Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices
- 28 September 2011
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- Vol. 48 (10) , 1416-1418
Abstract
Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.Keywords
This publication has 35 references indexed in Scilit:
- An orthosteric inhibitor of the Ras-Sos interactionNature Chemical Biology, 2011
- Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potencyProceedings of the National Academy of Sciences, 2010
- Disrupting protein–protein interactions with non-peptidic, small molecule α-helix mimeticsCurrent Opinion in Chemical Biology, 2010
- Inhibition of Hypoxia Inducible Factor 1—Transcription Coactivator Interaction by a Hydrogen Bond Surrogate α-HelixJournal of the American Chemical Society, 2009
- Direct inhibition of the NOTCH transcription factor complexNature, 2009
- Structural and biological mimicry of protein surface recognition by α/β-peptide foldamersProceedings of the National Academy of Sciences, 2009
- A Hydrogen Bond Surrogate Approach for Stabilization of Short Peptide Sequences in α-Helical ConformationAccounts of Chemical Research, 2008
- Foldamers with Heterogeneous BackbonesAccounts of Chemical Research, 2008
- β-Peptidic PeptidomimeticsAccounts of Chemical Research, 2008
- Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 HelixScience, 2004