Prions are infectious agents responsible for transmissible spongiform encephalopathies (TSEs), a class of fatal neurodegenerative diseases in many mammals, including humans. The infectious prion protein, PrPSc, propagates by converting the non-pathological conformation of the prion protein, PrPc, into the misfolded PrPSc. It is unclear how infectious PrPSc initially arose, and the mechanism behind the misfolding, conversion, and replication of PrPSc is still widely debated. Since PrPc is found extracellularly and GPI-anchored to the cell membrane, gaining insight on prion-membrane interactions is required to shed light on these uncertainties. In this presentation, we will discuss our results based on biomolecular modeling techniques to identify favorable modes of interaction of the PrPc molecule with model membranes.