Polymorphism in Self-Assembly of Short Peptoid Sequences.

Area of Science:

• Materials Science
• Polymer Chemistry
• Biomaterials Engineering

Background:

• Controlling polymer self-assembly into specific morphologies is key for developing advanced functional materials.
• Peptoids (poly-N-substituted glycines) offer a versatile platform for creating sequence-defined polymers with tunable properties.
• Understanding the relationship between molecular structure and self-assembled morphology is crucial for material design.

Purpose of the Study:

• To achieve morphological control over the self-assembly of short peptoids with asymmetric hydrophobic domains.
• To investigate the mechanisms driving peptoid assembly polymorphism and identify methods for precise control.
• To explore the potential of peptoids in creating bioinspired functional materials with designed morphologies.

Main Methods:

• Synthesized a series of short peptoids with asymmetric hydrophobic domains.
• Investigated self-assembly using techniques to control sequence design, solution pH, and temperature.
• Employed molecular dynamics simulations to understand the role of hydrophobic domains in assembly.
• Utilized heating to induce morphological transformations.

Main Results:

• Demonstrated assembly polymorphism in peptoids, yielding nanosheets, twisted ribbons, and nanofibers.
• Achieved precise control over peptoid bilayer twisting and folding through sequence design, pH, and temperature.
• Showcased the transformation of nanosheets into nanohelices via controlled heating.
• Identified asymmetric hydrophobic domains as key to peptoid bilayer flexibility and assembly polymorphism.

Conclusions:

• The study provides a mechanistic understanding of peptoid assembly polymorphism.
• Precise control over peptoid self-assembly can be achieved by tuning molecular interactions.
• This work lays the foundation for designing biomimetic materials with tailored morphologies and functionalities using peptoids.