Engineers reveal molecular mysteries of cephalopod powers

Engineers uncover molecular mysteries of cephalopod powers

“This research can be seen as a valuable conceptual framework for the use of this class of proteins in bioengineering applications,” said Alon Gorodetsky, UCI associate professor of chemical and biomolecular engineering. Cliu: Debbie Morales / UCI

Reflectins, the unique structural proteins that enable squids and octopuses to change colors and blend in with their surroundings, are thought to have great potential for innovations in such diverse fields. to electronics, optics and medicine. Scientists and entrepreneurs have been entwined in their efforts to give full power to these biomolecules due to their acetic chemical content and their sensitivity to environmental change.

In a study recently published in the Proceedings of the National Academy of Sciences, University of California, Irvine researchers have revealed the structure of a reflectin variable at the molecular level, and have demonstrated a method for mechanically controlling the hierarchical composition and optical properties of the protein. These findings are seen as key steps in exploiting many of the potentially useful features in the reflectin family.

“My lab at UCI has been working for a long time to mimic the scattering powers of light and light-emitting cephalopods with the goal of creating new classes of adaptive thermoregulatory clothing and other everyday technologies,” he said. co-author Alon Gorodetsky, UCI associate professor of chemical and biomolecular engineering. ”With this research, we have focused on developing a detailed basic understanding of how reflectins work at the molecular level. “

Gorodetsky said scientists are attracted to reflectins because, like other protein-based products, they offer many beneficial properties such as controllable self-assembly, stimulus-response, customizable functionality and compatibility. with other biological systems. The biomaterials models have also shown their usefulness for modifying the remodeling index of human cells and supporting the growth of cloud cells.

In their laboratory at UCI’s Henry Sameuli School of Engineering, Gorodetsky and his colleagues used bioinformatics prediction to select a variety of reflectin, extracted the protein in bacteria and developed solution conditions to maintain it. in a stable condition.

The researchers then used several devices to analyze the protein and its solutions, including molecular dynamics simulations, small-angle X-ray scattering, and a nuclear magnetic resonance spectroscope. They also examined the complex protein ensembles assembled by methods such as atomic force microscope and three-dimensional holotomographic microscope. These methods allowed the team to evaluate the full range of properties and properties for the reflectin variable.

“Through our computational and synergistic experimental approaches, we were able to define the three-dimensional structure of the reflectin variable, thus establishing a direct correlation between the structural properties of the protein and inherent optical properties,” Gorodetsky said. . “This research can be seen as a valuable conceptual framework for the use of this class of proteins in bioengineering applications.”

Gorodetsky said the work of his team will enable new methods for processing materials based on reflection and identify new avenues for conventional tailor-made films of the protein at the nano- and micrometer meters, which would be beneficial for applications biophotonic and bioelectronic as well as for promoting the design of polymeric materials with diffuse light scattering capabilities. He also said that the approach used in this project could help to better understand the mechanisms that underlie the ability of cephalopods to change color.

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Further information:
Mehran J. Umerani et al, Structure, self-assembly, and properties of a truncated reflectin variable, Proceedings of the National Academy of Sciences (2020). DOI: 10.1073 / pnas.2009044117

Presented by the University of California, Irvine

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