Supervisors: Prof Naba Dutta and Prof Namita Roy Choudhury
Aim: To understand, control and exploit the unique chemical and hierarchical structures in resilin protein for promising applications.
Elastic proteins occur in a wide range of biological systems, where they have been evolved to fulfil precise biological roles. Resilin is the most efficient elastomeric protein known and is present in most, if not all insects, where it has been adapted for flight, jumping and sensory mechanisms. The most dramatic example of the effect of resilin is the jumping power of fleas.
Over the past number of years, synthetic polymer gels have been employed to create many artificial soft machines such as gel valves, chemical motors, artificial muscles, etc; however, the lack of hierarchical structures in the synthetic polymers lead to a decreased response and restricted their further applications for practical uses. Currently, elastomeric proteins attract significant research interest due to: (i) their biological and medical significance, particularly in human disease; and (ii) their unusual properties provide opportunity to develop novel materials for diverse application. In this project we propose to investigate the idea of using the sequence of the protein resilin as a building block for polymer structures that emulate the remarkable properties of resilin.
Resilin exhibits unusual elasomeric behaviour only when swollen in polar solvents such as water. The resultant polymer is expected to emulate the unique elstomeric and fatigue resistance characteristic of natural resilin only in the gel state. Therefore, different means of forming and optimising hydrogels using crosslinks in the soluble recombinant protein will be crucial. Extensive investigation on the structures, origin of elasticity, thermodynamic, kinetics, morphology and biomechanical properties of the swollen crosslinked resilin; will be the goal of the project.