For information about this Alzheimer's lecture series, see:
http://int.lanl.gov/news/index.php/fuseaction/nb.story/story_id/13644/nb_date/2008-06-19----------------------------------------------------------------------------
Proteins behaving badly: Link between misfolding and Alzheimer's disease
Gnana Gnanakaran
Research Talk Background:
Proteins need to adopt three-dimensional shapes (native fold) to
function properly. Information needed to adopt the native fold is
encoded in the chain of aminoacids that are easily obtained from genome
sequencing projects. However, the protein folding problem, how a linear
chain of amino acids attains the functional shape, still remains a
challenging research activity. When a protein misfolds, cellular
mechanisms are in place to detect and degrade it before it can become
toxic. Despite these efforts, a range of debilitating human diseases is
associated with protein misfolding. Lately, most attention has been paid
to a group of diseases where proteins or peptides convert from their
normally soluble forms to aggregates of insoluble fibrils or plaques.
The final forms of these aggregates often have an ordered assembly of
cross¾-sheet fibrils and referred as amyloids. The deposits of amyloid
are associated with at least 20 diseases, including such diverse
entities as Alzheimer's disease, prion disease, type 2 diabetes
mellitus, Parkinson's disease and Huntington's disease. In this talk we
will present results from all-atom computer simulations that considered
the monomer and oligomers of the aggregation-prone fragment of amyloid
beta peptide which is implicated in the Alzheimer's disease. These
simulations are motivated by the clinical studies that have suggested
oligomers as the possible pathological agents. We provide a thorough
understanding of oligomer formation with detailed picture of forces that
drive the interaction between fragments. Collaborative research with
Ruth Nussinov (National Cancer Institute) and Angel Garcia (RPI).
Calculations were carried out on PINK as part of the institutional
computing project at LANL. Funded by LANL/DOE LDRD program
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