Abstract
A series of new alpha-helix mimetics based on a benzamide scaffold and potentially able to disrupt protein-protein interactions have been synthesized and characterized by X-ray analysis. Inspection of the solid state structures of aromatic amide dimers confirmed that the molecules adopt a curved conformation with intramolecular H-bonding between the amide NH and the alkoxy oxygen of the neighboring aromatic fragment (dNH⋯O ∼ 2 Å). Adjacent dimer molecules are prone to form supramolecular assemblies due to both hydrophobic alkyl side-chain/side-chain interactions and intermolecular H-bonding.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3705-3709 |
| Number of pages | 5 |
| Journal | Tetrahedron Letters |
| Volume | 52 |
| Issue number | 29 |
| DOIs | |
| State | Published - Jul 20 2011 |
Keywords
- Aromatic oligoamides
- Helical arrangement
- Hydrophobic interactions
- Self-assembly
ASJC Scopus subject areas
- Biochemistry
- Drug Discovery
- Organic Chemistry
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Kulikov, O. V., Incarvito, C., & Hamilton, A. D. (2011). Hydrophobic side-chain interactions in a family of dimeric amide foldamers-potential alpha-helix mimetics. Tetrahedron Letters, 52(29), 3705-3709. https://doi.org/10.1016/j.tetlet.2011.05.004