Editing Folding@home (section)

=== Alzheimer's disease ===
{{Multiple image|footer= Alzheimer's disease is linked to the aggregation of amyloid beta protein fragments in the brain (right). Researchers have used Folding@home to simulate this aggregation process, to better understand the cause of the disease.|image1= Amyloid 01big1.jpg|image2= Amyloid 02big1.jpg|image3= Amyloid 03big1.jpg}}

[[Alzheimer's disease]] is an incurable [[neurodegeneration|neurodegenerative]] disease which most often affects the elderly and accounts for more than half of all cases of [[dementia]]. Its exact cause remains unknown, but the disease is identified as a [[proteopathy|protein misfolding disease]]. Alzheimer's is associated with toxic [[protein aggregation|aggregations]] of the [[amyloid beta]] (Aβ) [[peptide]], caused by Aβ misfolding and clumping together with other Aβ peptides. These Aβ aggregates then grow into significantly larger [[senile plaques]], a pathological marker of Alzheimer's disease.<ref name="10.2119/2007-00100.Irvine"/><ref name="10.1001/archneurol.2007.56"/><ref name="10.1074/jbc.R800036200"/> Due to the heterogeneous nature of these aggregates, experimental methods such as [[X-ray crystallography]] and [[nuclear magnetic resonance]] (NMR) have had difficulty characterizing their structures. Moreover, atomic simulations of Aβ aggregation are highly demanding computationally due to their size and complexity.<ref name="10.1063/1.3010881"/><ref name="10.1371/journal.pone.0021776"/>

Preventing Aβ aggregation is a promising method to developing therapeutic drugs for Alzheimer's disease, according to Naeem and Fazili in a [[literature review]] article.<ref name="10.1007/s12013-011-9200-x"/> In 2008, Folding@home simulated the dynamics of Aβ aggregation in atomic detail over timescales of the order of tens of seconds. Prior studies were only able to simulate about 10 microseconds. Folding@home was able to simulate Aβ folding for six orders of magnitude longer than formerly possible. Researchers used the results of this study to identify a [[beta hairpin]] that was a major source of molecular interactions within the structure.<ref name="10.1038/cr.2010.57"/> The study helped prepare the Pande lab for future aggregation studies and for further research to find a small peptide which may stabilize the aggregation process.<ref name="10.1063/1.3010881"/>

In December 2008, Folding@home found several small drug candidates which appear to inhibit the toxicity of Aβ aggregates.<ref name="typepad: possible alz. drug"/> In 2010, in close cooperation with the Center for Protein Folding Machinery, these drug leads began to be tested on [[biological tissue]].<ref name="diseases FAQ"/> In 2011, Folding@home completed simulations of several [[mutation]]s of Aβ that appear to stabilize the aggregate formation, which could aid in the development of therapeutic drug therapies for the disease and greatly assist with experimental [[nuclear magnetic resonance spectroscopy]] studies of Aβ [[oligomer]]s.<ref name="10.1371/journal.pone.0021776"/><ref name="10.1021/jm201332p"/> Later that year, Folding@home began simulations of various Aβ fragments to determine how various natural enzymes affect the structure and folding of Aβ.<ref name="forum: 6871"/><ref name="description: 6571"/>