β-Amyloid-derived pentapeptide RIIGL a inhibits Aβ 1-42 aggregation and toxicity

Lívia Fülöp, Márta Zarándi, Zsolt Datki, Katalin Soós, Botond Penke

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Pr-IIGL a, a derivative of the tetrapeptide β-amyloid 31-34 (Aβ 31-34), exerts controversial effects: it is toxic in a neuroblastoma culture, but it protects glial cells from the cytotoxic action of Aβ 1-42. For an understanding of this phenomenon, a new pentapeptide, RIIGL a was synthetized, and both compounds were studied by different physicochemical and biological methods. Transmission electron microscopic (TEM) studies revealed that Pr-IIGL a forms fibrillar aggregates, whereas RIIGL a does not form fibrils. Congo red binding studies furnished the same results. Aggregated Pr-IIGL a acts as a cytotoxic agent in neuroblastoma cultures, but RIIGL a does not display inherent toxicity. RIIGL a co-incubated with Aβ 1-42 inhibits the formation of mature amyloid fibres (TEM studies) and reduces the cytotoxic effect of fibrillar Aβ 1-42. These results indicate that RIIGL a is an effective inhibitor of both the aggregation and the toxic effects of Aβ 1-42 and can serve as a lead compound for the design of novel neuroprotective peptidomimetics.

Original languageEnglish
Pages (from-to)64-69
Number of pages6
JournalBiochemical and biophysical research communications
Volume324
Issue number1
DOIs
Publication statusPublished - Nov 5 2004

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Keywords

  • Aggregation inhibitor
  • Alzheimer's disease
  • Amyloid aggregation
  • Toxic aggregates
  • Transmission electron microscopy
  • β-Amyloid 31-34

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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