New Perspectives in Reducing Amyloid Aggregation and Toxicity

Marina Chemerovski-Glikman, Michal Richman, Shai Rahimipour

Research output: Contribution to journalReview articlepeer-review

2 Scopus citations


One of the fundamental biochemical characteristics of Alzheimer′s Disease (AD) is the intercellular accumulation of amyloid beta (Aβ) peptide plaques in the brain. Although there is not yet a cure for AD, major efforts have been made to identify antiamyloidogenic agents and therapeutic strategies to treat this disease and related conditions. Our group focuses on inhibiting the aggregation and toxicity of Aβ using two distinct approaches. The first involves covalently attaching the sequence-derived core amyloidogenic amino acid fragment KLVFF to the surfaces of serum albumin microspheres. These particles bind soluble Aβ with high affinity, inhibit its aggregation, reduce its toxicity, and decrease the inflammation induced by its aggregates. Microsphere-bound Aβ stimulates microglia and is phagocytosed via a different mechanism from that used for Aβ removal, so enabling its clearance even by defective cells. Our second approach utilizes self-assembled cyclic D,L-α-peptides as conformational mimics of the amyloid fibril architecture that inhibit the aggregation and cytotoxicity of Aβ. Here, we review these strategies and their mechanisms of action.

Original languageEnglish
Pages (from-to)735-748
Number of pages14
JournalIsrael Journal of Chemistry
Issue number6
StatePublished - 1 Jun 2015

Bibliographical note

Publisher Copyright:
© 2015 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.


  • Alzheimer's disease
  • amyloid beta-peptides
  • conformational mimics
  • proteinaceous microspheres
  • self-assembly


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