441353-52-2Relevant academic research and scientific papers
Synthesis, activity and theoretical study of ABT-418 analogues
Avenoza, Alberto,Busto, Jesús H,Cativiela, Carlos,Dordal, Albert,Frigola, Jordi,Peregrina, Jesús M
, p. 4505 - 4511 (2002)
This report shows the synthesis and biological evaluation of two new conformationally restricted ABT-418 analogues. This restriction is introduced by the incorporation of the 7-azabicyclo[2.2.1]heptane skeleton. Furthermore, we report here a high-level qu
Efficient synthesis of a 7-azabicyclo[2.2.1]heptane based GlyT1 uptake inhibitor
Xiong, Hui,Frietze, William,Andisik, Donald W.,Ernst, Glen E.,Palmer, William E.,Hinkley, Lindsay,Varnes, Jeffrey G.,Albert, Jeffrey S.,Veale, Chris A.
scheme or table, p. 6741 - 6744 (2011/02/25)
An efficient synthetic route based on generation and subsequent electrophilic reaction of a Boc-protected azabicyclo[2.2.1]heptane anion to prepare a potent GlyT1 uptake inhibitor (1) is described.
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The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides.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.
