Reflectin is a cephalopods-derived protein that assembles into thin layers of the tunable Bragg reflectors in iridocytes. It has been a protein of interest for long due to its potential in constituting materials with extreme changeability. Previous works from Xie lab revealed some very interesting facts about reflectins: First, reflectins self-assemble into nano-scale hexagonal prisms or octagonal prisms, and these building blocks in turn assemble into two-dimensional-extended lamellar within seconds after the input of several small aromatic molecules, such as imidazole, histamine and octopamine. The sizes of these lamellar ranges from tens of micrometers to hundreds of micrometers, depending on the type of aromatic molecules added and assembling time. Second, subdomain 1 and some reflectin-inspired engineered peptides also hold the self-assembly properties, with a minimum functional sequence of 8 a.a..

 

According to these findings, it might be a better application of reflectins in a microscopic level where the delicate assembling pattern is preserved, rather than in a macroscopic level where these microscopic structures are very likely to be disrupted. Besides, it might also be better if protein is preserved in the host organisms rather than in vitro for the purpose of long-term maintenance and proliferation.

 

Upon these principles, reflectin, and especially its truncated versions, would be act as an efficient cell-based micro-scale recruiting platform and would become very competitive tools in inducible catalysis, pathway enhancement, organelle-targeted recruiting, construction of disease models, chip for protein analysis and bio-film formation.