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

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 2008

Fingerprint

Agglomeration
Serum Amyloid A Protein
Peptides
Conformations
Infrared radiation

Keywords

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

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Aggregation of Aβ(1-42) in the presence of short peptides : Conformational studies. / Laczkó, I.; Vass, E.; Soós, K.; Fülöp, L.; Zarándi, Márta; Penke, B.

In: Journal of Peptide Science, Vol. 14, No. 6, 06.2008, p. 731-741.

Research output: Contribution to journalArticle

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