Peptide Bundlemer Networks With Precise Crosslink Control

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Solution Overview

Problem

The challenge in designing polymer networks lies in achieving precise molecular control over physical/covalent crosslinks, leading to inhomogeneous networks with defects that affect mechanical behavior.

Innovation Solution

Development of tetrameric coiled-coil peptide bundlemers with specific amino acid sequences that form alpha-helical structures, allowing for controlled spatial display of chemical functional groups for intra- and interbundle crosslinking interactions, enabling fine control over network formation and mechanical properties.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Manufacturing precision

If conventional polymer networks are used, then network formation is achieved, but molecular control over crosslinks is poor leading to inhomogeneous networks with defects

Engineering Contradiction:
Improvemolecular control of crosslinksVSAvoidnetwork homogeneity
Core Design Contradiction:
Manufacturing precisionVSStability of the object's composition

Solution Approach 1:

The polymer network is segmented into discrete tetrameric coiled-coil building blocks, each with precisely defined crosslinking sites. This segmentation allows molecular-level control over crosslink density and distribution, eliminating the inhomogeneity found in conventional polymer networks while maintaining network formation.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The tetrameric coiled-coil structures provide locally controlled chemical functionality through specific amino acid sequences at defined positions. This local quality control enables precise spatial arrangement of crosslinking groups, ensuring uniform crosslink distribution and eliminating defects in the network structure.

Inventive Principle:
Principle #3Local quality

2Manufacturing precision

If peptide bundlemers with specific amino acid sequences are used, then precise spatial display of chemical functional groups is achieved, but structural complexity increases

Engineering Contradiction:
Improvespatial display of chemical functional groupsVSAvoidpeptide sequence design
Core Design Contradiction:
Manufacturing precisionVSDevice complexity

Solution Approach 1:

The complex peptide sequence is divided into standardized heptad repeat units (abcdefg), where each position has a defined function (a and d form hydrophobic core, g forms interhelical contacts, b/c/e/f are surface-exposed). This modular segmentation simplifies the design process while maintaining precise spatial control of functional groups.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The peptide bundlemers combine natural amino acid sequences with designed hydrophobic core patterns to create composite structures that self-assemble into tetrameric coiled-coils. This composite approach leverages both natural and designed elements to achieve precise spatial organization without excessive complexity.

Inventive Principle:
Principle #40Composite materials

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

The bundlemers enable the formation of lattice nanostructures, amorphous networks, and liquid crystalline structures with precise mechanical properties, overcoming the limitations of existing polymer networks.

Implementation Method 1

the a, d, and g positions form a hydrophobic core of the tetrameric coiled-coil bundlemer particle

Methodology Applied
Scientific EffectHydrophobic interaction: Hydrophobe

Implementation Method 2

the 1st, 2nd, 3rd and 4th amino acid sequences together form an alpha-helical structure

Methodology Applied
Scientific EffectAlpha-helical structure formation: Helix

Implementation Method 3

peptide bundlemers capable of assembling into lattice nanostructures, amorphous networks and liquid crystalline structures in solution

Methodology Applied
Scientific EffectSelf-assembly: Self-Assembly

Data Source

PatentUS20260028371A1High performance and environmentally compatible films, fibers, and membranes with bundlemer building blocks
Publication Date: 2026.01.29 UNIVERSITY OF DELAWARE
  • US20260028371A1 patent drawing
  • US20260028371A1 patent drawing
  • US20260028371A1 patent drawing

AI summary

Disclosed herein are to peptide bundlemers that possess one or more hydrophobic groups on the surface that are capable of assembling into lattice nanostructures, amorphous networks and liquid crystalline structures in solution. Methods of creating these structures and articles formed from these structures are also disclosed.