Atomic structure, assembly, interactions and engineering of functional amyloids

Summary

This project aims to engineer hydrophobins for a range of biotechnological applications from coating of medical implants to formulation of drug delivery vehicles. The work includes protein engineering, determining the atomic structure of engineered proteins to examining how they interact with a range of substrate including nanomaterials. The insights obtained will be applied to the development of anti-fungal agents and novel biomaterials.

Supervisor(s)

Dr Ann Kwan

Research Location

School of Life and Environmental Sciences

Program Type

Masters/PHD

Synopsis

Hydrophobins are fungal proteins that spontaneously self-assemble at hydrophobic:hydrophillic interfaces to form robust and amphipathic coatings.

In nature, hydrophobin coatings provide protection and water proofing of fungal structures e.g. spores, as well as mediate interactions with hosts during fungal infections.

Advantages of hydrophobins in biotech applications include: spontaneous self-assembly, robust coating, structure tolerant to mutations including additional of functional groups, biocompatibility and non-immunogenicity

We have shown that hydrophobins can be modified to have reactive groups at specific positions that enable biotech applications.

Can we expand the functionality of hydrophobin coatings through “smart” protein engineering?

Together with researchers at the Chris O’brien Lifehouse, we are currently engineering hydrophobins that can promote the adhesion and growth of osteoblasts in PEEK bone implants.

Another direction of the project is to discover conditions and reagents that control and inhibit hydrophobin assembly as anti-fungal agents.

This project is part of an ARC Discovery Project funded for 2020-2022.

Additional Information

Additional supervisor Assoc Prof Margaret Sunde


HDR Inherent Requirements


In addition to the academic requirements set out in the Science Postgraduate Handbook, you may be required to satisfy a number of inherent requirements to complete this degree. Example of inherent requirement may include:

- Confidential disclosure and registration of a disability that may hinder your performance in your degree;
- Confidential disclosure of a pre-existing or current medical condition that may hinder your performance in your degree (e.g. heart disease, pace-maker, significant immune suppression, diabetes, vertigo, etc.);
- Ability to perform independently and/or with minimal supervision;
- Ability to undertake certain physical tasks (e.g. heavy lifting);
- Ability to undertake observatory, sensory and communication tasks;
- Ability to spend time at remote sites (e.g. One Tree Island, Narrabri and Camden);
- Ability to work in confined spaces or at heights;
- Ability to operate heavy machinery (e.g. farming equipment);
- Hold or acquire an Australian driver’s licence;
- Hold a current scuba diving license;
- Hold a current Working with Children Check;
- Meet initial and ongoing immunisation requirements (e.g. Q-Fever, Vaccinia virus, Hepatitis, etc.)

You must consult with your nominated supervisor regarding any identified inherent requirements before completing your application.

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Keywords

hydrophobin, amyloid, interactions, protein engineering, biomaterial, structure biology, protein self-assembly, Biophysics

Opportunity ID

The opportunity ID for this research opportunity is: 1900

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