TCP Seminar: Ali HAKAMI ZANJANI

Many serious progressive diseases such as Alzheimer’s and Parkinson’s are related to undesirable amyloid aggregation. From a positive perspective, functional amyloids have applications as robust and versatile biomaterials in nature, nanotechnology, and biomedicine. In this work the thermodynamics and aggregation kinetics of the ILQINS hexapeptide, a biological material derived from hen’s egg-white lysozyme, are studied. Also solution X-ray scattering and X-ray crystallography of the IFQINS hexapeptide as the human homologue of ILQINS are compared to simulation, verifying that at least two metastable polymorphic structures exist for this system which are substantially different at the atomistic scale.