ArticleThe Journal of organic chemistry2013
Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.
Article in The Journal of organic chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Reprogramming the genetic code with flexizymes.Nature reviews. Chemistry · 2024Review
- Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides.Communications chemistry · 2024Article
- Translation initiation with exotic amino acids using EF-P-responsive artificial initiator tRNA.Nucleic acids research · 2023Article
- In vitro selection of macrocyclic peptide inhibitors containing cyclic γNature chemistry · 2023Article
- Synthesis of hybrid hydrazino peptides: protected vs unprotected chiral α-hydrazino acids.SpringerPlus · 2015Article
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Authors and funding
8 authors.
Funding
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.
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