Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene. Academic Article

abstract

• The interaction of amyloid -sheet segments with graphene-flake models is investigated by using DFT calculations. The structure of -sheets of selected amyloid segments is based on crystal structures obtained from the Protein Data Bank. Our study, based on DFT calculations for model systems, indicates that the interaction in amyloid-graphene aggregates can be stronger than the interaction in the respective amyloid-amyloid aggregates. The results also indicate an important specific role of aromatic sidechains in amyloid-graphene interactions. This work confirms recent experimental evidence that graphene and its modifications inhibit the aggregation of -amyloid peptides.

authors

• Belic, Milivoj

published proceedings

• Chemphyschem

altmetric score

• 0.5

author list (cited authors)

• Boinovski, D. M., Petrovi, P. V., Beli, M. R., & Zari, S. D.

citation count

• 6

complete list of authors

• Božinovski, Dragana M||Petrović, Predrag V||Belić, Milivoj R||Zarić, Snežana D

publication date

• May 2018

publisher

• Wiley  Publisher

published in

• n1439-4235ISSN  Journal

keywords

• Aggregation
• Amyloid Beta-Peptides
• Density Functional Calculations
• Graphene
• Graphite
• Noncovalent Interactions
• Quantum Theory

PubMed Central ID

• 28949054

Digital Object Identifier (DOI)

• 10.1002/cphc.201700847

start page

• 1226

end page

• 1233

volume

• 19

issue

• 10

URL

• http://dx.doi.org/10.1002/cphc.201700847