Conformational mapping of amyloid peptides from the putative neurotoxic 25-35 region.
The secondary structure of amyloid beta A(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 beta A(25-35)NH2 has a preferred beta-sheet conformation. Contrary to this beta A(31-35)NH2 tends to adopt a beta-turn conformation. Based on the comparable neurotoxic effect of beta A(25-35)NH2 and beta A(31-35)NH2 the neurotoxicity likely involves the same 31-35 core sequence and the "biologically active conformation" is a beta-turn rather than a beta-sheet structure.
Laczkó
I
I
Institute of Biophysics, Biological Research Center, Szeged, Hungary.
Holly
S
S
Kónya
Z
Z
Soós
K
K
Varga
J L
JL
Hollósi
M
M
Penke
B
B
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000633:toxicity; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D009420:Nervous System / Q000187:drug effects; D010446:Peptide Fragments / Q000737:chemistry* / Q000633:toxicity; D010449:Peptide Mapping; D017433:Protein Structure, Secondary; D017384:Sequence Deletion; D017550:Spectroscopy, Fourier Transform Infrared
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C074636:amyloid beta-protein (25-35)