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

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Stretching Peptides to Generate Small Molecule β-Strand Mimics.

Zoë C Adams¹, Anthony P Silvestri^1,2, Sorina Chiorean¹

¹Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States.

ACS Central Science

|May 1, 2023

Summary

This summary is machine-generated.

Researchers developed a novel method using diyne braces to create stable, extended-backbone peptide macrocycles. This technique offers new ways to target challenging protein-protein interactions (PPIs) for drug discovery.

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Area of Science:

Chemical Biology
Medicinal Chemistry
Structural Biology

Background:

Protein-protein interactions (PPIs) are crucial in disease mechanisms but difficult to target due to shallow binding surfaces.
Existing methods for targeting PPIs are limited, especially for accessing extended backbone structures.

Purpose of the Study:

To develop a novel method for creating rigid, extended-backbone peptide macrocycles.
To enable the targeting of challenging protein-protein interaction (PPI) interfaces.

Main Methods:

Incorporation of a rigid, linear diyne brace between side chains at the i to i+2 positions of peptides.
Utilized Nuclear Magnetic Resonance (NMR) and density functional theory (DFT) for structural and conformational analysis.
Developed a high-throughput synthesis approach for the diyne-braced peptides.

Main Results:

Generated a family of low-molecular-weight, extended-backbone peptide macrocycles with stable, rigid conformations in solution.
Demonstrated that the peptide conformation can be tuned to explore extended conformational space.
Achieved excellent conversions (>95%) for diyne brace formation and showed the utility of the technique with inhibitors of bacterial type 1 signal peptidase.

Conclusions:

The diyne brace strategy provides a versatile platform for designing conformationally constrained peptides.
This approach facilitates the exploration of extended peptide conformational space for targeting PPIs.
The developed peptide macrocycles hold potential for therapeutic and probe development against diseases driven by PPIs.