Shaping Protein Amphiphilic Assemblies via Allosteric Effect: From 1D Nanofilament to 2D Rectangular Nanosheet

Dynamically shaping protein assemblies into desired nanostructures is a grand challenge. Here we present a new strategy that exploits protein allosteric effect to flexibly manipulate protein amphiphilic self-assembly. This allosteric regulation emphasizes that a huge deformation of protein assemblies is stemmed from a tiny protein conformational switch. Using adenylate kinase as an allosteric protein, adenylate kinase (AKe)-based protein amphiphiles can transform their assembling architectures between 1D nanofilament and 2D crystalline nanosheet due to AKe conformation folding and unfolding. Control over the allosteric degree by tuning the allosteric signal level allows us to mold protein nanostructures in various morphologies and dimension-alities. This method is universal and would open a new avenue to construct dynamic protein structural materials.