Self-Templated Nucleation in Peptide and Protein aggregation

Details Self-Templated Nucleation in Peptide and Protein aggregation Self-Templated Nucleation in Peptide and Protein aggregation

2009-01-13

arxiv.org/abs/0901.1846v1

Phys. Rev. Lett., 101, 258101 (2008)

Biology

Quantitative Biology

Biomolecules

4 pages, 3 figures

Scientific paper

10.1103/PhysRevLett.101.258101

Peptides and proteins exhibit a common tendency to assemble into highly ordered fibrillar aggregates, whose formation proceeds in a nucleation-dependent manner that is often preceded by the formation of disordered oligomeric assemblies. This process has received much attention because disordered oligomeric aggregates have been associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. Here we describe a self-templated nucleation mechanism that determines the transition between the initial condensation of polypeptide chains into disordered assemblies and their reordering into fibrillar structures. The results that we present show that at the molecular level this transition is due to the ability of polypeptide chains to reorder within oligomers into fibrillar assemblies whose surfaces act as templates that stabilise the disordered assemblies.

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