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BEGIN:VEVENT
DTSTAMP:20260828T214213Z
LAST-MODIFIED:20121116T203436Z
DTSTART:20071116T183000Z
DTEND:20071116T193000Z
UID:event176@bu.edu
URL:http://physics.bu.edu/internal/events/show/176
SUMMARY:"Ab Initio Discrete Molecular Dynamics Approach to Studies of Alzhe
	imer’s Amyloid β-Protein Folding and Assembly" 
DESCRIPTION:Featuring Brigita Urbanc\, Boston University\n\nPart of the Bio
	physics/Condensed Matter Seminar Series.\n\nAbstract: Misfolding and self-a
	ssembly of proteins into nanoaggregates of different sizes and morphologies
	 is a common theme unifying a number of human pathologies termed protein mi
	sfolding diseases.  Discrete molecular dynamics (DMD) approach combined wit
	h a coarse-grained protein model has been recently developed to study such 
	biologically relevant processes.  Using this efficient computational approa
	ch\, I will introduce a study of early events of amyloid -protein (Aβ) 
	assembly\, which are believed to be critical to the onset of Alzheimer's di
	sease.  Substantial evidence supports the notion that small soluble Aβ ass
	emblies are toxic to cells.  Recent experimental studies demonstrated that 
	Aβ-derived peptide fragments\, when added to Aβ in cell cultures\, inhibi
	t Aβ toxicity.  I will describe a recent application of the DMD approach t
	o examine the effect of the peptide inhibitors on Aβ assembly\, and the re
	sulting structural insights relevant to understanding of Aβ toxicity.
LOCATION:SCI 352\, 590 Commonwealth Avenue\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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