ROBUSTNESS-STRENGTH PERFORMANCE OF HIERARCHICAL ALPHA-HELICAL PROTEIN FILAMENTS

An abundant trait of biological protein materials are hierarchical nanostructures, ranging through atomistic, molecular to macroscopic scales. By utilizing the recently developed Hierarchical Bell Model, here we show that the use of hierarchical structures leads to an extended physical dimension in the material design space that resolves the conflict between disparate material properties such as strength and robustness, a limitation faced by many synthetic materials. We report materiomics studies in which we combine a large number of alpha-helical elements in all possible hierarchical combinations and measure their performance in the strength-robustness space while keeping the total material use constant. We find that for a large number of constitutive elements, most random structural combinations of elements (> 98%) lead to either high strength or high robustness, reflecting the so-called banana-curve performance in which strength and robustness are mutually exclusive properties. This banana-curve type behavior is common to most engineered materials. In contrast, for few, very specific types of combinations of the elements in hierarchies (< 2%) it is possible to maintain high strength at high robustness levels. This behavior is reminiscent of naturally observed material performance in biological materials, suggesting that the existence of particular hierarchical structures facilitates a fundamental change of the material performance. The results suggest that biological materials may have developed under evolutionary pressure to yield materials with multiple objectives, such as high strength and high robustness, a trait that can be achieved by utilization of hierarchical structures. Our results indicate that both the formation of hierarchies and the assembly of specific hierarchical structures play a crucial role in achieving these mechanical traits. Our findings may enable the development of self-assembled de novo bioinspired nanomaterials based on peptide and protein building blocks.