34078-88-1Relevant articles and documents
Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to ester interconversion
Nuijens, Timo,Piva, Elena,Kruijtzer, John A. W.,Rijkers, Dirk T. S.,Liskamp, Rob M. J.,Quaedflieg, Peter J. L. M.
experimental part, p. 1039 - 1044 (2011/07/09)
Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required and racemisation does not occur rendering purification easier compared to chemical peptide synthesis. In this paper, a novel interconversion reaction of peptide C-terminal α-carboxamides into primary alkyl esters with alcalase was used to develop a fully enzymatic peptide synthesis strategy. For each elongation step a cost-efficient amino acid carboxamide building block was used followed by the interconversion of the elongated peptide carboxamide to the corresponding primary alkyl ester. These peptide esters are the starting materials for the next enzymatic peptide elongation step. Copyright
General and versatile approach to the synthesis of optically active 5-alkylpiperazine-2-carboxylic acids
Falorni,Giacomelli,Satta,Cossu
, p. 391 - 395 (2007/10/02)
General and convenient syntheses of optically active 5-alkylpiperazine-2-carboxylic acids are described. The methods are based on cyclization of L- or D-serine with α-amino acids and occur without loss of optical purity. The presented procedures are based
A short, stereospecific synthesis of dihydrooxazoles from serine and threonine derivatives
Wipf, Peter,Miller, Chris P.
, p. 907 - 910 (2007/10/02)
Cyclization of serine and threonine derivatives with Burgess reagent provides a one-step, streospecific access to 4,5-dihydrooxazoles. Noteworthy features of this new methodology include mild experimental conditions, and the absence of β-lactam, aziridine
