Protein self-assembly on surfaces, interfaces and nanoparticles

In this project we apply advanced computer modelling techniques to investigate the role of surfaces and nanoparticles in amyloid fibril formation.

One of the greatest challenges currently posed by the industrial uptake of nanomaterials is the lack of understanding of the interactions of these novel molecular systems with biological environments. Nanomaterials present a high surface area that can interact with proteins and promote a locally increased protein concentration leading to aggregation. A specific type of protein aggregation caused by the partial misfolding and self-association of proteins to form insoluble amyloid fibrils occurs in a number of common and debilitating diseases, including Alzheimer’s and Parkinson disease. We have been studying amyloid fibril formation by human apolipoprotein (ApoC-II) as a model to explore the factors that affect the self-assembly process.

Outcomes of the work include a molecular level understanding of protein misfolding related to disease, a rational basis for designing inhibitors to protein aggregation and the establishment of design principles for novel nanomaterials via controlled self assembly of proteins and peptides on surfaces.

Atomistic model of an amyloid fibril interacting with a fullerene, nanotube and graphene surfaces. Atomistic model of an amyloid fibril interacting with a fullerene, nanotube and graphene surfaces.

Key people


  • Associate Professor Geoff Howlett, Bio21 Institute, University of Melbourne
  • Dr Michael Griffin, Bio21 Institute, University of Melbourne
  • Dr Arash A. Mostofi, Department of Materials and Physics, Imperial College London UK
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Acknowledgement of country

RMIT University acknowledges the people of the Woi wurrung and Boon wurrung language groups of the eastern Kulin Nation on whose unceded lands we conduct the business of the University. RMIT University respectfully acknowledges their Ancestors and Elders, past and present. RMIT also acknowledges the Traditional Custodians and their Ancestors of the lands and waters across Australia where we conduct our business.