Selected article for: "fibril formation and secondary structure"

Author: Yichun Wang; Usha Kadiyala; Zhibei Qu; Paolo Elvati; Christopher Altheim; Nicholas A. Kotov; Angela Violi; J. Scott VanEpps
Title: Anti-biofilm Activity of Graphene Quantum Dots via Self-Assembly with Bacterial Amyloid Proteins
  • Document date: 2019_2_19
  • ID: e0sxynb1_20
    Snippet: In all the images, the contrast of the agglomerates was enhanced with increasing GQD concentration, which is associated with the tendency of GQDs to co-assemble with amyloid peptides. The delayed fibrillation for four days suggested that the kinetics of fibril formation changed in presence of GQDs which matches the expectations of the formation of 'decoy' complexes. Similarly to NPs, 42 these supramolecular structures affect the secondary structu.....
    Document: In all the images, the contrast of the agglomerates was enhanced with increasing GQD concentration, which is associated with the tendency of GQDs to co-assemble with amyloid peptides. The delayed fibrillation for four days suggested that the kinetics of fibril formation changed in presence of GQDs which matches the expectations of the formation of 'decoy' complexes. Similarly to NPs, 42 these supramolecular structures affect the secondary structure of peptides that serve as nucleation centers for fibrillation. Thus, binding of GQDs to PSM monomers or small prefibrillar oligomers is likely to hinder the formation of critical nuclei and elongation of the fibrils.

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