Compilation and Analysis of Enzymes, Engineered Antibodies, and Nanoparticles Designed to Interfere with Amyloid-β Aggregation

Jun Zhao, Buyong Ma, Ruth Nussinov

Research output: Contribution to journalReview articlepeer-review

Abstract

The abnormal accumulation and aggregation of amyloid β (Aβ) is one of the key factors of the synaptic impairment in Alzheimer's disease. Biomolecules, e.g., apolipoproteins, and membrane receptors, are implicated in the aggregation and toxicity of Aβ. Engineered molecules, such as enzymes, antibodies, and nanoparticles, are designed to interfere with these processes. We compile structural information on these molecules and their essential roles in the complex processes of aggregation, disaggregation, degradation, clearance, and inhibition of Aβ. The interactions between Aβ and its partners have no obvious emerging commonalities. One exception is the recognition of the N-terminal region of Aβ peptides by antibody heavy and light chains, which are facilitated by cooperative interaction not observed in other Aβ-peptide molecules. Overall, the emerging picture charts a diverse, to date unexplored, landscape and serves as the first-of-its-kind partner- and scenario-specific analysis.

Original languageEnglish
Pages (from-to)622-633
Number of pages12
JournalIsrael Journal of Chemistry
Volume57
Issue number7
DOIs
StatePublished - Jul 2017

Keywords

  • Alzheimer's disease therapies
  • amyloid beta-peptides
  • amyloid β-interacting partners
  • antibodies
  • monoclonal antibody

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