Sohail Lab @ Swarthmore College

Understanding Peptide Self-Assembly Using Fluorescence Imaging


In the Sohail Lab, we aim to gain physical insight into protein self-assembly and how to better control it for biomaterial applications. The core of our research uses Fluorescence Lifetime Imaging Microscopy (FLIM) to assess mixtures of fibrils with distinct morphologies at the single fibril level.

What are the chemical and physical driving forces of amyloid assembly?

The kinetics of amyloid formation for functional and disease-related amyloids have been shown to be strongly affected by ionic strength. However, amyloid formation is dependent on complex protein-protein interactions, making it difficult to predict how ionic interactions will affect amyloid formation. There have been limited studies characterizing how screening effects modulate assembly. We will compare how NaCl concentration and Hofmeister ions modulate the diversity of polymorphs for the disease-related amyloid-β (Aβ) 42 peptide and the R5 repeat fragment of the functional bacterial amyloid protein CsgA (Curli).