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.
We report the asymmetric synthesis of the γ-amino acid (1R,2R)-2-aminomethyl-1-n class="Chemical">cyclopentanecarboxylic 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.
Authors: Łukasz Berlicki; Ludwig Pilsl; Edit Wéber; István M Mándity; Chiara Cabrele; Tamás A Martinek; Ferenc Fülöp; Oliver Reiser Journal: Angew Chem Int Ed Engl Date: 2012-01-26 Impact factor: 15.336
Authors: István M Mándity; Edit Wéber; Tamás A Martinek; Gábor Olajos; Gábor K Tóth; Elemér Vass; Ferenc Fülöp Journal: Angew Chem Int Ed Engl Date: 2009 Impact factor: 15.336
Authors: Young-Hee Shin; David E Mortenson; Kenneth A Satyshur; Katrina T Forest; Samuel H Gellman Journal: J Am Chem Soc Date: 2013-05-23 Impact factor: 15.419