Comparative α-helicity of cyclic pentapeptides in water
Research output: Contribution to journal › Journal article › Research › peer-review
Helix-constrained polypeptides have attracted great interest for modulating protein-protein interactions (PPI). It is not known which are the most effective helix-inducing strategies for designing PPI agonists/antagonists. Cyclization linkers (X1-X5) were compared here, using circular dichroism and 2D NMR spectroscopy, for α-helix induction in simple model pentapeptides, Ac-cyclo(1,5)-[X1-Ala-Ala-Ala-X5]-NH2, in water. In this very stringent test of helix induction, a Lys1→Asp5 lactam linker conferred greatest α-helicity, hydrocarbon and triazole linkers induced a mix of α- and 3₁₀-helicity, while thio- and dithioether linkers produced less helicity. The lactam-linked cyclic pentapeptide was also the most effective α-helix nucleator attached to a 13-residue model peptide.
Original language | English |
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Journal | Angewandte Chemie International Edition |
Volume | 53 |
Issue number | 27 |
Pages (from-to) | 6965-6969 |
Number of pages | 5 |
ISSN | 1433-7851 |
DOIs | |
Publication status | Published - 2014 |
Externally published | Yes |
- Amino Acid Sequence, Circular Dichroism, Magnetic Resonance Spectroscopy, Oligopeptides, Peptides, Cyclic, Protein Structure, Secondary, Temperature, Water
Research areas
ID: 158554477