Protein coacervation-driven active forces power protocell dynamics

Area of Science:

• Biophysics
• Soft Matter Physics
• Synthetic Biology

Background:

• Protein coacervates, formed via liquid-liquid phase separation (LLPS), are emerging as novel force generators.
• Their force generation is independent of traditional ATP-driven molecular motors.
• The coordination and force scaling of these coacervates remain largely unexplored.

Purpose of the Study:

• To engineer a model system for studying force generation and harnessing by protein coacervates.
• To investigate temperature-modulated contractility and force amplification in engineered protocells.
• To explore the potential of protein coacervates in performing large-scale mechanical work.

Main Methods:

• Engineered a temperature-responsive elastin-based protocell model.
• Utilized liquid-liquid phase separation (LLPS) properties to modulate protocell dynamics.
• Investigated the effect of membrane crosslinking on contraction and force accumulation.
• Employed mathematical modeling to analyze force amplification.

Main Results:

• Demonstrated temperature-modulated contractility and force harnessing in the engineered protocells.
• Observed spontaneous expulsion of internal LLPS complexes due to accumulated mechanical forces.
• Showcased force amplification from piconewton to large-scale mechanical work via protein coacervation.
• Established a model framework for harnessing coacervate-driven forces.

Conclusions:

• Protein coacervates possess significant mechanical potential for force generation and amplification.
• Engineered protocells provide a viable platform for studying and harnessing coacervate-driven forces.
• This work paves the way for applications in synthetic biology, biomaterials, and soft robotics.