Samuel Kim1,Marcus Cathey1,Brandon Bounds1,Piotr Marszalek2,Minkyu Kim1,3
University of Arizona1,Duke University2,The University of Arizona3
Samuel Kim1,Marcus Cathey1,Brandon Bounds1,Piotr Marszalek2,Minkyu Kim1,3
University of Arizona1,Duke University2,The University of Arizona3
Natural materials are a great blueprint for the development of next-generation biomaterials because of their exceptional physical, chemical, and biological properties. To mimic the unique properties of natural materials, protein-based polymer networks are utilized to develop well-characterized functional proteins that can be engineered into artificial protein polymers. However, it is still unclear how these artificial proteins can be incorporated into polymer networks that can properly translate protein nanomechanics. To translate protein nanomechanics to bulk mechanical properties, strong and specific cross-linkers is necessary to form stable polymer networks with reduced topological defects. Our recent work has shown that streptavidin tetramers fulfill the requirements and can be used to form protein-based polymer networks, potentially allowing the translation of protein nanomechanics to bulk hydrogel materials.<br/><br/>In this study, we investigated a novel mechanism involving streptavidin cross-linkers to determine optimal design components for producing protein polymer networks that can translate the single-molecule behavior into bulk mechanical properties. To properly mimic the reversible deformability of red blood cells and develop functional biomaterials for cardiovascular tissue engineering applications, ankyrin, a cytoskeleton protein from red blood cells were designed as artificial protein building blocks for fabricating polymer networks that can translate ankyrin nanomechanics to macroscale functional biomaterials.