Chemistry of Biological Nanoassemblies

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Living organisms have always been an inestimable source of inspiration for the design of biomaterials for medical and nanotechnological applications. Endogenous peptides and proteins are known for their unique ability to self-associate and the resulting supramolecular structures are performing vital physiological functions in host, as exemplified by spider silk and byssus from bivalve molluscs. The overarching goal of the Canada Research Chair in Chemistry of Biological Nanoassemblies is to expand the fundamental study of protein self-assembly into different supramolecular architecture in order to manipulate self-recognition. We will take advantage of this knowledge to design functionalized proteinaceous assemblies for applications in vaccination and to explore innovative opportunities in (bio)nanotechnology. While the proposed research program mainly focuses on amyloid fibrils, other protein nanostructures, such as those inspired by bacterial flagella and pilus, will also be engineered. Amyloids are highly organized proteinaceous nanostructures that have been historically associated with pathological states. Over the last decade, amyloid structures that accomplish essential biological activities have been identified in almost all species, from bacteria to mammals. The stability and mechanical properties of amyloids suggest that they hold great potential as biomaterials. However, the use of amyloids is still limited by the incomplete understanding of the mechanisms of self-assembly, difficulty to control the final supramolecular architecture and lack of understanding of their biological/immunological properties. To address these issues, the following specific aims will be conducted: (i) design tools to manipulate and probe amyloid self-assembly, (ii) harness cross-ß-sheet assemblies to design self-adjuvanted antigen delivery system, (iii) identify novel bacterial self-assembling proteins as nanovaccine scaffolds, (iv) expand the scope of applications for amyloid fibrils. Due to their historical association with diseases, amyloids have gathered limited attention as biomaterials despite their remarkable properties. By combining (bio)chemical, biophysical and biological approaches, this research chair program will lead to strategies to manipulate proteinaceous assemblies and will uncover novel functionalities. This program will allow the demystification of these protein nanostructures, fostering their applications in vaccine design and (bio)nanotechnology.