The role of repeat motifs in proteins to define self-assembly and network formation

Proteins serve as highly adaptable molecular building blocks that nature exploits to create a wide range of functional materials. To diversify this molecular toolkit, nature employs sophisticated strategies, such as tandem repeat sequences, which function as molecular “hotspots” for genetic variability by modulating the number of repeat units or introducing subtle modifications to the repeat motifs. These segmented biopolymers can serve as templates to guide the self-assembly of complementary materials. In this discussion, we focus on the assembly dynamics of various repeat proteins in the context of atomically thin inorganic sheets and metal coordination. Given the geometric constraints imposed by these complementary materials, we analyze how the modular repeat segments influence the topological states of nanosheets and investigate the kinetics of network formation during interactions with metal ions. The goal of this work is to develop a foundational understanding of how tandem repeat units facilitate state transitions and self-assembly processes in protein-based biomaterials from a physical perspective.