1292320-85-4Relevant academic research and scientific papers
Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure
Giuliano, Michael W.,Maynard, Stacy J.,Almeida, Aaron M.,Reidenbach, Andrew G.,Guo, Li,Ulrich, Emily C.,Guzei, Ilia A.,Gellman, Samuel H.
, p. 12351 - 12361 (2014/01/17)
We report the asymmetric synthesis of the γ-amino acid (1R,2R)-2-aminomethyl-1-cyclopentane carboxylic acid (AMCP) and an evaluation of this residue's potential to promote secondary structure in α/γ- peptides. Simulated annealing calculations using NMR-derived distance restraints obtained for α/γ-peptides in chloroform reveal that AMCP-containing oligomers are conformationally flexible. However, additional evidence suggests that an internally hydrogen-bonded helical conformation is partially populated in solution. From these data, we propose characteristic NOE patterns for the formation of the α/γ-peptide 12/10-helix and discuss the apparent conformational frustration of AMCP-containing oligomers.
GAMMA AMINO ACID BUILDING BLOCKS
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, (2011/05/05)
The invention provides compounds and methods, for example, to carry out organocatalytic Michael additions of aldehydes to cyclically constrained nitroethylene compounds catalyzed by a pro line derivative to provide cyclically constrained α-substituted-γ-n
