Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern.
The molecular basis of fibril formation in Alzheimers disease was explored by electron micrographic and x-ray diffraction analysis of a series of synthetic peptides corresponding to portions of the amino acid sequence of beta protein and that of its putative precursor. A minimum 14 residue peptide was identified that formed typical amyloid fibrils under physiological conditions. Of these 14 residues, 10 were sufficient to give an identical 4.76 A and 10.6 A diffraction pattern as that recently described for isolated neurofibrillary tangles, amyloid plaque cores and leptomeningeal amyloid fibrils.
Gorevic
P D
PD
Castano
E M
EM
Sarma
R
R
Frangione
B
B
D000544:Alzheimer Disease / Q000473:pathology*; D000595:Amino Acid Sequence; D000682:Amyloid; D016229:Amyloid beta-Peptides; D006801:Humans; D008854:Microscopy, Electron; D009419:Nerve Tissue Proteins; D009454:Neurofibrils / Q000473:pathology*; D010446:Peptide Fragments; D011498:Protein Precursors; D014961:X-Ray Diffraction
D000682:Amyloid; D016229:Amyloid beta-Peptides; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011498:Protein Precursors