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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
"Bridged" n→π* interactions can stabilize peptoid helices
Benjamin C Gorske1, Ryan C Nelson, Zara S Bowden
1Department of Chemistry, Bowdoin College , 6600 College Station, Brunswick, Maine 04011-8466, United States.
The Journal of Organic Chemistry
|September 21, 2013
Summary
Peptoids and thiopeptoids folding can be controlled by engineering specific side-chain interactions. This study reveals new strategies for stabilizing structures in these peptidomimetics for therapeutic applications.
Area of Science:
- Chemical Biology
- Supramolecular Chemistry
- Materials Science
Background:
- Peptoids, a class of peptidomimetic foldamers, are valuable in diverse applications including therapeutics and catalysis.
- Controlling peptoid secondary structures is crucial for their function, with side-chain engineering being a key strategy.
- N→π*(Ar) interactions are important for stabilizing helical structures in aromatic peptoids.
Purpose of the Study:
- To investigate n→π*(Ar) interactions in peptoid and thiopeptoid models.
- To characterize a novel
- bridged
- interaction mode.
- To explore strategies for controlling peptoid and thiopeptoid folding.
Main Methods:
- Computational modeling of peptoid and thiopeptoid structures.
- Experimental validation of predicted interactions.
- Analysis of amide rotamerism and secondary structure stabilization.
Main Results:
- N→π*(Ar) interactions significantly influence amide rotamerism in both peptoids and thiopeptoids.
- A new "bridged" interaction mode involving N-α-C-H σ orbitals was characterized.
- Thiopeptoids exhibit significant structural ordering due to these interactions.
Conclusions:
- N→π*(Ar) interactions offer a powerful strategy for controlling peptoid and thiopeptoid folding.
- Thiopeptoids show promise as highly structured molecules for therapeutic and nanotechnological applications.
- This research provides new insights into the fundamental principles governing foldamer structure and function.
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