Self-Assembly of α-Helices to Form Rare Two-Dimensional Square P4mm Symmetry via Silica Mineralization

摘要

Proteins are one of the most important types of biomacromolecules in living organisms and play specific and irreplaceable roles in human metabolism, especially during biochemical processes. In addition to their specific amino acid sequence proteins have a sophisticated hierarchical structure and spatial conformation.~([1]) The a-helix, which is a central type of secondary structure in proteins, forms the cornerstone of many more complex three-dimensional architectures in proteins, and dominates numerous biological activities both in vivo and in vitro.~([2]) Because they have a rigid, rod-like morphology and a unique conformational transformation property,~([3]) a-helices have been well studied and broadly used as building blocks in the design of molecular assemblies, generating a variety of functional materials with notable activities, such as micelles, vesicles, hydrogels and organic–inorganic hybrids.~([4–9]) These functional materials have been applied for controlled compound release, diagnosis, biological simulation, hard tissue engineering and double emulsions.~([6, 10–17])