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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Accessing Diverse Pyridine-Based Macrocyclic Peptides by a Two-Site Recognition Pathway.

Dinh T Nguyen^1,2,3, Tung T Le^1,3, Andrew J Rice^1,2

¹Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.

Journal of the American Chemical Society

|June 17, 2022

Summary

Researchers developed a novel enzymatic method to synthesize pyridine-based macrocyclic peptides (pyritides) from linear precursors. This approach enables the creation of diverse pyritide analogues for drug discovery, expanding access to these valuable molecular scaffolds.

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Area of Science:

Biochemistry
Organic Chemistry
Drug Discovery

Background:

Macrocyclic peptides are crucial scaffolds in drug discovery.
Accessing diverse libraries of these molecules is of significant interest.
Pyridine-based macrocyclic peptides (pyritides) are a recently identified class of ribosomally synthesized and post-translationally modified peptides (RiPPs).

Purpose of the Study:

To report the enzymatic synthesis of pyritides from linear precursor peptides.
To investigate the recognition mechanisms of pyritide-forming enzymes.
To explore the generation of diverse pyritide analogues for drug discovery.

Main Methods:

Enzymatic synthesis of pyritides using linear precursor peptides.
Characterization of pyritide-forming enzyme substrate recognition, focusing on leader and core regions.
Combinatorial biosynthesis integrating pyritide pathway with azole-forming enzymes.

Main Results:

Demonstrated enzymatic synthesis of pyritides from linear precursors.
Identified recognition of both leader and C-terminal tripeptide motifs by pyritide-forming enzymes.
Showcased successful generation of diverse pyritide analogues through core region substitutions.
Created a novel thiazole-containing pyritide by combining pathways.

Conclusions:

The pyritide biosynthetic enzymes exhibit broad substrate scope, enabling facile generation of diverse analogues.
This enzymatic platform is a promising tool for macrocyclic peptide lead discovery and optimization.
The study expands the chemical space accessible for drug development using RiPPs.