Photosensitizing materials and platforms for light-triggered modulation of Alzheimer's β-amyloid self-assembly

Biomaterials. 2019 Jan;190-191:121-132. doi: 10.1016/j.biomaterials.2018.10.043. Epub 2018 Oct 30.

Abstract

The abnormal aggregation of β-amyloid (Aβ) peptides is a hallmark of Alzheimer's disease (AD) that affects more than 10% of the people over the age 60 world-wide. While the exact mechanism of neuronal loss and cognitive decline has not been elucidated yet, the amyloid hypothesis about the causative role of Aβ aggregation in AD pathology has been widely supported by the numerous in vivo and in vitro data. In this respect, many efforts have been made to explore therapeutic agents that can modulate the aggregation of Aβ, but none of the efforts succeeded in producing effective anti-Aβ drugs for treating AD. This article provides an overview of recent attempts that have employed light energy to intervene with the self-assembly process of Aβ peptides via the generation of oxidative stress by photosensitizers, such as natural or synthetic dyes, light-responsive nanomaterials, and photoelectrochemical platforms. The underlying mechanism of photodynamic reactions suppressing Aβ aggregation and the dilemma in generating long-been-blamed oxidative stress are discussed by addressing the positive role of oxidative stress produced by the photosensitizers in the light-induced suppression of Aβ-mediated neurotoxicity. We have summarized current challenges and strategies to advance photo-induced inhibition and modulation of Aβ aggregation as a therapeutic option for treating AD in the future.

Keywords: Alzheimer's disease; Peptide self-assembly; Photodynamic reactions; Photosensitizers; β-amyloid.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alzheimer Disease / drug therapy*
  • Alzheimer Disease / metabolism
  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Humans
  • Oxidative Stress / drug effects
  • Photochemotherapy / methods
  • Photosensitizing Agents / pharmacology*
  • Photosensitizing Agents / therapeutic use
  • Protein Aggregates / drug effects

Substances

  • Amyloid beta-Peptides
  • Photosensitizing Agents
  • Protein Aggregates