Purification and Characterization of a Membrane Sculpting Bacterial BAR Domain-Containing Protein for Engineering Tunable Scaffolds into Novel Biological Metamaterials
Abstract
Metamaterial construction relies upon the ability to introduce precise features in surfaces at size scales proportional to the wavelength of the radiation being manipulated. Biology excels at forming precise structures on the nanometer to micrometer scale, but a fundamental understanding of the processes involved in their formation is essential to engineer these structures in a controlled manner. The ordered tubules formed through interaction between Bin/Amphiphysin/Rvs (BAR) domain-containing proteins and lipids fall within the diameter and length range required to affect visible light. A novel bacterial BAR domain-containing protein (BdpA) was investigated for its membrane sculpting capabilities both within the context of in vitro interaction between purified protein and liposomes and in vivo through protein expression and membrane extension formation. Predicted structures generated of BdpA show a characteristic BAR domain-like appearance and provide potential targets for engineering through targeted mutagenesis. Negative stain transmission electron microscopy experiments show that purified BdpA resembles previously characterized BAR domain proteins with intrinsic curvature and the predicted structure model. These initial experiments will serve to baseline future engineered membrane sculpting proteins towards the goal of using BAR domain protein-mediated tubule formation to generate tunable scaffolds for templating conductive structures, paving the way for biologically engineered metamaterials.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 25, 2022
- Accession Number
- AD1165367
Entities
People
- Aleksandr E. Miklos
- Barbara Smith
- Brian J Eddie
- Daniel A Phillips
- Duncan Sousa
- Jennifer A Lee
- Kelley Betts
- Patricia E. Buckley
Organizations
- Defense Threat Reduction Agency
- Johns Hopkins School of Medicine
- Oak Ridge Institute for Science and Education
- United States Army Combat Capabilities Development Command
- United States Naval Research Laboratory