37784-23-9Relevant academic research and scientific papers
O-Benzyl derivatives of (S)-(+) and (R)-(-)-2-aminobutan-1-ol as new resolving agents for racemic acids. Practical resolutions of N-acyl derivatives of phenylglycine and 4-hydroxyphenylglycine
Touet, Joel,Faveriel, Laurent,Brown, Eric
, p. 2957 - 2960 (2007/10/02)
Treatment of the readily available (S)-(+) and (R)-(-)-2-aminobutan-1-ol 1 with sodium hydride followed by benzyl chloride, or a substituted benzyl halide, afforded the corresponding O-benzyl bases 2-5 in high yields. These new bases are recommended for the large scale resolution of racemic acids. For instance, they proved efficient for the practical resolution of N-acetylphenylglycine (±)-7, N-acetyl-(4-hyroxylphenyl)glycine (±)-9 and N-chloroacetyl-(4-hydroxyphenyl) glycine (±)-10.
Racemization of Optically Active Aromatic N-Acetylamino Acids and Asymmetric Transformation of N-Acetyl-2-(4-hydroxyphenyl)glycine via Salt Formation with Optically Active α-Methylbenzylamine
Shiraiwa, Tadashi,Sakata, Shinji,Natsuyama, Hisashi,Fujishima, Keiko,Miyazaki, Hideya,et al.
, p. 965 - 970 (2007/10/02)
The racemization rates of N-acetyl-(S)-tyrosine, N-acetyl-(S)-phenylalanine, N-acetyl-(R)-2-(4-hydroxyphenyl)glycine , N-acetyl-(R)-2-phenylglycine, and N-acetyl-(S)-alanine were measured by use of (RS)-α-methylbenzylamine as base-catalyst.The first-order rate constant for racemization tended to increase with an increase in the polar substituent constant of the N-acetylamino acid side chain.The racemization appeared to be subject to the inductive effect by the side chain.An asymmetric transformation of (RS)-AcHpg by using (R)-MBA, based on the result of racemization, gave an optically pure salt of (R)-AcHpg with (R)-MBA by successive use of the filtrate as the solvent.Optically pure (R)-2-(4-hydroxyphenyl)glycine was separated from the salt in 87-90percent yield based on the starting (RS)-AcHpg.In addition, the asymmetric transformation of (R)-AcHpg was achieved by using (S)-MBA to give optically pure (S)-Hpg in 80percent yield after purification of the salt of (S)-AcHpg with (S)-MBA followed by hydrolysis.
Inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cells by the peptides related to bacterial cell wall mucopeptide precursors: Quantitative structure-activity relationships
Kim,Martin,Otis,Mao
, p. 84 - 93 (2007/10/02)
Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cell wall have been developed to probe the details of the binding between ristocetin and N-acetylated peptides. The correlation equations indicate that (1) the binding is stronger for peptides in which the side chain of the C-terminal amino acid has a large molar refractivity (MR) value, (2) the binding is weaker for peptides with polar than for those with nonpolar C-terminal side chains, (3) the N-terminal amino acid in N-Ac dipeptides contributes 12 times that of the C-terminal amino acid to binding affinity, and (4) the interactions between ristocetin and the N-terminal amino acid of N-acetyl tripeptides appear to be much weaker than those with the first two amino acids.
