3967-18-8Relevant academic research and scientific papers
Synthesis and application of an Nδ-acetyl-N δ-hydroxyornithine analog: Identification of novel metal complexes of deferriferrichrysin
Kobayashi, Kazuya,Oishi, Shinya,Kobayashi, Yuka,Ohno, Hiroaki,Tsutsumi, Hiroko,Hata, Yoji,Fujii, Nobutaka
scheme or table, p. 2651 - 2655 (2012/06/01)
Synthesis of Fmoc-protected Nδ-acetyl-N δ-(tert-butoxy)-l-ornithine has revealed it to be a metal-chelating amino-acid precursor. This protected amino acid was compatible with the preparation of ferrichrome peptides by standard Fmoc-
Enzymatic removal of carboxyl protecting groups. 2. Cleavage of the benzyl and methyl moieties
Barbayianni, Efrosini,Fotakopoulou, Irene,Schmidt, Marlen,Constantinou-Kokotou, Violetta,Bornscheuer, Uwe T.,Kokotos, George
, p. 8730 - 8733 (2007/10/03)
Enzymes are versatile reagents for the efficient removal of methyl and benzyl protecting groups. An esterase from Bacillus subtilis (BS2) and a lipase from Candida antarctica (CAL-A) allow a mild and selective removal of these moieties in high yields without affecting other functional groups.
2-Phenyl isopropyl and t-butyl trichloroacetimidates: Useful reagents for ester preparation of N-protected amino acids under neutral conditions
Thierry, Josiane,Yue, Chongwei,Potier, Pierre
, p. 1557 - 1560 (2007/10/03)
2-Phenylisopropyl and t-butyl trichloroacetamidates 1 and 2 are useful reagents for the esterification of N-protected aminoacids under mild neutral conditions. In the case of hydroxyl-containing amino acids dialkylation occurs but no selectivity could be obtained.
