A toolbox of oligopeptide-modified polymers for tailored elastomers

Area of Science:

• Materials Science
• Polymer Chemistry
• Supramolecular Chemistry

Background:

• Biomaterials achieve versatility through hierarchical structure formation using identical supramolecular motifs.
• Synthetic supramolecular elastomers offer potential for tailored properties but require precise structural control.

Purpose of the Study:

• To exert structural control in synthetic supramolecular elastomers for a broad range of thermomechanical properties.
• To investigate the self-assembly behavior of oligopeptide-terminated polymers based on oligopeptide length.
• To develop a toolbox for tailored elastomers with versatile properties using blends of modified polymers.

Main Methods:

• Oligopeptide-terminated polymers were synthesized with varying oligopeptide lengths.
• Selective self-assembly into aggregates or nanofibrils was induced by controlling oligopeptide length.
• Self-sorting of differently lengthed oligopeptides was utilized to create coexisting nanostructures.
• Blends of polymers with matching or non-matching oligopeptides were prepared and characterized.

Main Results:

• Oligopeptide length determined the formation of small aggregates or nanofibrils.
• Blends with matching oligopeptides yielded reinforced elastomers with significantly higher shear moduli.
• Blends with non-matching oligopeptides formed interpenetrating supramolecular networks with excellent vibration damping.

Conclusions:

• Oligopeptide-terminated polymers self-assemble into distinct nanostructures based on length.
• Precise control over self-assembly enables the creation of elastomers with tunable mechanical and damping properties.
• Blends of oligopeptide-modified polymers provide a versatile platform for designing advanced elastomer materials.