Abstract
In the search for synthetic mimics of protein secondary structures relevant to the mediation of protein-protein interactions, we have synthesized a series of tetrasubstituted diphenylacetylenes that display β-sheet structures in two directions. Extensive X-ray crystallographic and NMR solution phase studies are consistent with these proteomimetics adopting sheet structures, displaying both hydrophobic and hydrophilic amino acid side chains. The importance of β-sheet structures at the interface of protein-protein interactions has prompted the development of a range of synthetic strategies to template and stabilize this secondary structural motif. A tetrasubstituted diphenylacetylene is examined as a central nucleating point for the projection of extended sheet structures in two directions.
Original language | English (US) |
---|---|
Pages (from-to) | 3650-3653 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 53 |
Issue number | 14 |
DOIs | |
State | Published - Apr 1 2014 |
Keywords
- beta-sheets
- peptidomimetics
- protein surfaces
- protein-protein interactions
- secondary structures
ASJC Scopus subject areas
- Catalysis
- General Chemistry