Random heteropolymers preserve protein function in foreign environments.

Area of Science:

• Biomaterials Science
• Polymer Chemistry
• Biotechnology

Background:

• Incorporating active proteins into synthetic polymers offers potential for novel biomaterials.
• Proteins typically do not function under standard polymer processing conditions.
• Mimicking intrinsically disordered proteins is key to overcoming this challenge.

Purpose of the Study:

• To design synthetic heteropolymers capable of solubilizing and stabilizing proteins in non-native environments.
• To create a new strategy for interfacing biological systems with synthetic materials for protein-based applications.

Main Methods:

• Analysis of protein sequence trends and surface chemical patterns.
• Design of four-monomer random heteropolymers with optimized composition and statistical monomer distribution.
• Application of heteropolymers in cell-free synthesis of membrane proteins and enzyme-containing plastics.

Main Results:

• Developed heteropolymers that mimic intrinsically disordered proteins, enabling protein stabilization in non-native conditions.
• Achieved proper protein folding for transport in cell-free synthesized membrane proteins.
• Demonstrated successful toxin bioremediation using enzyme-containing plastics.

Conclusions:

• Controlling statistical monomer distribution in heteropolymers is a viable strategy for protein stabilization.
• This approach enables the creation of functional protein-based biomaterials for diverse applications.
• The findings open new avenues for interfacing biological functions with synthetic materials.