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Updated: Sep 9, 2025
11:56
Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
12.6K
A focus on unexpected surprises in RiPP natural product biosynthesis
1McGill University, Department of Chemistry 801 Sherbrooke St West Montreal Quebec H3A0B8 Canada christopher.thibodeaux@mcgill.ca.
Chemical Science
|September 5, 2025
Summary
Researchers characterized thuricin CD, an antimicrobial ribosomally-synthesized and post-translationally modified peptide (RiPP). The study revealed unexpected biosynthetic mechanisms, highlighting the need for detailed pathway analysis before engineering applications.
Area of Science:
- Natural Product Chemistry
- Biochemistry
- Synthetic Biology
Background:
- Natural products are crucial in drug discovery, inspiring ~75% of human medicines.
- Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a promising class of natural products.
- Understanding RiPP biosynthesis is key for harnessing their potential in chemical synthesis.
Purpose of the Study:
- To characterize the biosynthesis of the antimicrobial RiPP, thuricin CD.
- To investigate novel enzymatic mechanisms in RiPP production.
- To inform future engineering of RiPP pathways for chemical applications.
Main Methods:
- Biochemical characterization of thuricin CD.
- Analysis of RiPP biosynthetic gene clusters.
- Enzymatic assays to elucidate reaction mechanisms.
Main Results:
- Detailed characterization of thuricin CD revealed unexpected biosynthetic surprises.
- Expanded understanding of the diversity in RiPP biosynthetic pathways.
- Identified novel enzymatic activities within the thuricin CD pathway.
Conclusions:
- RiPP biosynthetic pathways exhibit significant natural diversity.
- Assumptions about RiPP biosynthesis should be made with caution.
- Detailed characterization is essential for the successful engineering of RiPP pathways.
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