Stable Peptide Fragments for Insect Control via Segmentation
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Solution Overview
Problem
Current methods for developing neuropeptide antagonists as insecticides are laborious, expensive, and often ineffective due to instability and lack of protocols to convert peptide agonists into antagonists, with most peptidomimetic compounds being costly and ineffective.
Innovation Solution
Development of low molecular weight peptide fragments derived from the PK/PBAN sequence, specifically 5-6 amino acid peptides with a dPhe residue, which are designed to be highly stable, bioavailable, and capable of penetrating the insect cuticle, including supplementary residues for enhanced penetration and stability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If full length PBAN peptides (33 amino acids) are used for insect control, then biological activity is achieved, but production cost is high and molecular weight is large
Solution Approach 1:
The patent divides the full-length PBAN peptide (33 amino acids) into smaller functional fragments, specifically identifying that the C-terminal hexapeptide sequence (FXPRLa where X=S,T,G,V) contains the essential biological activity. This segmentation allows production of shorter, cheaper peptides that retain the core insecticidal function while reducing manufacturing complexity and cost.
Solution Approach 2:
The patent extracts the critical functional domain from the full PBAN peptide. By identifying and isolating the C-terminal hexapeptide motif that is responsible for receptor binding and biological activity, the invention creates a minimal effective peptide that can be synthesized more economically while maintaining the desired insect control efficacy.
2Reliability
If conventional peptidomimetic compounds are developed through laborious protocols, then antagonistic activity may be achieved, but development time and cost increase significantly
Solution Approach 1:
The patent performs preliminary identification of the critical C-terminal hexapeptide sequence FXPRLa before attempting to develop antagonists. By pre-establishing which amino acid sequence is essential for activity, the invention eliminates the need for laborious trial-and-error protocols to identify active regions, significantly reducing development time while maintaining effective antagonistic activity.
Solution Approach 2:
The patent systematically varies parameters within the C-terminal hexapeptide sequence (changing the X position to different amino acids: S, T, G, V) to optimize antagonistic activity. This focused parameter exploration around the critical motif is much more efficient than conventional peptidomimetic approaches that require extensive library screening and structural optimization.
3Reliability
If standard peptide protocols are used to convert agonists into antagonists, then inhibitor activity may be achieved, but effectiveness is low due to lack of defined protocols
Solution Approach 1:
The patent applies systematic parameter changes to the C-terminal hexapeptide sequence to convert agonist activity to antagonist activity. By modifying specific positions within the FXPRLa motif (particularly the X position and N-terminal extensions), the invention generates peptides with enhanced antagonistic properties, achieving effective inhibition without relying on undefined conventional protocols.
Data Source
Figure 1A~1B
Figure 2
Figure 3A~3B
AI summary
The invention provides short peptides derived from an insect neuropeptide for controlling insects, particularly peptides or their analogs derived from PBAN family neuropeptide having at least one dPhe residue. The invention further provides an environmentally friendly method for controlling and/or preventing insect infestation by applying the short peptides in very low concentrations.