ABSTRACT Alzheimer’s disease (AD) is the most common type of dementia and the 6th leading cause of death in the United States. The main pathological features of AD are the brain deposition of misfolded forms of amyloid-beta (Aβ) and tau proteins. Compelling evidence demonstrate that these proteins share several characteristics with infectious prions, including their mechanisms of spread and disease transmission in experimental animals. Considering that prion diseases can be transmitted through contaminated materials (one of the focuses of the current R01 application), concerns have been raised on whether pathological features of AD can be transmitted in a similar way. In this application, we will explore this possibility using in vitro and in vivo assays. Specifically, the ability of Aβ- and tau- exposed materials to spread pathological conformations will be tested by: (i) in vitro aggregation assays, and (ii) surgical procedures using contaminated surgical instruments. In parallel, we will explore whether different decontamination methods used in clinical and research settings are able to decrease binding of misfolded proteins and their ability to propagate. Results from this research could help to address an important concern related to the prion-like transmission of misfolded proteins and may be useful for other cerebral and systemic proteinopathies.