NRPS Library Construction via Non-Native Restriction Sites

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Solution Overview

Problem

Current methods for producing non-ribosomal peptides (NRPs) using non-ribosomal peptide synthetases (NRPSs) are limited in efficiency and diversity, as they rely on native restriction enzyme recognition sequences that restrict modification and variation of NRPSs.

Innovation Solution

Introduction of non-native restriction enzyme recognition sequences into nucleic acids encoding NRPSs, allowing for the production of modified NRPSs and novel NRPs through controlled cleavage and ligation of nucleic acid fragments, enabling the creation of diverse NRPS modules and peptides.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Adaptability or versatility

If native restriction enzyme recognition sequences are used in NRPS nucleic acids, then the original NRPS function is maintained, but the ability to modify and create diverse NRPS variants is limited

Engineering Contradiction:
Improvediversity of NRPS variantsVSAvoidfunctional capability of original NRPS
Core Design Contradiction:
Adaptability or versatilityVSReliability

Solution Approach 1:

The NRPS nucleic acid is divided into modular segments separated by restriction enzyme recognition sequences. Each module can be independently manipulated, allowing creation of diverse variants while preserving functional domains. The segmentation enables precise modification without compromising overall NRPS function.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

Non-native restriction enzyme recognition sequences serve as intermediary elements inserted into the NRPS nucleic acid. These intermediary sequences facilitate controlled cleavage and recombination, enabling diverse NRPS variant creation while the modular design ensures original functional capability is maintained through proper domain preservation.

Inventive Principle:
Principle #24Intermediary (Mediator)

2Ease of manufacture

If restriction enzyme recognition sequences are introduced into NRPS nucleic acid, then controlled cleavage and ligation can be performed, but the complexity of nucleic acid manipulation increases

Engineering Contradiction:
Improvecontrolled cleavage and ligationVSAvoidnucleic acid structure
Core Design Contradiction:
Ease of manufactureVSDevice complexity

Solution Approach 1:

Restriction enzyme recognition sequences are pre-inserted into the NRPS nucleic acid at designated module boundaries before any modification is attempted. This preliminary action creates ready-to-use cleavage sites, simplifying subsequent manipulation steps and reducing the complexity of nucleic acid handling during actual variant creation.

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

The nucleic acid structure is modified by introducing specific recognition sequences that change its parameters (adding cleavage sites). However, the overall modular architecture and functional domain integrity are maintained, balancing increased manipulability with controlled structural complexity.

Inventive Principle:
Principle #35Parameter changes

3Adaptability or versatility

If multiple NRPS modules are combined to create novel peptides, then peptide diversity increases, but the efficiency of production decreases

Engineering Contradiction:
Improvepeptide diversityVSAvoidproduction efficiency
Core Design Contradiction:
Adaptability or versatilityVSProductivity

Solution Approach 1:

The NRPS system is segmented into standardized modules with uniform restriction enzyme recognition sequences. This segmentation allows rapid assembly of diverse peptide variants through controlled recombination of pre-characterized functional domains, maintaining production efficiency while increasing peptide diversity.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The modular NRPS design with universal restriction sites enables the same framework to produce multiple different peptide variants. Each module can be independently swapped or combined, allowing one NRPS construct to serve multiple functions and produce diverse peptides efficiently through standardized assembly procedures.

Inventive Principle:
Principle #6Universality (Multi-functionality)

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

This approach enables efficient production of novel NRPSs and NRPs, expanding the diversity and range of peptides that can be synthesized, while maintaining the functional capability of the original NRPSs.

Implementation Method 1

a step of preparing a mixture of containing a plurality of resulting cleaved nucleic acid fragments by treating the set of starting plasmids with a restriction enzyme

Methodology Applied
Scientific EffectRestriction enzyme cleavage: Enzyme

Implementation Method 2

a step of forming a linked nucleic acid by ligating the plurality of cleaved nucleic acid fragments

Methodology Applied
Scientific EffectLigation: Chemical Bonding

Data Source

PatentEP4563701A1Peptide synthetase library construction method
Publication Date: 2025.06.04 KOBE UNIV
  • EP4563701A1 patent drawingFigure 1A~1B
  • EP4563701A1 patent drawingFigure 2
  • EP4563701A1 patent drawingFigure 3

AI summary

The present disclosure pertains to produce a novel NRPS. In the present disclosure, a restriction enzyme recognition sequence was successfully introduced into a nucleic acid encoding an NRPS while maintaining a function of producing a target NRP. Various NRPSs can be produced using the introduced restriction enzyme recognition sequence. In one aspect, the present disclosure provides a nucleic acid containing a non-native restriction enzyme recognition sequence and encoding an NRPS. In another aspect, the present disclosure provides a method for efficiently producing a nucleic acid encoding a novel NRPS using a non-native restriction enzyme recognition sequence. In addition, the present disclosure also provides a novel NRPS and a novel NRP.