90013-41-5Relevant academic research and scientific papers
Incorporation of Ahc into model dipeptides as an inducer of a β-turn with a distorted amide bond. Conformational analysis
Avenoza, Alberto,Busto, Jesus H.,Peregrina, Jesus M.,Rodriguez, Fernando
, p. 4241 - 4249 (2007/10/03)
The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides. The conformational analysis of the new peptides in the solid state revealed that the Ahc-Ser sequence displays a type I β-turn, which includes a distorted amide bond. In contrast, the Ser-Ahc sequence exists in a nonfolded structure.
Synthesis and Structure of Cyclic Phosphopeptides Containing a Phosphodiester Linkage
Oijen, Anita H.,Behrens, Stefan,Mierke, Dale F.,Kessler, Horst,Boom, Jacques H. van,Liskamp, Rob M. J.
, p. 3722 - 3730 (2007/10/02)
The synthesis of three cyclic phosphopeptides, which contain a phosphodiester linkage, is described.Starting from either Boc-L-Ser(OBn)-OH or Boc-L-Thr(OBn)-OH, three precursors for the macrocyclization by phosphitylation were prepared.After phosphitylati
