Aggregation of Aβ(1-42) in the presence of short peptides: Conformational studies

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Abstract

CD and infrared spectroscopic studies were performed on (i) the inhibitory effects of equimolar quantities of LPFFD-OH and LPYFD-NH2 on the time-dependent aggregation of amyloid β-protein (Aβ) (1-42) and (ii) the β-sheet-breaker effects of two-fold molar excess of the pentapeptides on aggregated Aβ(1-42) aged 1 week. The data obtained from the time-dependent studies demonstrated that LPFFD-OH did not significantly influence, whereas LPYFD-NH2 exerted some inhibitory effect on the aggregation of Aβ(1-42). When added to a solution of Aβ(1-42) aged 1 week, LPFFD-OH accelerated, while LPYFD-NH2 delayed, but did not prevent further fibrillogenesis. The difference in the effects of these two pentapeptides on the aggregational profile of Aβ(1-42) is probably due to the difference in their conformational preferences: LPFFD-OH adopts a β-turn and extended structures, while LPYFD-NH2 adopts a prevailing β-turn conformation.

Original languageEnglish
Pages (from-to)731-741
Number of pages11
JournalJournal of Peptide Science
Volume14
Issue number6
DOIs
Publication statusPublished - Jun 1 2008

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Keywords

  • Alzheimer's disease
  • Circular dichroism
  • Fibrillogenesis
  • Infrared spectroscopy
  • Inhibitory pentapeptides
  • β-amyloid

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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