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 |
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Keywords
- Catalysis
- Circular dichroism
- Conformation
- Foldamers
- Nuclear magnetic resonance
- Peptides
Cite this
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Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics. / Drewniak, Magda; Węglarz-Tomczak, Ewelina; Ożga, Katarzyna; Rudzińska-Szostak, Ewa; Macegoniuk, Katarzyna; Tomczak, Jakub M.; Bejger, Magdalena; Rypniewski, Wojciech; Berlicki, Łukasz.
In: Bioorganic Chemistry, Vol. 81, 01.12.2018, p. 356-361.Research output: Contribution to Journal › Article › Academic › peer-review
TY - JOUR
T1 - Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics
AU - Drewniak, Magda
AU - Węglarz-Tomczak, Ewelina
AU - Ożga, Katarzyna
AU - Rudzińska-Szostak, Ewa
AU - Macegoniuk, Katarzyna
AU - Tomczak, Jakub M.
AU - Bejger, Magdalena
AU - Rypniewski, Wojciech
AU - Berlicki, Łukasz
PY - 2018/12/1
Y1 - 2018/12/1
N2 - 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.
AB - 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.
KW - Catalysis
KW - Circular dichroism
KW - Conformation
KW - Foldamers
KW - Nuclear magnetic resonance
KW - Peptides
UR - http://www.scopus.com/inward/record.url?scp=85052900151&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85052900151&partnerID=8YFLogxK
U2 - 10.1016/j.bioorg.2018.07.012
DO - 10.1016/j.bioorg.2018.07.012
M3 - Article
VL - 81
SP - 356
EP - 361
JO - Bioorganic Chemistry
JF - Bioorganic Chemistry
SN - 0045-2068
ER -