79807-13-9Relevant articles and documents
Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C
Makowski, Maciej,Lenartowicz, Pawe?,Oszywa, Bartosz,Jewgiński, Micha?,Pawe?czak, Ma?gorzata,Kafarski, Pawe?
, p. 3157 - 3165 (2015)
The procedures for the synthesis of esters of dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine have been elaborated. These esters appeared to be moderate or weak inhibitors of cathepsin C, with some of them exhibiting slow
An improved procedure for the synthesis of dehydroamino acids and dehydropeptides from the carbonate derivatives of serine and threonine using tetrabutylammonium fluoride
Ramapanicker, Ramesh,Mishra, Roli,Chandrasekaran, Srinivasan
experimental part, p. 123 - 125 (2011/02/24)
Dehydroamino acids are important precursors for the synthesis of a number of unnatural amino acids and are structural components in many biologically active peptide derivatives. However, efficient synthetic procedures for their production in large amounts
An efficient synthesis of dehydroamino acids and dehydropeptides from O-Cbz and O-Eoc derivatives of serine and threonine
Ramesh, Ramapanicker,De, Kavita,Chandrasekaran, Srinivasan
, p. 10534 - 10542 (2008/02/13)
A simple and efficient method for the synthesis of dehydroamino acids from serine and threonine is reported. Various O-Cbz and O-Eoc derivatives of serine and threonine are prepared using CbzCl and EocCl, respectively, and are subjected to an anti-selective elimination on treatment with K2CO3 in DMF at 65 °C to afford dehydroalanine and dehydroamino butyric acid derivatives, respectively, in excellent yields. The high stability of these carbonate derivatives of serine and threonine allows their use in normal peptide synthesis as protected serine and threonine residues. Peptides synthesized by incorporating O-Cbz or O-Eoc derivatives undergo ready elimination under the reported conditions, to give the corresponding dehydropeptides in excellent yields. The reaction conditions are mild enough not to cause the racemization of other stereogenic centers present in the peptide.