Abstract
De novo designed helix-loop-helix peptide foldamers containing cis-2-aminocyclopentanecarboxylic acid residues were evaluated for their conformational stability and possible use in enzyme mimetic development. The correlation between hydrogen bond network size and conformational stability was demonstrated through CD and NMR spectroscopies. Molecules incorporating a Cys/His/Glu triad exhibited enzyme-like hydrolytic activity.
Original language | English |
---|---|
Pages (from-to) | 356-361 |
Number of pages | 6 |
Journal | Bioorganic Chemistry |
Volume | 81 |
DOIs | |
Publication status | Published - 1 Dec 2018 |
Externally published | Yes |
Funding
The work was financed by the National Science Centre, Poland (Grant No. DEC-2013/10/E/ST5/00625 ). Appendix A
Funders | Funder number |
---|---|
Narodowe Centrum Nauki | DEC-2013/10/E/ST5/00625 |
Narodowym Centrum Nauki |
Keywords
- Catalysis
- Circular dichroism
- Conformation
- Foldamers
- Nuclear magnetic resonance
- Peptides