By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Computational Biology. According to news reporting originating from Melbourne, Australia, by NewsRx correspondents, research stated, "Experimental studies have demonstrated that nanoparticles can affect the rate of protein self-assembly, possibly interfering with the development of protein misfolding diseases such as Alzheimer's, Parkinson's and prion disease caused by aggregation and fibril formation of amyloid-prone proteins. We employ classical molecular dynamics simulations and large-scale density functional theory calculations to investigate the effects of nanomaterials on the structure, dynamics and binding of an amyloidogenic peptide apoC-II(60-70)."
Our news editors obtained a quote from the research from Research Institute, "We show that the binding affinity of this peptide to carbonaceous nanomaterials such as C60, nanotubes and graphene decreases with increasing nanoparticle curvature. Strong binding is facilitated by the large contact area available for ?-stacking between the aromatic residues of the peptide and the extended surfaces of graphene and the nanotube. The highly curved fullerene surface exhibits reduced efficiency for ?-stacking but promotes increased peptide dynamics. We postulate that the increase in conformational dynamics of the amyloid peptide can be unfavorable for the formation of fibril competent structures."
According to the news editors, the research concluded: "In contrast, extended fibril forming peptide conformations are promoted by the nanotube and graphene surfaces which can provide a template for fibril-growth."
For more information on this research see: Dimensionality of carbon nanomaterials determines the binding and dynamics of amyloidogenic peptides: multiscale theoretical simulations. Plos Computational Biology, 2013;9(12):e1003360. (Public Library of Science - www.plos.org; Plos Computational Biology - www.ploscompbiol.org)
The news editors report that additional information may be obtained by contacting N. Todorova, Health Innovations Research Institute, Melbourne, Australia. Additional authors for this research include A.J. Makarucha, N.D. Hine, A.A. Mostofi and I. Yarovsky (see also Computational Biology).
Keywords for this news article include: Peptides, Proteins, Melbourne, Amino Acids, Computational Biology, Australia and New Zealand.
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