discovery of genotoxic amino acids derived from phenylglycine, and posessing halogen substituents, is described. The utility of hypervalent iodine reagents in the synthesis of this class of compounds is highlighted. The mechanism of action of the (hal
Enzymatic Asymmetric Synthesis of α-Amino Acids. Enantioselective Cleavage of 4-Substituted Oxazolin-5-ones and Thiazolin-5-ones
Crich, Joyce Z.,Brieva, Rosario,Marquart, Peer,Gu, Rui-Lin,Flemming, Steffen,Sih, Charles J.
, p. 3252 - 3258 (2007/10/02)
A general enzymatic asymmetric synthesis of L-α-amino acids has been developed.This method entails the use of the Pseudomonas cepacia lipase (P-30) to catalyze the enantioselective methanolysis of a variety of 4-substituted 2-phenyloxazolin-5-one derivatives in a nonpolar organic solvent to furnish optically active N-benzoyl-L-α-amino acid methyl esters (ee = 66-98 percent), which in turn is subjected to a protease-catalyzed kinetic resolution yielding enantiomerically pure N-benzoyl-L-α-amino acids.This synergistic coupling of two enzymes allows the ready preparation of L-α-amino acids of high enantiopurity in yields greater than 50 percent, an inherent advantage over conventional resolution procedures.Two proteases were found to catalyze the enantioselective hydrolysis of a variety of 4-substituted 2-phenylthiazolin-5-one derivatives to give N-(thiobenzoyl)-L-α-amino acids of high optical purity.
