Amyloid beta is a 42 amino acid peptide that is associated with Alzheimer’s Disease (AD).  In its oligomeric form, the peptide kills neuronal cells, possibly commencing a process leading to the start of AD.  There are considerable efforts to find ways to reduce the oligomerisation of amyloid beta, through direct binding/blocking agents.  Other approaches are to reduce the levels of the peptide through autophagic responses.  In our studies yeast have been genetically engineered to understand how to ameliorate amyloid beta toxicity.  Amyloid beta has been fused to green fluorescent protein (GFP) to enable its visualisation and oligomerisation in real time.  Yeast can reasonably model aging due to the budding process.  A mother yields a bud a every cell division so daughter cells comprise 50% of the population and mothers the remaining 50%.  Each new bud leaves a scar that is readily visualized so the age of a mother cell can be readily ascertained.  We show that the youngest cells remove the amyloid beta-GFP using autophagy, while the oldest cells retain it.  The cells of intermediate age that have the fusion can be induced to degrade the fusion protein and reduce fluorescence using drugs that increase autophagy.  For example, Dimebon, a drug used in AD has been shown to reduce the green fluorescence.  Some compounds that inhibit oligomerisation in vitro have been shown to increase green fluorescence indicating that they are bioavailable and inhibit oligomerisation in vivo as well.  The manipulated yeast offer a convenient method of in vivo screening for compounds that affect amyloid beta within cells.