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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

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Published on: May 4, 2018

Guidelines for Optimizing Type S Nonribosomal Peptide Synthetases.

Nadya Abbood^1,2, Juliana Effert¹, Kenan A J Bozhueyuek^1,2,3

¹Max-Planck-Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043 Marburg, Germany.

ACS Synthetic Biology

|July 31, 2023

Summary

Engineered bacterial biosynthetic assembly lines (NRPSs) now produce artificial peptides with 55x higher yields. Optimizing synthetic protein interaction reagents (SYNZIPs) enhances production for synthetic biology applications.

Keywords:

NRPS engineering biocombinatorial approach iterative optimization natural products nonribosomal peptides synthetic biology

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Published on: April 27, 2018

Area of Science:

Synthetic biology
Biochemistry
Natural product biosynthesis

Background:

Bacterial nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs) synthesize natural products with therapeutic potential.
Engineering these systems allows for the creation of novel peptides and polyketides.

Purpose of the Study:

To introduce and optimize a synthetic NRPS variant (type S NRPS) for high-throughput library generation.
To overcome production yield bottlenecks in engineered NRPS systems.

Main Methods:

Introduced a simplified type S NRPS variant for biocombinatorial engineering.
Truncated synthetic protein interaction reagents (SYNZIPs) from NRPS termini.
Incorporated glycine-serine linkers to improve domain interactions.

Main Results:

Achieved up to 55-fold increase in production yields compared to non-optimized NRPSs.
Restored and surpassed wild-type production levels.
Demonstrated successful parallelized generation of nonribosomal peptide libraries.

Conclusions:

Optimized type S NRPSs enable efficient production of artificial nonribosomal peptides.
SYNZIP toolbox optimization benefits synthetic biology, metabolic engineering, and multienzyme complex engineering.