T. John1,2,3, L.L. Martin3, H.J. Risselada1,4, and B. Abel1,2
1Leibniz Institute of Surface Modification, Leipzig (Germany)
2Wilhelm-Ostwald-Institute for Physical and Theoretical Chemistry, Leipzig University, Leipzig (Germany)
3School of Chemistry, Monash University, Clayton (Australia)
4Department of Theoretical Physics, Georg-August-University Göttingen, Göttingen (Germany)
Amyloid peptides aggregate into characteristic fibrils with cross-β-sheet structure, also known as amyloid plaque. They are associated with several diseases such as Alzheimer’s disease or type II diabetes. However, there is evidence that indicates the soluble transient oligomers, instead of mature fibrils, as the toxic species. Amyloid-forming peptides are natively soluble and only aggregate under certain circumstances. Comprehensive knowledge on the aggregation mechanism and a detailed characterisation of the transient species is essential to understand the physiological role of these peptides .
Interfaces, such as nanoparticles, can act to accelerate or inhibit peptide aggregation. Experimental studies and molecular dynamics simulations (MD) presented an accelerated fibril formation in the presence of citrate-stabilised gold nanoparticles [2,3]. The role of gold surfaces in oligomer formation and peptide aggregation is discussed in this study. Moreover, possible mechanisms for the observed acceleration of the peptide aggregation by a reduction of the conformational space that is sampled are presented.
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