Anti-biofilm Activity of Graphene Quantum Dots via Self-Assembly with Bacterial Amyloid Proteins

Yichun Wang; Usha Kadiyala; Zhibei Qu; Paolo Elvati; Christopher Altheim; Nicholas A. Kotov; Angela Violi; J. Scott VanEpps

PSMα1 by monitoring the changes in secondary structure of the individual peptides. PSMα1 peptide contains 21 amino acids and consist of a single amphipathic helix with a slight bend near the N-and C-terminal (Figure 5a) . 47 (Figure 5c) , which is consistent with the enhanced CD signal of β-turns at ≈208 nm. At the same time, the number of peptide configurations containing both helix and coils decreases by 3.0 %, but the distributions are affected differently: the residues involved in helix secondary structure decrease in both number and frequency, while the variance of the number of residues in a coil configuration increase (Figure 5d, e) . In other words, the peptide losses α-helix structure in favor of the formation of β-turns or coils. Overall, the formation of stable PSMα1/GQD complexes by electrostatic interactions leads to relevant changes in the secondary structure and peptide motifs, and therefore we expect the presence of GQDs to affect unfavorably the organization of PSMα1 All rights reserved. No reuse allowed without permission.