Abstract:

The neuronal membrane bound prion protein has been of substantial interest as it is
impliciated in the sole ``protein-only'' class of infectious diseases known (e.g., mad cow
disease). The prion protein exists in two forms, a normal ``cellular'' form of unknown
function, and the anomalous “scrapies'' form associated with infection and disease,
which has the remarkable ability to autocatalytically convert the cellular form to the
scrapies form.

In this talk I will review the work of my collaborators and myself on theoretical
modeling of: (i) the statistical mechanics of prion aggregation on neuronal and the use
of it to describe prion epidemiology and dose incubation curves, (ii) a new model for the
minimal infectious unit of prion proteins based upon the emerging concept of domain
swapping, (iii) the possible role of copper binding to protect against prion disease, and
(iv) the role of the membrane in mediating both toxicity and infectivity of the prion
disease. I will first introduce the general study of amyloid diseases and prion disease
concepts in particular.