Surface-modified protein microspheres capture amyloid-β and inhibit its aggregation and toxicity

Michal Richman, Sarah Wilk, Natalia Skirtenko, Alex Perelman, Shai Rahimipour

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


The biocompatible and biodegradable properties of protein microspheres and the recent advances in their preparation have generated considerable interest of utilizing these core-shell structures for drug delivery and diagnostic applications. However, effective targeting of protein microspheres to desirable cells or loci still remains a challenge. Here, we describe for the first time a facile one-pot sonochemical approach for covalent modification of protein microspheres made from serum albumin; the surface of which is covalently decorated with a short recognition peptide to target amyloid-β (Aβ) as the main pathogenic protein in Alzheimer's disease (AD). The microspheres were characterized for their morphology, size, and entrapment efficacy by electron microscopy, dynamic light scattering and confocal microscopy. Fluorescence-activated cell-sorting analysis and Thioflavin-T binding assay demonstrated that the conjugated microspheres bind with high affinity and selectivity to Aβ, sequester it from the medium and reduce its aggregation. Upon incubation with Aβ, the microspheres induced formation of amorphous aggregates on their surface with no apparent fibrillar structure. Moreover, the microspheres directly reduced the Aβ-induced toxicity toward neuron like PC12 cells. The conjugated microspheres are smaller than unmodified microspheres and remained stable throughout the incubation under physiological conditions.

Original languageEnglish
Pages (from-to)11171-11177
Number of pages7
JournalChemistry - A European Journal
Issue number40
StatePublished - 26 Sep 2011


  • amyloid-beta peptides
  • drug delivery
  • multivalent interactions
  • protein microspheres
  • sonochemistry


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