By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Proteomics. According to news reporting originating from Santa Barbara, California, by NewsRx correspondents, research stated, "The microtubule associated protein tau is essential for the development and maintenance of the nervous system. Tau dysfunction is associated with a class of diseases called tauopathies, in which tau is found in an aggregated form."
Our news editors obtained a quote from the research from the University of California, "This paper focuses on a small aggregating fragment of tau, (273)GKVQIINKKLDL(284), encompassing the (PHF6*) region that plays a central role in tau aggregation. Using a combination of simulations and experiments, we probe the self-assembly of this peptide, with an emphasis on characterizing the early steps of aggregation. Ion-mobility mass spectrometry experiments provide a size distribution of early oligomers, TEM studies provide a time course of aggregation, and enhanced sampling molecular dynamics simulations provide atomistically detailed structural information about this intrinsically disordered peptide. Our studies indicate that a point mutation, as well the addition of heparin, lead to a shift in the conformations populated by the earliest oligomers, affecting the kinetics of subsequent fibril formation as well as the morphology of the resulting aggregates. In particular, a mutant associated with a K280 deletion (a mutation that causes a heritable form of neurodegeneration/dementia in the context of full length tau) is seen to aggregate more readily than its wild-type counterpart."
According to the news editors, the research concluded: "Simulations and experiment reveal that the ?K280 mutant peptide adopts extended conformations to a greater extent than the wild-type peptide, facilitating aggregation through the pre-structuring of the peptide into a fibril-competent structure."
For more information on this research see: Initiation of assembly of tau(273-284) and its ?K280 mutant: an experimental and computational study. Physical Chemistry Chemical Physics, 2013;15(23):8916-28. (Royal Society of Chemistry - www.rsc.org/; Physical Chemistry Chemical Physics - pubs.rsc.org/en/journals/journalissues/cp)
The news editors report that additional information may be obtained by contacting L. Larini, Dept. of Physics, University of California at Santa Barbara, Santa Barbara, California 93106, United States. Additional authors for this research include M.M. Gessel, N.E. LaPointe, T.D. Do, M.T. Bowers, S.C. Feinstein and J.E Shea (see also Proteomics).
Keywords for this news article include: Peptides, Proteins, California, Proteomics, Santa Barbara, United States, North and Central America.
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