Exploring the influence of carbon nanoparticles on the formation of β-sheet-rich oligomers of IAPP₂₂₋₂₈ peptide by molecular dynamics simulation

PLoS One. 2013 Jun 5;8(6):e65579. doi: 10.1371/journal.pone.0065579. Print 2013.

Abstract

Recent advances in nanotechnologies have led to wide use of nanomaterials in biomedical field. However, nanoparticles are found to interfere with protein misfolding and aggregation associated with many human diseases. It is still a controversial issue whether nanoparticles inhibit or promote protein aggregation. In this study, we used molecular dynamics simulations to explore the effects of three kinds of carbon nanomaterials including graphene, carbon nanotube and C₆₀ on the aggregation behavior of islet amyloid polypeptide fragment 22-28 (IAPP₂₂₋₂₈). The diverse behaviors of IAPP₂₂₋₂₈ peptides on the surfaces of carbon nanomaterials were studied. The results suggest these nanomaterials can prevent β-sheet formation in differing degrees and further affect the aggregation of IAPP₂₂₋₂₈. The π-π stacking and hydrophobic interactions are different in the interactions between peptides and different nanoparticles. The subtle differences in the interaction are due to the difference in surface curvature and area. The results demonstrate the adsorption interaction has competitive advantages over the interactions between peptides. Therefore, the fibrillation of IAPP₂₂₋₂₈ may be inhibited at its early stage by graphene or SWCNT. Our study can not only enhance the understanding about potential effects of nanomaterials to amyloid formation, but also provide valuable information to develop potential β-sheet formation inhibitors against type II diabetes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Islet Amyloid Polypeptide / chemistry*
  • Molecular Dynamics Simulation*
  • Nanotubes, Carbon / chemistry*
  • Peptide Fragments / chemistry*
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Structure, Secondary
  • Surface Properties

Substances

  • Islet Amyloid Polypeptide
  • Nanotubes, Carbon
  • Peptide Fragments

Grants and funding

This work was supported by the National Natural Science Foundation of China (Grant No: 21103075, http://www.nsfc.gov.cn). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.