Exploiting extremophilic proteins as robust biological components for advanced biomaterials

Lead Research Organisation: University of Leeds
Department Name: Astbury Centre

Abstract

Background: Mechanical robustness is an essential property of biological scaffolds. This includes the remarkable combination of high mechanical strength, fracture toughness and elasticity in the muscle protein titin and the intriguing mechanical properties of natural silk fibres. Biological scaffolds offer attractive model systems for the design of advanced biomaterials. In particular, proteins from extremophile organisms present interesting opportunities to rationally engineer or re-engineer robust biological materials for exploitation.

Objectives: We will exploit proteins from extremophile organisms to make biomaterials with advanced mechanical and thermal stability properties. By understanding the properties of the building block (the extremophilic proteins) we will have predictive control of the biomaterial. This approach will bridge the gap between single molecule mechanics and material biomechanics, revealing how the mechanical properties of individual components are translated to the properties of macroscopic materials.

Novelty: The project will lead to the development of extremophilic protein-based hydrogels which are promising biomaterials for a number of applications due to their high water content, tuneable mechanical properties and biocompatibility. The project has three outputs: i) production and characterization of extremophilic protein constructs using single molecule forces spectroscopy. ii) production of novel biomaterials using extremophile protein components iii) development of tools for the rational design of extreme biomaterials with specific properties.

Timeliness: Studies on the mechanical properties of proteins found in nature have provided inspiration for the design of biomimetic biopolymers that have a balance of advanced material properties. These studies are revealing that the mechanical characteristics of proteins are determined by important non-covalent interactions which define their unique molecular structure. Understanding the importance and role of these non-covalent interactions will allow fundamental understanding of the biological scaffold.

Experimental Approach: The project will involve state-of-the-art single molecule force spectroscopy to characterize the mechanical properties of extremophilic proteins in environmental extremes of temperature and solvent environment. It will exploit a recently developed photo-crosslinking technology for the production of protein-based hydrogels.

Publications

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Studentship Projects

Project Reference Relationship Related To Start End Student Name
BB/M011151/1 30/09/2015 29/09/2023
1775206 Studentship BB/M011151/1 30/09/2016 30/03/2021 Alexander Wright
 
Description - How much protein still works after gelation
- How efficiently protein gels are bound together
- relationship between number of bonds per molecule and gel strength
Exploitation Route Comprehensive understanding of relationships between concentration, crosslink density, folded fraction, network topology, and a wider range of mechanical properties
Sectors Agriculture, Food and Drink,Healthcare,Manufacturing, including Industrial Biotechology,Pharmaceuticals and Medical Biotechnology