title: The role of protein assembly in dynamically tunable bio-optical tissues.
abstract: Cephalopods are nicknamed the "masters of disguise" for their highly evolved camouflage mechanisms, including the hallmark ability to rapidly change the color and reflectance of their skin. Previously, reflectin proteins were identified as the major biomaterial component of iridosomes [1], specialized light-reflecting architectures that contribute intense structural color to squid skin, eyes, and organs [2-5]. Supramolecular assembly of reflectin has been recognized as a key property in the protein's function [6]. Here, we report the first cloning and expression of a specific reflectin protein found in the responsive iridophore cells of the squid Loligo pealeii, which are unique in their ability to switch on/off and change color. We demonstrate that these iridophores can be chemically tuned to reflect the entire visible spectrum. By examining recombinant reflectin, we show that this dynamic optical function is facilitated by the hierarchical assembly of nanoscale protein particles that elicit large volume changes upon condensation. These findings provide insight into the design and synthesis of biomaterials for complex, responsive function in optical applications.
authors.affiliation: Institute for Collaborative Biotechnologies and the Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, 93106, USA. atao@ucsd.edu
authors.forename: Andrea R
authors.initials: AR
authors.lastname: Tao
authors.forename: Daniel G
authors.initials: DG
authors.lastname: DeMartini
authors.forename: Michi
authors.initials: M
authors.lastname: Izumi
authors.forename: Alison M
authors.initials: AM
authors.lastname: Sweeney
authors.forename: Amanda L
authors.initials: AL
authors.lastname: Holt
authors.forename: Daniel E
authors.initials: DE
authors.lastname: Morse
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D003116:Color; D008027:Light; D049834:Loligo / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012031:Refractometry; D012542:Scattering, Radiation
chemical_list: D011506:Proteins; D011994:Recombinant Proteins