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- Title
Controlling the Helix Handedness of ααβ-Peptide Foldamers through Sequence Shifting.
- Authors
Szefczyk, Monika; Węglarz-Tomczak, Ewelina; Fortuna, Paulina; Krzysztoń, Agnieszka; Rudzińska-Szostak, Ewa; Berlicki, Łukasz
- Abstract
Peptide foldamers containing both cis-β-aminocyclopentanecarboxylic acid and α-amino acid residues combined in various sequence patterns (ααβ, αααβ, αβααβ, and ααβαααβ) were screened using CD and NMR spectroscopy for the tendency to form helices. ααβ-Peptides were found to fold into an unprecedented and well-defined 16/17/15/18/14/17-helix. By extending the length of the sequence or shifting a fragment of the sequence from one terminus to another in ααβ-peptides, the balance between left-handed and right-handed helix populations present in the solution can be controlled. Engineering of the peptide sequence could lead to compounds with either a strong propensity for the selected helix sense or a mixture of helical conformations of opposite senses.
- Subjects
MOLECULAR structure of oligomers; PEPTIDE synthesis; HELICES (Algebraic topology); MATHEMATICAL sequences; PROTEIN folding
- Publication
Angewandte Chemie International Edition, 2017, Vol 56, Issue 8, p2087
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201610154