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Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.
- Source :
-
The Journal of organic chemistry [J Org Chem] 2013 Dec 20; Vol. 78 (24), pp. 12351-61. Date of Electronic Publication: 2013 Dec 05. - Publication Year :
- 2013
-
Abstract
- 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.
Details
- Language :
- English
- ISSN :
- 1520-6904
- Volume :
- 78
- Issue :
- 24
- Database :
- MEDLINE
- Journal :
- The Journal of organic chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 24303945
- Full Text :
- https://doi.org/10.1021/jo401501g