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A Coupled Experiment-finite Element Modeling Methodology for Assessing High Strain Rate Mechanical Response of Soft Biomaterials

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What Is the Force-per-Molecule Inside a Biomaterial Having Randomly Oriented Units?

Joel Nowitzke¹, Ionel Popa¹

¹Department of Physics, University of Wisconsin-Milwaukee, 3135 N. Maryland Avenue, Milwaukee, Wisconsin 53211, United States.

The Journal of Physical Chemistry Letters

|July 28, 2022

Summary

Researchers developed a coarse-grained model to calculate the force per molecule in protein-based materials. Experiments with protein hydrogels achieved forces up to 17 pN per domain, advancing biomaterial tension understanding.

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Area of Science:

Biomaterials Science
Computational Biology
Protein Engineering

Background:

Protein-based materials, both synthetic and natural, consist of randomly oriented, cross-linked molecules.
Understanding the mechanical properties, specifically force response, is crucial for designing advanced biomaterials.

Purpose of the Study:

To develop a coarse-grained computational approach for estimating the average force per molecule in globular protein-based materials.
To experimentally validate the computational model using synthesized protein hydrogels.

Main Methods:

A three-step coarse-grained modeling approach: molecule placement, cross-linking, and trimming of non-participating domains.
Calculation of active domains per cross-section area to determine force per domain.
Synthesis and mechanical testing of protein hydrogels using Bovine Serum Albumin (BSA) and polyprotein L.

Main Results:

The computational model successfully estimates force per molecule in protein materials.
Material concentration was identified as the most sensitive parameter influencing force response.
Experimental synthesis of protein hydrogels yielded forces of up to 17 pN per domain.

Conclusions:

The developed coarse-grained approach provides a method for predicting force-per-molecule in protein biomaterials.
Experimental validation confirms the model's predictive capability and demonstrates significant force-per-domain values.
This work contributes to a fundamental understanding of tension scaling in protein-based biomaterials.