- Self-assembly of functionalized colloids and short amyloidogenic peptides: Modelling, theory and simulations
- Award date
- 11 November 2015
- Number of pages
- Document type
- PhD thesis
- Faculty of Science (FNWI)
- Van 't Hoff Institute for Molecular Sciences (HIMS)
In nature, self-assembly occurs on all scales. We try to understand such processes so that we can, for instance, create nanostructures in a 'bottom up' way, or even interrupt the process such as the unwanted aggregation of proteins in the human body. These processes often take place on time- and lengthscales inaccessible to conventional microscopic methods, therefore we use theory and simulations to better understand them.
We studied the self-assembly of polymer-coated colloids into nanostructures using simple simulation models and the Monte Carlo method. These structures can be used to tailor materials with unique physical properties, such as flame resistance, conductivity, flexibility, etc. The models are based on the minimal interactions that underlie the self-assembly process, while they can qualitatively reproduce experimental observations. This makes the model fast and we obtain direct insight into the aggregation mechanism.
The self-assembly of proteins in the human body leads to a range of unwanted neurological disorders. This process is however still poorly understood. We showed that we can map the thermodynamical and kinetic properties of three different protein segments, GNNQQNY, KLVFFAE and VEALYL, using the hydrophobic and hydrogen bond interactions as a driving force. This lead to the prediction of a polymerized fluid of peptides which we could validate using molecular simulations. The discovery of this phase is potentially relevant for understanding the stability of oligomers in the brains of patients with e.g. Alzheimer's or Parkinson's disease.
- Research conducted at: Universiteit van Amsterdam
Thesis (complete) (Embargo until 11 November 2017)
4: Self-assembly of virus-like shells via colloidal bond hybridization and anisotropy (Embargo until 11 November 2017)
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