Atomic force microscopy to study the structure, micromechanical properties and aggregation kinetics of protein nanostructures


Misfolding of proteins leading to formation of fibrillar aggregates, called amyloid fibrils, is a process commonly associated with neurodegenerative disorders. The mechanism which leads to aggregation is not yet fully understood, however the aggregates are structures which appear to have very specific material properties. These proteins can be used in combination with nanostructured surfaces to create new nanomaterials.

The goal is to analyze different mechanical properties of amyloid fibrils formed by the protein α-synuclein. Furthermore topographic or chemical controlled surfaces should be created combined with the correct environment conditions to be able to specifically grow the fibrils.


High-resolution AFM image of α-synuclein fibrils (E46K mutant) using ultra-sharp silicon probes with a diamond-like tip (DP18, HI’RES series, 3.5 N/m, 1 nm tip radius, MikroMasch).


PhD student: Kim Sweers
Project leader: Martin Bennink