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Details of Grant 

EPSRC Reference: EP/S017542/1
Title: Custom nanomaterials from modular synthetic proteins
Principal Investigator: Parmeggiani, Dr F
Other Investigators:
Researcher Co-Investigators:
Project Partners:
Department: Chemistry
Organisation: University of Bristol
Scheme: EPSRC Fellowship
Starts: 01 April 2019 Ends: 31 March 2024 Value (£): 1,151,785
EPSRC Research Topic Classifications:
Biomaterials Protein engineering
Synthetic biology
EPSRC Industrial Sector Classifications:
No relevance to Underpinning Sectors
Related Grants:
Panel History:
Panel DatePanel NameOutcome
29 Jan 2019 Engineering Fellowship Interview Panel Meeting Announced
06 Dec 2018 Engineering Prioritisation Panel Meeting 6 and 7 December 2018 Announced
Summary on Grant Application Form
Science and technology constantly strive to develop sustainable materials and processes. Biology is an extremely rich source of solutions to similar problems that bacteria, fungi, animals and plants face, such as adhesion, specific recognition, tensile strength and resistance to impact. These solutions are often the result of interactions happening at the micro- and nano-scale between proteins that work together to form hierarchical structures. Although these natural building blocks have been shaped by evolution, proteins have been successfully repurposed for new tasks by researchers. However, this is not always possible, as proteins are often intrinsically related to the biological system where they come from by evolutionary and environmental constraints that are hard to underpin. Indeed, despite decades of efforts and numerous advancements, synthetic silk is still far away from the properties of silk produced by spiders. Therefore, it is important to start considering, in a truly synthetic-biology approach, the use of custom proteins that, from the beginning, offer favourable characteristics for large scale production and processing. While, for specific recognition and catalysis, we are still mostly reliant on existing proteins and their modification, it is now possible to design and produce novel protein structures. This process requires a high level of expertise, substantial funding and time, which effectively limit the application of these methods outside a restricted circle of experts.

The goal of this project is to develop a computational and experimental platform for rapid and reliable design of custom protein structures, whether that is a new vaccine, a layer in an ultra-light composite material for airplanes, or a miniaturized electronic component. A platform of this kind would allow cell biologists, material scientists and electric engineers to consider tailored biological tools to tackle scientific problems and develop novel specific solutions. In a way, this is similar to how people take pictures and print them, focusing on the content without having to know how digital cameras and laser printers work. This is possible by using a set of predefined protein building blocks with known structures, properties and interactions with each other. Large custom structures and their properties emerge from the combination of these building blocks, and they can be rapidly predicted, indicating which design is a viable solution for a specific problem.

While developing this platform, I will partner with experts in other fields where these concepts can be applied. In collaboration with aerospace engineers, we will design protein nanomaterials with defined mechanical properties, able to withstand impact and improve the durability of composite materials. With cell biologists, we will develop proteins able to interact with the cytoskeleton that determine cell shape and motility, and understand how mechanical forces generated internally affect cell behaviour. In collaboration with the NIHR Bristol Blood and Transplant Research Unit (BTRU), we will design structures able to display multiple cellular signals to improve growth of tissues from patient stem cells, making regenerative medicine approaches available to everybody at a fraction of the cost.

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Organisation Website: http://www.bris.ac.uk