TY - JOUR
T1 - Structure, self-assembly, and properties of a truncated reflectin variant
AU - Umerani, Mehran J.
AU - Pratakshya, Preeta
AU - Chatterjee, Atrouli
AU - Cerna Sanchez, Juana A.
AU - Kim, Ho Shin
AU - Ilc, Gregor
AU - Kovacic, Matic
AU - Magnan, Cristophe
AU - Marmiroli, Benedetta
AU - Sartori, Barbara
AU - Kwansa, Albert L.
AU - Orins, Helen
AU - Bartlett, Andrew W.
AU - Leung, Erica M.
AU - Feng, Zhijing
AU - Naughton, K.L.
AU - Norton-Baker, Brenna
AU - Phan, Long
AU - Long, James
AU - Allevato, Alex
AU - Leal-Cruz, Jessica E.
AU - Lin, Qiyin
AU - Baldi, Pierre
AU - Bernstorff, Sigrid
AU - Plavec, Janez
AU - Yingling, Yaroslava G.
AU - Gorodetsky, A. A.
PY - 2020/12/29
Y1 - 2020/12/29
N2 - Naturally occurring and recombinant protein-based materials are frequently employed for the study of fundamental biological processes and are often leveraged for applications in areas as diverse as electronics, optics, bioengineering, medicine, and even fashion. Within this context, unique structural proteins known as reflectins have recently attracted substantial attention due to their key roles in the fascinating color-changing capabilities of cephalopods and their technological potential as biophotonic and bioelectronic materials. However, progress toward understanding reflectins has been hindered by their atypical aromatic and charged residue-enriched sequences, extreme sensitivities to subtle changes in environmental conditions, and well-known propensities for aggregation. Herein, we elucidate the structure of a reflectin variant at the molecular level, demonstrate a straightforward mechanical agitation-based methodology for controlling this variant’s hierarchical assembly, and establish a direct correlation between the protein’s structural characteristics and intrinsic optical properties. Altogether, our findings address multiple challenges associated with the development of reflectins as materials, furnish molecular-level insight into the mechanistic underpinnings of cephalopod skin cells’ color-changing functionalities, and may inform new research directions across biochemistry, cellular biology, bioengineering, and optics.
AB - Naturally occurring and recombinant protein-based materials are frequently employed for the study of fundamental biological processes and are often leveraged for applications in areas as diverse as electronics, optics, bioengineering, medicine, and even fashion. Within this context, unique structural proteins known as reflectins have recently attracted substantial attention due to their key roles in the fascinating color-changing capabilities of cephalopods and their technological potential as biophotonic and bioelectronic materials. However, progress toward understanding reflectins has been hindered by their atypical aromatic and charged residue-enriched sequences, extreme sensitivities to subtle changes in environmental conditions, and well-known propensities for aggregation. Herein, we elucidate the structure of a reflectin variant at the molecular level, demonstrate a straightforward mechanical agitation-based methodology for controlling this variant’s hierarchical assembly, and establish a direct correlation between the protein’s structural characteristics and intrinsic optical properties. Altogether, our findings address multiple challenges associated with the development of reflectins as materials, furnish molecular-level insight into the mechanistic underpinnings of cephalopod skin cells’ color-changing functionalities, and may inform new research directions across biochemistry, cellular biology, bioengineering, and optics.
KW - Biomaterials
KW - Optical properties
KW - Proteins
KW - Reflectin
KW - Self-assembly
UR - http://www.scopus.com/inward/record.url?scp=85100168998&partnerID=8YFLogxK
U2 - 10.1073/PNAS.2009044117
DO - 10.1073/PNAS.2009044117
M3 - Article
SN - 0027-8424
VL - 117
SP - 32891
EP - 32901
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 52
ER -