Controlling self-assembly of amyloids and designed peptides
Fritz Haber Seminar: Yifat Miller, Dept.  of Chemistry, Ben Gurion University of the Negev

The pathological self-assembly (or aggregation) of amyloid proteins into toxic aggregate species plays important
role in amyloidogenic diseases, such as Alzheimer’s disease (AD). One of the amyloids that have been implicated
in the development of AD is amyloid β (Aβ). Metal ions are factors that induce the self-assembly of Aβ. The
first part of the lecture will focus on peptides and proteins that able to inhibit the initial seeding of the self-
assembly of Aβ. The peptides that demonstrated bifunctional activity of controlling the self-assembly in presence
and in absence of metal ions are neuropeptides - small molecules that are produced and released by neurons.1,2
The proteins that revealed inhibition of self-assembly of amyloids that our lab investigated recently are insulin3,4
and insulin degrading enzyme. In the second part of the lecture, a series of novel designed peptides that have
the capability to bind Zn2+ ions and to produce fibrillar structures will be presented.5 The location and the type
of the residues along the peptide sequence can determine the nature of the fibril. This work presents a proof-of-
concept milestone for designing peptides with different properties to control and produce diverse materials.