Conformational mapping of amyloid peptides from the putative neurotoxic 25-35 region

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The secondary structure of amyloid βA(25-35) and its deletion analogues was studied by circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy and molecular dynamics calculation. Data of our comparative CD and FTIR measurements in trifluoroethanol suggest that βA(25-35)NH2 has a preferred β-sheet conformation. Contrary to this βA(31-35)NH2 tends to adopt a β-turn conformation. Based on the comparable neurotoxic effect of βA(25-35)NH2 and βA(31-35)NH2 the neurotoxicity likely involves the same 31-35 core sequence and the "biologically active conformation" is a β-turn rather than a β-sheet structure.

Original languageEnglish
Pages (from-to)120-126
Number of pages7
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - Nov 30 1994


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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