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Related Experiment Video

Updated: May 21, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

End-Capped α-Helices as Modulators of Protein Function.

Andrew B Mahon¹, Paramjit S Arora

¹Department of Chemistry, New York University, New York, NY 10003.

Drug Discovery Today. Technologies

|June 20, 2012

Summary

This study explores using a helix nucleation strategy to create new ways to control protein-protein interactions. This approach targets alpha-helices, crucial for biomolecular binding.

Area of Science:

Biochemistry and Molecular Biology
Structural Biology

Background:

Proteins interact with biomolecules via folded sub-domains with secondary structures.
Alpha-helices are the most abundant protein secondary structures and are vital for specific interactions.

Purpose of the Study:

To investigate a helix nucleation strategy for developing protein-protein interaction modulators.
To leverage the role of alpha-helices in biomolecular recognition.

Main Methods:

Computational modeling and design of helix nucleation strategies.
In vitro or in vivo validation of designed molecules (details not provided in abstract).

Main Results:

Demonstrated the feasibility of a helix nucleation strategy.

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Last Updated: May 21, 2026

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Published on: August 1, 2018

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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Identified potential for generating novel protein-protein interaction modulators.

Conclusions:

A helix nucleation strategy offers a promising route to design modulators of protein-protein interactions.
Targeting alpha-helices is a viable approach for therapeutic intervention.