Protein fibrillation and nanoparticle interactions: opportunities and challenges

Nanoscale. 2013 Apr 7;5(7):2570-88. doi: 10.1039/c3nr33193h.

Abstract

Due to their ultra-small size, nanoparticles (NPs) have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. NPs are recognized as promising and powerful tools to fight against the human brain diseases such as multiple sclerosis or Alzheimer's disease. In this review, after an introductory part on the nature of protein fibrillation and the existing approaches for its investigations, the effects of NPs on the fibrillation process have been considered. More specifically, the role of biophysicochemical properties of NPs, which define their affinity for protein monomers, unfolded monomers, oligomers, critical nuclei, and other prefibrillar states, together with their influence on protein fibrillation kinetics has been described in detail. In addition, current and possible-future strategies for controlling the desired effect of NPs and their corresponding effects on the conformational changes of the proteins, which have significant roles in the fibrillation process, have been presented.

Publication types

  • Review

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Humans
  • Kinetics
  • Models, Biological*
  • Models, Molecular*
  • Nanoparticles / chemistry*
  • Protein Binding
  • Protein Multimerization*

Substances

  • Amyloid beta-Peptides