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Unravelling The Spontaneous Self-assembly Of ?-helical A?-peptides In Lipid Membranes By Analytical And Multiscale Approach | 12475
Journal of Alzheimers Disease & Parkinsonism
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The mechanisms underlying the neurotoxicity in Alzheimer?s disease are still under intense debate. As experimentally
shown, A? peptide, primary component of amyloid plaques, self assembles to aggregate that permeabilize membranes. By
a combination of multi scale simulations and analytical theory, we unveiled the early steps of the spontaneous self-assembly of
membrane-embedded ?-helical A? (1-40) peptides. The presence of distorted structures called ??frustrated helices?? was predicted
and confirmed by large scale Coarse Grained simulations while the stability of these helical structures has been validated by fully
atomistic simulations. In addition, CG simulations clearly evidenced mechanical stress on the membrane structure induced by
the presence of the growing assemblies. We believe that these findings will provide an alternative view to the traditional models
that consider a conformational transition towards b-sheet rich structures as a prerequisite for triggering membrane damage,
suggesting new potential targets for the drug treatment.
Martina Pannuzzo has completed her Ph.D. in Chemical Science in 2012 from University of Catania (Italy), and she has been awarded for the best
Italian Ph.D. thesis in Theoretical Biophysics, 2010-2012. She got several fellowships to visit important research groups in the field of Computational
Biophysics in the Netherlands and Canada. She is currently postdoctoral researcher in Computational Biology at the University of Erlangen-
Nuremberg, working in the field of membrane biophysics. She is the author of 9 papers published in well reputed chemical-physics journals.
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